Interleukin-18 muteins and single domain il-18BP antibodies and uses thereof

Abstract

The disclosure provides variant human IL- 18 proteins, anti-IL-18BP binding proteins, and corresponding fusion proteins. In one embodiment, a variant human IL- 18 (interleukin- 18) protein, comprises a modification at one or more amino acid positions selected from the group consisting of L9, Vll, N14, C38. 149, V62, C68, C76, K79, F101, SI 17, SI 19, ¥120, ¥123, C127, Q154, and E156, as compared to wildtype human IL 18. In one embodiment, a single domain anti-IL-18BP (interleukin- 18 binding protein) antibody comprises a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 1-50, the CDR- H2 has an amino acid sequence at least 90% identical to SEQ ID NO: 51-100. and the CDR-H3 has an amino acid sequence at least 90% identical to SEQ ID NO: 101-150, wherein the numbering is according to Rabat.

Description

Docket No. WRENCH-001 / WO01 INTERLEUKIN-18 MUTEINS AND SINGLE DOMAIN IL-18BP ANTIBODIES AND USES THEREOF CROSS-REFERENCING This application claims the benefit of U.S. provisional application serial no.63 / 655,162, filed on June 3, 2024, and U.S. provisional application serial no. 63 / 765,198, filed on February 28, 2025, the contents of which are hereby incorporated by reference in their entirety. SEQUENCE LISTING The present application is accompanied by a sequence listing submitted as an electronically filed XML document entitled “2025-06-02 WRENCH-001-WO01 Sequence Listing.xml”, created on June 2, 2025, and having a size of 484 KB. The content of this sequence listing is hereby incorporated by reference in its entirety. BACKGROUND Cancer immunotherapy utilizes the immune system of a subject to fight the patient’s cancer. This is achieved by stimulating the patient’s immune system so that it recognizes and destroys tumors or other cancerous tissue. One method of activating the immune system to attack cancer cells in the body of a subject is via cytokines. Cytokines are proteins produced in the body that are important in cell signaling and in modulating the immune system. Some cytokine therapy utilizes these properties of cytokines to enhance the immune system of a subject to kill cancer cells. Human interleukin-18 (hIL-18), initially cloned as an IFN-g- inducing factor secreted by macrophages or Kupffer cells, strongly augments the production of IFN-g both in natural killer cells and T cells, having a key role in many inflammatory diseases including allergy and autoimmune diseases. IL-18 exerts its activity upon binding to the IL-18 receptor IL18R1 (SEQ ID NO: 553) and the IL-18 receptor accessory protein (IL18RAP) (SEQ ID NO: 554) to form a ternary signaling complex which activates NF-kappa-B, and in turn activates synthesis of inflammatory mediators. IL-18 signaling contributes to cytokine production and immune response by Th1 and Th2 lymphocytes. The activity of IL-18 can be suppressed by the IL-18 binding protein (IL-18BP) which binds to IL-18 and prevents it from binding to the IL-18 receptor. Thus, there is a need for novel approaches to prevent the inhibition of endogenous IL-18 by IL-18BP in order to unleash the full anti-tumor potential of IL-18. In addition, recombinant IL-18 has been examined for treatment of cancer including clinical trials in humans. Concerns about intertrial consistency raised the necessity for a more stable IL-18. BRIEF SUMMARY The present disclosure provides compositions and methods related to IL-18 mutant proteins; anti-IL- 18BP binding proteins, antibodies or antigen binding fragments; multispecific binding proteins; and fusion proteins. Variant IL-18 proteins and variant IL-18 fusion proteins with improved thermostability, half-life, and function as described herein can be administered in vivo, resulting in functional levels of IL-18 despite natural inhibition by IL-18BP. Anti-IL-18BP binding proteins as described herein can prevent IL-18BP from interacting with and down-regulating IL-18 with novel anti-IL-18BP binding proteins and anti-IL-18BP fusion proteins, which may remove IL-18BP from circulation or otherwise prevent the interaction of IL-18 with IL-18BP (e.g.,Docket No. WRENCH-001 / WO01 by disassociating bound IL-18 from IL-18BP). Further, such IL-18 variants and IL-18BP binding proteins can be administered simultaneously, e.g., by co-administration of an IL-18 variant / IL-18 variant fused to an Fc with an anti-IL-18BP binding protein, yielding synergistic effects. In one embodiment, a variant human IL-18 protein is provided. In some embodiments, the variant human IL-18 protein comprises a modification at one or more amino acid positions selected from the group consisting of L9, V11, N14, C38, I49, V62, C68, C76, K79, F101, S117, S119, Y120, Y123, C127, Q154, and E156, as compared to wildtype human IL-18. In some embodiments, the variant human IL-18 protein comprises an additional 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid modifications. In some embodiments, the variant IL-18 protein comprises a modification at one or more amino acid positions selected from the group consisting of L9, E156, K79, Y120, S117, and S119, as compared to wildtype human IL-18. In some embodiments, the variant IL-18 protein comprises amino acid substitutions selected from the group consisting of: L9 / E156, V11 / Q154, I49 / V62, V62 / F101, K79 / Y120, K79 / Y123, S117, S119, and N14. In some embodiments, the variant IL-18 protein further comprises amino acid substitutions at residues C38 and / or C68, as compared to wildtype human IL-18. In some embodiments, the variant IL-18 protein further comprises an amino acid substitution at residue C127, as compared to wildtype human IL-18. In some embodiments, the variant IL-18 protein further comprises an amino acid substitution resulting in a cysteine residue, wherein that cysteine residue forms a disulfide bond with C76 or C127. In some embodiments, the amino acid substitution resulting in a cysteine residue comprises S117C or S119C, wherein that cysteine residue forms a disulfide bond with C76. In some embodiments, the amino acid substitution resulting in a cysteine residue comprises N14C, wherein that C forms a disulfide bond with C127. In some embodiments, the amino acid substitution resulting in a cysteine is positioned within 3, 2, or 1 angstroms of C76 or C127. In some embodiments, the variant IL-18 protein comprises amino acid substitutions at residues C38, C68, C76, and C127. In some embodiments, the variant human IL-18 protein has improved thermostability compared to wildtype human IL-18. In some embodiments, the variant human IL-18 protein has a melting temperature of at least 50C. In some embodiments, the variant human IL-18 protein has a melting temperature of at least 60C. In some embodiments, the variant human IL-18 protein has a melting temperature of at least 70C. In some embodiments, the variant human IL-18 protein has an improved ability to activate IL-18 receptor-mediated signaling, as compared to wildtype human IL-18. In some embodiments, the variant human IL-18 protein exhibits improved production yield compared to wildtype human IL-18. In some embodiments, the modification at one or more amino acid positions comprises a substitution resulting in a cysteine residue. In some embodiments, the cysteine residue forms a disulfide bond within the variant human IL-18 protein, thereby improving thermostability. In some embodiments, the variant human IL- 18 protein exhibits increased activation of the IL-18 receptor-mediated signaling compared to wildtype IL-18, optionally wherein the variant IL-18 protein comprises an amino acid substitution of S117C. In some embodiments, the variant human IL-18 protein exhibits decreased activation of the IL-18 receptor-mediatedDocket No. WRENCH-001 / WO01 signaling compared to wildtype IL-18, optionally wherein the variant IL-18 protein comprises an amino acid substitution N14C. In some embodiments, a pharmaceutical composition comprises the variant human IL-18 protein and a pharmaceutically acceptable carrier is provided. In some embodiments, a nucleic acid encodes the variant human IL-18 protein is provided. In some embodiments, an expression vector comprising the nucleic acid is provided. In some embodiments, a host cell comprising the nucleic acid or the expression vector is provided. In some embodiments, a method of making a variant human IL-18 protein comprises culturing the host cell and recovering the variant human IL-18 protein from the cell culture. In one embodiment, a single domain anti-IL-18BP (interleukin-18 binding protein) antibody is provided. In some embodiments, the single domain anti-IL-18BP antibody comprises a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 1-50, the CDR-H2 has an amino acid sequence at least 90% identical to SEQ ID NO: 51-100, and the CDR-H3 has an amino acid sequence at least 90% identical to SEQ ID NO: 101-150, wherein the numbering is according to Kabat. In some embodiments, the CDR-H1 is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 1-50, the CDR-H2 is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 51-100, and the CDR-H3 is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 101-150, wherein the numbering is according to Kabat. In some embodiments, the single domain anti-IL-18BP antibody is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 500- 549. In one embodiment, a single domain anti-IL18BP antibody, comprises a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 16, the CDR-H2 has an amino acid sequence of A- I-X1-X2-X3-X4-G-X5-T-Y-Y, wherein X1 is Y, H, D, N, P, or R; X2 is K, E, N, Q, T, P, or R; X3 is D, A, G, H, N, or V; X4 is G, A, D, P, R, or V; and X5 is K, Q, E, N, R, or T; and the CDR-H3 has an amino acid sequence of S-A-W-G-Z1-Z2-Z3-Z4-P-Z5-Z6-Z7-Z8-W, wherein Z1=K, R, or I; Z2 is S, A, Q, T, L, or E; Z3 is I, T, L, V, N, or Y; Z4 is V, D, G, H, A, N, or R; Z5 is H, N, R, L, or S; Z6 is F or Y; and Z7=Y, H, N, S, A, or D; wherein the numbering is according to Kabat. In one embodiment, a single domain anti-IL18BP antibody comprises a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 9, the CDR-H2 has an amino acid sequence of any one of SEQ ID Nos: 59-65 or 99-100, and the CDR-H3 has an amino acid sequence of A-R-P-Z1-Z2-H-Z3-P- Z4-Z5-Z6-I-Y-P-Z7-W, wherein Z1 is T, R, H, S, A, or P; Z2 is K or R; Z3 is V, L, I, or R; Z4 is H or N; Z5 is R, E, A, K, F, T, G, L, or I; Z6 is N, R, or S; and Z7 is R, L, or H; wherein the numbering is according to Kabat. In some embodiments, a single domain anti-IL-18BP antibody is provided, wherein the antibody dissociates from IL-18BP within the acidic environment of endosomes, thereby resulting in increased clearance of IL-18BP.Docket No. WRENCH-001 / WO01 In some embodiments, the single domain anti-IL-18-BP antibody dissociates from IL-18BP within the acidic environment of endosomes, thereby resulting in increased clearance of IL-18BP.In some embodiments, the binding affinity of the IL-18BP antibody for IL-18BP is pH-sensitive. In some embodiments, the single domain anti-IL-18BP antibody has a decreased binding affinity for IL-18BP at a pH of 5.8, compared to a pH of 6.5-7.4. In some embodiments, the binding affinity of the anti-IL-18BP antibody for IL-18BP is 10-fold, 20- fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, or 100-fold less at a pH of 5.0-5.8, compared to the binding affinity at a pH of 6.5-7.4. In some embodiments, the binding affinity of the single domain anti- IL-18BP antibody for IL-18BP is 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, or 100-fold less at a pH of 5.8 or lower, as compared to the binding affinity at a pH of 7.4 or above. In some embodiments, the single domain anti-IL-18BP antibody exhibits a binding affinity or KD of less than 50 nM, 40 nM, 30 nM, 20nM, 10nM, 5nM, 1nM, or 100pM at pH 6.5 – 7.4. In some embodiments, the single domain anti-IL-18BP antibody prevents the interaction of IL-18BP with IL-18. In some embodiments, the single domain anti-IL-18BP antibody does not interfere with IL-18 binding to IL-18 receptors, thereby enabling the activity of endogenous IL-18. In some embodiments, the IL- 18 receptors are located on effector T cells or NK cells, thereby enabling the activity of endogenous IL-18. In some embodiments, the single domain anti-IL-18BP antibody restores IL-18-mediated signaling that was inhibited by the interaction of IL-18 and IL-18BP. In some embodiments, the single domain anti-IL-18BP antibody antagonizes at least one immune inhibitory effect of IL-18BP. In some embodiments, the single domain anti-IL-18BP the antibody blocks the IL-18 : IL-18BP binding interaction. In some embodiments, the single domain anti-IL-18BP antibody competes for binding with an antibody that binds to human IL-18BP of SEQ ID NO: 555 and / or the secreted chain of human IL-18BP of SEQ ID NO: 556 and or that competes for binding to IL-18. In some embodiments, the single domain anti-IL-18BP antibody is non-naturally occurring. In some embodiments, the single domain anti-IL18-BP antibody blocks endogenous IL-18BP produced by peripheral blood mononuclear cells. In some embodiments, the single domain anti-IL-18BP antibody inhibits tumor growth in a mouse tumor model. In some embodiments, the single domain anti-IL18-BP antibody does not have any treatment-induced toxicity when administered to a mouse tumor model. In some embodiments, the single domain anti-IL-18BP antibody is useful for treating a hepatocellular carcinoma, a lung adenocarcinoma, or an ovarian cancer. In some embodiments, the anti-IL-18BP antibody comprises a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR- H1 has an amino acid sequence at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 9-15 or 49- 50, the CDR-H2 has an amino acid sequence at least 90% identical to SEQ ID NO: 59-65 or 99-100, and the CDR-H3 has an amino acid sequence at least 90% identical to SEQ ID NO: 109-115 or 149-150, wherein the numbering is according to Kabat. In some embodiments, the single domain anti-IL-18BP antibody further comprises a Fc domain. In some embodiments, the single domain anti-IL-18BP antibody further comprises a half-life extension domain. In some embodiments, the half-life extension domain comprises an albumin-targeting polypeptide.Docket No. WRENCH-001 / WO01 In some embodiments, a pharmaceutical composition comprises the single domain anti-IL-18BP antibody and a pharmaceutically acceptable carrier is provided. In some embodiments, a nucleic acid that encodes the single domain anti-IL-18BP antibody is provided. In some embodiments, an expression vector comprising the nucleic acid is provided. In some embodiments, a host cell comprising the nucleic acid or the expression vector is provided. In some embodiments, a method of making a single domain anti-IL-18BP antibody comprises culturing the host cell and recovering the single domain anti-IL-18BP antibody from the cell culture. In some embodiments, a pharmaceutical composition comprising (a) a variant IL-18 protein, and (b) a single domain anti-IL-18BP antibody is provided. In one embodiment, a multispecific binding protein is provided. In some embodiments, the multispecific binding protein comprises a first domain and a second domain, wherein the first domain comprises a variant human IL-18 protein, and the second domain comprises a single domain anti-IL-18BP antibody. In another embodiment, a multispecific binding protein comprises a first domain and a second domain, wherein the first domain comprises a single-domain anti-IL-18BP antibody, and the second domain binds to a target molecule that is not IL-18BP. In some embodiments, the second domain selectively binds to a tumor associated antigen (TAA). In some embodiments, the TAA is selected from the group consisting of B-cell maturation antigen (BCMA), carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (Her2), epithelial cell adhesion molecule (EpCAM), CD20, CD26, CD123, CD30, CD33, CD47, CD52, CD133, glycoprotein A33 (gpA33), mucins, tumor associated glycoprotein-72 (TAG-72), type IX collagen (CIX), glutamate carboxypeptidase II (PSMA), folate-binding protein, GD2, GD3, GM2, vascular endothelial growth factor (VEGF), vascular endothelial growth factor receptor (VEGFR), integrin, αVβ3, α5β1, ERBB2, ERBB3, mesenchymal epithelial transition (MET), insulin-like growth factor-I receptor (IGFIR), ephrin type-A receptor 3 (EPHA3), TRAIL receptor 1 (TRAILR1), TRAIL receptor 2 (TRAILR2), receptor activator of nuclear factor kappa beta (RANKL), fibroblast activation protein (FAP), claudin 18.2, mesothelin, receptor tyrosine kinase like orphan receptor 1 (ROR1), epidermal growth factor receptor variant III (EGFRVIII), six-transmembrane epithelial antigen of the prostate-2 (STEAP2), orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), and tenascin. In some embodiments, the first domain and the second domain are coupled via chemical coupling, gene fusion, or a non-covalent association. In some embodiments, the multispecific binding protein further comprises a linker. In some embodiments, the linker comprises a glycine-serine linker. In some embodiments, the glycine-serine linker comprises a sequence of (GS)n, wherein n = 1 to 10. In some embodiments, the linker comprises (GS)n, (GGS)n, (GGGS)n, (GGSG)n, (GGSGG)n, (GGGGS)n, (GGGGG)n, or (GGG)n, wherein n = 1 to 10. In some embodiments, the linker comprises (GGGGS)4 or (GGGGS)3.Docket No. WRENCH-001 / WO01 In some embodiments, the multispecific binding protein is a bispecific protein. In some embodiments, the multispecific binding protein is a trispecific protein. In some embodiments, the multispecific binding protein binds to four different target molecules. In some embodiments, the multispecific binding protein is non- naturally occurring. In some embodiments, the multispecific binding protein further comprises a Fc domain. In some embodiments, the multispecific binding protein further comprises a half-life extension domain. In some embodiments, the half-life extension domain comprises an albumin-targeting polypeptide. In some embodiments, the first Fc domain is a wild type Fc. In some embodiments, the first Fc domain has amino acid substitutions M428L and N434A, compared to wild type Fc. In some embodiments, the first Fc domain has amino acid substitutions T307E, M428L, and N434A, compared to wild type Fc. In some embodiments, the VHH-Fc fusion protein has an increased thermostability compared to a VHH-Fc fusion protein with a wild type Fc. In some embodiments, a pharmaceutical composition comprises the multispecific binding protein and a pharmaceutically acceptable carrier is provided. In some embodiments, a nucleic acid that encodes the multispecific binding protein is provided. In some embodiments, an expression vector comprising the nucleic acid is provided. In some embodiments, a host cell comprising the nucleic acid or the expression vector is provided. In some embodiments, a method of making a multispecific binding protein comprises culturing the host cell and recovering the multispecific binding protein from the cell culture. In one embodiment, a fusion protein is provided. In one embodiment, the fusion protein is a variant human IL-18-Fc fusion protein comprising (a) a first monomer comprising from N-terminus to C-terminus: a variant human IL-18 protein and a first Fc domain, and (b) a second monomer comprising a second Fc domain. In one embodiment, the fusion protein is a VHH-Fc fusion protein comprising (a) a first monomer comprising from N-terminus to C-terminus: a single domain anti-IL-18BP antibody and a first Fc domain, and (b) a second monomer comprising a second Fc domain. In one embodiment, the fusion protein is an Fc fusion protein comprising (a) a first monomer comprising one or more single domain anti-IL-18BP antibodies and a first Fc domain, and (b) a second monomer comprising a second Fc domain. In some embodiments, the second monomer further comprises one or more variant human IL-18 proteins. In some embodiments, the second monomer further comprises one or more single domain anti-IL- 18BP antibodies. In some embodiments, the first monomer comprises two single domain anti-IL-18BP antibodies. In some embodiments, the second monomer comprises two single domain anti-IL-18BP antibodies. In some embodiments, the first monomer comprises, from N-terminus to C-terminus: a first single domain anti- IL-18BP antibody, a first Fc domain, and a second single domain anti-IL-18BP antibody. In one embodiment, an Fc fusion protein is provided. In one embodiment, the Fc fusion protein comprises (a) a first monomer comprising two single domain anti-IL-18BP antibodies and a first Fc domain, and (b) a second monomer comprising a single domain anti-IL-18BP antibody, a variant human IL-18 protein, and a second Fc domain.Docket No. WRENCH-001 / WO01 In one embodiment, a variant IL-18 x Fab-Fc fusion protein is provided. In one embodiment, the variant IL-18 x Fab-Fc fusion protein comprises (a) a first monomer comprising from N-terminus to C-terminus: a variable heavy (VH) chain and a first Fc domain, (b) a second monomer comprising from N-terminus to C- terminus: a variant human IL-18 protein and a second Fc domain, and (c) a third monomer comprising a variable light (VL) chain, wherein the VH and VL form an antigen binding fragment (Fab). In one embodiment, a VHH x Fab-Fc fusion protein is provided. In one embodiment, the VHH x Fab-Fc fusion protein comprises (a) a first monomer comprising from N-terminus to C-terminus: a variable heavy (VH) chain and a first Fc domain, (b) a second monomer comprising from N-terminus to C-terminus: a single domain anti-IL-18BP antibody and a second Fc domain, and (c) a third monomer comprising a variable light (VL) chain, wherein the VH and VL form an antigen binding fragment (Fab). In some embodiments, the Fab selectively binds to a tumor-associated antigen (TAA). In some embodiments, the Fab selectively binds to an immune checkpoint selected from the list consisting of Cytotoxic T-lymphocyte-associated protein 4 (CTLA-4), Programmed cell death protein 1 (PD-1), Programmed death- ligand 1 (PD-L1), Lymphocyte-activation gene 3 (LAG-3), T cell immunoglobulin and mucin-domain containing-3 (TIM-3), T cell immunoglobulin and ITIM domain (TIGIT), and V-domain Ig suppressor of T cell activation (VISTA). In some embodiments, the TAA is selected from the group consisting of B-cell maturation antigen (BCMA), carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (Her2), epithelial cell adhesion molecule (EpCAM), CD20, CD26, CD123, CD30, CD33, CD47, CD52, CD133, glycoprotein A33 (gpA33), mucins, tumor associated glycoprotein-72 (TAG-72), type IX collagen (CIX), glutamate carboxypeptidase II (PSMA), folate-binding protein, GD2, GD3, GM2, vascular endothelial growth factor (VEGF), vascular endothelial growth factor receptor (VEGFR), integrin, αVβ3, α5β1, ERBB2, ERBB3, mesenchymal epithelial transition (MET), insulin-like growth factor-I receptor (IGFIR), ephrin type-A receptor 3 (EPHA3), TRAIL receptor 1 (TRAILR1), TRAIL receptor 2 (TRAILR2), receptor activator of nuclear factor kappa beta (RANKL), fibroblast activation protein (FAP), claudin 18.2, mesothelin, receptor tyrosine kinase like orphan receptor 1 (ROR1), epidermal growth factor receptor variant III (EGFRVIII), six-transmembrane epithelial antigen of the prostate-2 (STEAP2), orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), and tenascin. In some embodiments, the fusion protein has a melting temperature of at least 50C. In some embodiments, the fusion protein has a melting temperature of at least 60C. In some embodiments, the fusion protein has a melting temperature of at least 70C. In some embodiments, the fusion protein prevents the interaction of IL-18BP with IL-18. In some embodiments, the fusion protein increases the activity of endogenous IL-18. In some embodiments, the fusion protein restores IL-18-mediated signaling that was inhibited by the interaction of IL-18 and IL-18BP. In some embodiments, the fusion protein antagonizes at least one immune inhibitory effect of IL-18BP. In some embodiments, the fusion protein blocks the IL-18 : IL-18BP binding interaction. In some embodiments, theDocket No. WRENCH-001 / WO01 fusion protein releases IL-18BP within the acidic environment of endosomes, thereby resulting in an increased clearance of IL-18BP. In some embodiments, the first Fc domain and second Fc domain are configured in an asymmetrical manner. In some embodiments, the first domain and the second domain comprise complementary pairs of amino acid substitutions that improve thermostability. In some embodiments, the first Fc domain comprises a set of amino acid substitutions selected from the group consisting of S354C and T366W. In some embodiments, the second Fc domain comprises a set of amino acid substitutions selected from the group consisting of Y349C, T366S, L368A, and Y407V. In some embodiments, the variant IL-18 protein and / or single domain anti-IL-18BP antibody are covalently attached to the N-terminus or the C-terminus of the first or the second Fc domain. In some embodiments, the variant IL-18 protein and / or single domain anti-IL-18BP antibody are covalently attached to the N-terminus or the C-terminus of the first or the second Fc domain. the variant IL-18 protein and / or single domain anti-IL-18BP antibody are covalently attached to the N-terminus or the C-terminus of the first or the second Fc domain via a linker. In some embodiments, the linker comprises a glycine-serine linker. In some embodiments, the glycine-serine linker comprises a sequence of (GS)n, wherein n = 1 to 10. In some embodiments, the linker comprises (GS)n, (GGS)n, (GGGS)n, (GGSG)n, (GGSGG)n, (GGGGS)n, (GGGGG)n, or (GGG)n, wherein n = 1 to 10. In some embodiments, the linker comprises (GGGGS)4 or (GGGGS)3. In some embodiments, a pharmaceutical composition comprises the fusion protein and a pharmaceutically acceptable carrier is provided. In some embodiments, a nucleic acid that encodes the fusion protein is provided. In some embodiments, an expression vector comprising the nucleic acid is provided. In some embodiments, a host cell comprising the nucleic acid or the expression vector is provided. In some embodiments, a method of making a fusion protein comprises culturing the host cell and recovering the multispecific binding protein from the cell culture. In one embodiment, a method of treating a disease or condition in a subject in need thereof is provided. In one embodiment, the method comprises administering to the subject a therapeutically effective amount of a variant human IL-18 protein, a single domain anti-IL-18BP antibody of any one of claims, a multispecific binding protein, and / or a fusion protein according to the disclosure. In some embodiments, the disease or condition comprises a cancerous disease, a proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, a graft-versus-host disease or a host-versus-graft disease. In one embodiment, a method of treating cancer in a patient is provided. In one embodiment, the method comprises administering a composition comprising a variant human IL-18 protein, a single domain anti-IL-18BP antibody, a multispecific binding protein, and / or a fusion protein according to the disclosure. In some embodiments, the cancer is selected from the group consisting of renal clear cell carcinoma (RCC), lung cancer, NSCLC, lung adenocarcinoma, lung squamous cell carcinoma, gastric adenocarcinoma, ovarian cancer,Docket No. WRENCH-001 / WO01 endometrial cancer, breast cancer, triple negative breast cancer (TNBC), head and neck tumor, colorectal adenocarcinoma, melanoma, and metastatic melanoma. In some embodiments, the patient experiences an increase in tumor growth inhibition of at least about 10%, 20%, 30% 40% 50% 60% 70% 80% 90%, 100%, 125%, 150%, 175%, 200% 225% 250%, 275%, 300%, 325% 350%, 375%, 400%, 425%, 450%, 475%, 50Q%, 525%, 550%, 575%, 600%, 625%, 650%, 675%, 700%, 725%, 750%, 775%, 800%, 825%, 850%, 875%, 900%, 925%, 950%, 975%, or 1000%, as compared to a control or an untreated patient. In some embodiments, the patient experiences a decrease in tumor growth inhibition of at least about 10%, 20%, 30% 40% 50% 60% 70% 80% 90%, 100%, 125%, 150%, 175%, 200% 225% 250%, 275%, 300%, 325% 350%, 375%, 400%, 425%, 450%, 475%, 50Q%, 525%, 550%, 575%, 600%, 625%, 650%, 675%, 700%, 725%, 750%, 775%, 800%, 825%, 850%, 875%, 900%, 925%, 950%, 975%, or 1000%, as compared to a control or an untreated patient. In one embodiment, a method of reducing a tumor is provided. In one embodiment, the method comprises contacting the tumor with a composition comprising a variant human IL-18 protein, a single domain anti-IL-18BP antibody, a multispecific binding protein, and / or a fusion protein according to the disclosure. In one embodiment, a method of reducing a tumor in a subject in need thereof is provided. In one embodiment, the method comprises administering to the subject a composition comprising a variant human IL- 18 protein, a single domain anti-IL-18BP antibody, a multispecific binding protein, and / or a fusion protein according to the disclosure. In one embodiment, a method of treating a subject having a cancer is provided. The method comprises administering to the subject a composition comprising a variant human IL-18 protein, a single domain anti-IL- 18BP antibody, a multispecific binding protein, and / or a fusion protein according to the disclosure. In some embodiments, the subject or patient is a human subject. BRIEF DESCRIPTION OF THE FIGURES The novel features of the invention are set forth with particularity in the appended claims. A better understanding of the features and advantages of the present disclosure will be obtained by reference to the following detailed description that sets forth illustrative embodiments, in which the principles of the disclosure are utilized, and the accompanying drawings of which: FIG. 1A illustrates the protein sequence of mature human IL-18. The 4 non-paired cysteines are underlined. FIG. 1B is visualization of the crystal structure of IL-18BP (PDB 3WO2) of residues in close proximity, which are candidates for mutations with cysteines to create novel intra-molecular disulfide bonds. FIG. 2A is a cartoon representing the structure of an IL-18 mutein-Fc fusion according to an embodiment of the disclosure; FIG. 2B are images showing the results of SDS-PAGE of the purified IL-18 mutein-Fc fusions; and FIG.2C depicts analytical SEC-HPLC profiles of the purified IL-18 mutein-Fc fusions. FIG. 3 shows the results of an HEK blue reporter assay measuring the activity of the purified IL-18 mutein-Fc fusions and recombinant wild type human IL-18.Docket No. WRENCH-001 / WO01 FIG. 4 is a phylogenetic tree of the sequences of certain VHHs (anti-IL-18BP binders) identified through the screening of the VHH QUINTHETIC LIBRARYTM. FIG.5 is a diagram illustrating the clustering of the CDR3 regions of the VHHs (anti-IL-18BP binders) identified through the screening of the VHH QUINTHETIC LIBRARYTM. FIG. 6 illustrates the detection of the binding of the different anti-IL-18BP binders (VHHs) in the absence or presence of 1 (1) or 10 (10) mg / mL of IL-18. FIG. 7A depicts experimental results showing the determination of the binding parameters of IL-18 and IL-18BP by BLI; FIG.7B depicts experimental results showing the determination of the binding parameters of selected anti-IL-18BP binders (VHHs) and IL-18BP by BLI; and FIG. 7C depicts experimental results showing assessing the competition between IL-18 and selected anti-IL-18BP binders (VHHs) by BLI. FIG.8 is a chart showing the functional validation of selected anti-IL-18BP binders (VHHs) using the HEK blue reporter assay. IL-18-mediated signaling represents the activity of IL-18 that was dissociated from IL-18BP by increasing concentrations of selected anti-IL-18BP binders (VHHs). FIG. 9 is a chart showing an investigation of the pH sensitivity of selected anti-IL-18BP binders (VHHs) detected by ELISA. The binding of anti-IL-18BP binders to IL-18BP was determined by ELISA at pH 7.4, 6.5, and 5.0. FIG. 10 is a chart showing the determination of the EC50 of various anti-IL-18BP antibodies of the disclosure (WB41, WB42, WB43, WB44, WB46, WB47, WB48, WB49) expressed as bivalent Fc fusion proteins by ELISA. FIGS. 11A-C are charts depicting the in vitro efficacy of a bivalent VHH (VHH “H10”) Fc fusion protein. FIG.11A, B: Anti-IL-18BP antibody blocks IL-18BP secreted from peripheral blood mononuclear cells (PBMCs): Thawed PBMCs were cultured for 24 hours with rhIL-12 (10 ng / mL), rhIL-18 (33.3ng / ml) and a dose titration of an anti-IL-18BP antibody (20ug / mL to 0.625 ug / mL; dilution factor of 1:2) or isotype control (20 ug / mL). Anti-IL18BP antibodies were able to induce dose-dependent IFN-g secretion above the IL-12+IL- 18 control levels, indicating that the antibody can block endogenous IL-18BP produced by the PBMCs. FIG. 11C: Isolated human NK cells were were cultured for 24 hours and stimulated with rhIL-12 (10 ng / mL), rhIL- 18 (10ng / ml), in the absence or presence of 80nM IL-18BP, for 30 minutes. Treatment with an anti-IL18BP antibody induced IFN-g secretion above the IL-12+IL-18_IL-18BP levels, indicating that the antibody can block IL-18BP and release IL-18 that can in turn activate NK cells. FIGS. 12A-D are charts depicting the assessment of anti-IL-18BP monotherapy in human PBMC- reconstituted M-NSG mouse xenograft HEP3B (FIG. 12A, B) and NCI-H23 (FIG. 12C, D) tumor models. Dosing of 10 mg / kg every 3 days of the anti-IL-18BP antibody led to a significant tumor growth inhibition. FIG. 12A, C. The anti-IL-18BP antibody did not induce any weight loss compared to the control group, suggesting the absence of treatment-induced toxicity (FIG. B, D). FIGS. 13A-E are diagrams depicting exemplary multifunctional Fc fusion proteins combining anti- IL18BP VHH and recombinant IL-18 variant Fc fusion proteins of the disclosure.Docket No. WRENCH-001 / WO01 FIG. 14A is a chart depicting the assessment of anti-IL-18BP monotherapy in human PBMC- reconstituted M-NSG mouse xenograft HEP3B tumor model. Dosing of 3 mg / kg every 3 days of the anti-IL- 18BP antibody WB216 led to a significant tumor growth inhibition. FIG. 14B is a cartoon that describes the molecules used in the study: WB89 is an IgG4 antibody; WB216 is a bivalent VHH-IgG1 Fc fusion; WB231 is a tetravalent VHH-IgG1 Fc fusion; WB233 is a trivalent VHH-IgG1 Fc fusion, and monovalent IL-18 mutein (corresponding to WB09), fused to the iRGD peptide FIG. 15 is a chart summarizing the quantification of WB89 (an anti-IL18BP IgG4) and WB216 (an anti-IL18BP VHH-Fc fusion protein) concentrations in the serum and tumors, 6 and 24 hours after dosing HEP3B tumor-bearing NSG mice. The VHH-Fc fusion exhibits higher tumor vs serum concentrations ratios indicating higher tumor penetration compared to the IgG4. FIG. 16 are charts depicting the in vitro efficacy of bivalent VHH-Fc fusion proteins. Anti-IL-18BP VHH-Fc fusions block IL-18BP secreted from peripheral blood mononuclear cells (PBMCs): Thawed PBMCs were cultured for 24 hours with rhIL-12 (10 ng / mL), rhIL-18 (33.3ng / ml) and a dose titration of an anti-IL- 18BP antibody (5ug / mL to 0.078125ug / mL; dilution factor of 1:2) or isotype control (5 ug / mL). Anti-IL18BP antibodies were able to induce dose-dependent IFN-g secretion above the IL-12+IL-18 control levels, indicating that the antibody can block endogenous IL-18BP produced by the PBMCs. DETAILED DESCRIPTION I. Overview Interleukin 18 (IL-18) is a pro-inflammatory cytokine that can stimulate T-cells, NK-cells, and myeloid cells. IL-18 has been proposed as an immunotherapeutic agent for the treatment of cancer, given its ability to stimulate anti-tumor immune cells. However, the clinical efficacy of IL-18 has been limited by its sequestration and neutralization by the decoy receptor IL-18BP. As a result, IL-18BP inhibits IL-18-induced T and NK cell activation and proliferation, and pro-inflammatory cytokine production, resulting in reduced T and NK cell activity and T-helper type 1 immune responses. Consequently, there is a need for compositions and methods that restore effective IL-18 signaling activity to treat and prevent cancer and other diseases and disorders. The inventor has recognized and appreciated that restoring effective IL-18 signaling activity can be accomplished in several ways. For example, variant IL-18 proteins and variant IL-18 fusion proteins with improved thermostability, half-life, and function can be administered in vivo, resulting in functional levels of IL-18 despite natural inhibition by IL-18BP. Second, IL-18BP can be prevented from interacting with and down-regulating IL-18 with novel anti-IL-18BP binding proteins and anti-IL-18BP fusion proteins, which may remove IL-18BP from circulation or otherwise prevent the interaction of IL-18 with IL-18BP (e.g., by disassociating bound IL-18 from IL-18BP). Further, such IL-18 variants and IL-18BP binding proteins can be administered simultaneously, by co-administration of an IL-18 variant / IL-18 variant fused to an Fc with an anti-IL-18BP binding protein; alternatively, such IL-18 variants and IL-18BP binding proteins can be administered simultaneously via a Fusion protein that contains one or more molecules of an IL-18 variant and one or more molecules of an anti-IL-18BP binding protein. This fusion protein can be an Fc fusion where theDocket No. WRENCH-001 / WO01 IL-18 variant is fused to the N-terminus or C-terminus of the Fc, and the anti-IL18 binding protein is fused to the N-terminus and / or the C-terminus of the Fc. This could result in a Fc fusion protein, symmetrical or asymmetrical, with at least one IL-18 variant fused to the Fc and at least one IL-18BP binding protein fused to the Fc. Accordingly, provided herein are IL-18 variant proteins and IL-18-Fc fusion proteins where specific residues were mutated based in part on their proximity to certain cysteine residues, resulting in the formation of new disulfide bridges and a more compact structure. Such IL-18 variant proteins have improved thermostability, expression yield, and with the intent to create additional disulfide bridges resulting in a more compact structure. Such mutations were designed to increase the stability, expression yield, and overall utility of the resulting IL-18 variant proteins. Further provided herein are novel IL-18BP binding proteins (such as single domain anti-IL-18BP antibodies) and anti-IL-18BP-Fc fusion proteins, which result in increased levels of circulating IL-18, and are useful for the treatment of disease. This increase is a result of several mechanisms, including but not limited to blocking IL-18BP, preventing the binding of IL-18 to IL-18BP, disassociating IL- 18 from IL-18BP, and augmenting the clearance of IL-18BP. Although most antibodies effectively neutralize their cognate antigens, relatively high doses and / or frequent injections are required to achieve therapeutic efficacy when targeting antigens with high rates of synthesis. Antibodies targeting these antigens show significant antigen-mediated clearance. For many conventional antibodies, each antigen-binding site binds to only one antigen molecule during the antibody’s lifetime in plasma. Because their cognate antigens are usually produced continuously in vivo, the minimum number of antigen-binding sites required to completely neutralize the function of the antigen cannot be less than the amount of antigen that is produced between doses. This restricts the dose and dosing frequency of many therapeutic antibodies. Improvements beyond higher binding affinity or modulation of FcRn binding can only be achieved by increasing the number of cycles in which an antibody binds to and releases the antigen for subsequent lysosomal degradation and thereby increasing the amount of antigen that can be bound by a single antigen-binding site. This can be achieved by providing antibodies that dissociate from their target within the acidic environment of the endosome by decreasing its binding affinity at pH 5.5–6.0, without affecting its binding affinity in plasma at pH 7.4. Accordingly, in some embodiments, an IL-18BP binding protein exhibits a pH-sensitive binding to IL-18BP. In some embodiments, the IL-18BP binding protein exhibits a decreased binding affinity to IL-18BP at pH 6 and below, compared to the binding affinity at pH 6.5 or pH 7.4. In some embodiments, the decreased binding affinity to IL-18BP at pH6 and below compared to pH 7.4 and 6.5 results in a 5-fold, 10-fold, 20-fold, 50-fold, 100-fold up to 1000-fold, decrease in binding affinity (measured, e.g., by the constant of dissociation).Docket No. WRENCH-001 / WO01 II. Definitions All terms are intended to be understood as they would be understood by a person skilled in the art. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which the disclosure pertains. The following definitions supplement those in the art and are directed to the current application and are not to be imputed to any related or unrelated case, e.g., to any commonly owned patent or application. Although any methods and materials similar or equivalent to those described herein can be used in the practice for testing of the present disclosure, the preferred materials and methods are described herein. Accordingly, the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting. The terminology used herein is for the purpose of describing particular cases only and is not intended to be limiting. In this application, the use of the singular includes the plural unless specifically stated otherwise. As used herein, the singular forms “a”, “an” and “the” are intended to include the plural forms as well, unless the context clearly indicates otherwise. In this application, the use of “or” means “and / or” unless stated otherwise. The terms “and / or” and “any combination thereof” and their grammatical equivalents as used herein, can be used interchangeably. These terms can convey that any combination is specifically contemplated. Solely for illustrative purposes, the following phrases “A, B, and / or C” or “A, B, C, or any combination thereof” can mean “A individually; B individually; C individually; A and B; B and C; A and C; and A, B, and C.” The term “or” can be used conjunctively or disjunctively, unless the context specifically refers to a disjunctive use. The term “about” or “approximately” can mean within an acceptable error range for the particular value as determined by one of ordinary skill in the art, which will depend in part on how the value is measured or determined, i.e., the limitations of the measurement system. For example, “about” can mean within 1 or more than 1 standard deviation, per the practice in the art. Alternatively, “about” can mean a range of up to 20%, up to 15%, up to 10%, up to 5%, or up to 1% of a given value. Alternatively, particularly with respect to biological systems or processes, the term can mean within an order of magnitude, within 5-fold, or within 2-fold, of a value. Where particular values are described in the application and claims, unless otherwise stated the term “about” meaning within an acceptable error range for the particular value should be assumed. As used in this specification and claim(s), the words “comprising” (and any form of comprising, such as “comprise” and “comprises”), “having” (and any form of having, such as “have” and “has”), “including” (and any form of including, such as “includes” and “include”) or “containing” (and any form of containing, such as “contains” and “contain”) are inclusive or open-ended and do not exclude additional, unrecited elements or method steps. It is contemplated that any embodiment discussed in this specification can be implemented with respect to any method or composition of the present disclosure, and vice versa. Furthermore, compositions of the present disclosure can be used to achieve methods of the present disclosure.Docket No. WRENCH-001 / WO01 Reference in the specification to “some embodiments,” “an embodiment,” “one embodiment” or “other embodiments” means that a particular feature, structure, or characteristic described in connection with the embodiments is included in at least some embodiments, but not necessarily all embodiments, of the present disclosures. To facilitate an understanding of the present disclosure, a number of terms and phrases are defined below. Ranges provided herein are understood to be shorthand for all of the values within the range. For example, a range of 1 to 50 is understood to include any number, combination of numbers, or sub-range from the group consisting of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50, as well as all intervening decimal values between the aforementioned integers such as, for example, 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, and 1.9. With respect to sub-ranges, “nested sub-ranges” that extend from either end point of the range are specifically contemplated. For example, a nested sub-range of an exemplary range of 1 to 50 may comprise 1 to 10, 1 to 20, 1 to 30, and 1 to 40 in one direction, or 50 to 40, 50 to 30, 50 to 20, and 50 to 10 in the other direction. The term “subject” refers to an animal which is the object of treatment, observation, or experiment. By way of example only, a subject includes, but is not limited to, a mammal, including, but not limited to, a human or a non-human mammal, such as a non-human primate, bovine, equine, canine, ovine, or feline. The term “optional” or “optionally” denotes that a subsequently described event or circumstance can but need not occur, and that the description includes instances where the event or circumstance occurs and instances in which it does not. “Non-naturally occurring” (used interchangeably with “isolated”, “substantially pure” or “purified”) when applied to a polynucleotide or a polypeptide means a polynucleotide or a polypeptide that is synthesized chemically or synthetically, or is purified away from associated and contaminating components. The term generally means a polynucleotide or a polypeptide that has been separated from other proteins and nucleic acids with which it naturally occurs and / or substances which are used to purify it. In some instances, polynucleotide or a polypeptide herein is about 95%, about 96%, about 97%, about 98%, about 99% or above pure. A binding protein as defined herein is said to be “specific for” or “selectively binds to” IL-18BP or to a target antigen when it binds to IL-18BP or to the target antigen with an affinity that is at least 5 times, at least 10 times, at least 25 times, least 50 times, least 100 times, etc., better than the affinity with which said amino acid sequence or polypeptide binds to a non-specific polypeptide. "IL-18," "Interleukin-18," and "IL18” herein is meant a proinflammatoty cytokine that binds to IL18 receptor (IL18RI). IL18 is capable of stimulating IFNγ production and regulating Th1 and Th2 responses. Sequences of various IL18 proteins, corresponding IL18 receptors, IL18 receptor accessory proteins (IL18RAPs), and IL18 binding proteins (IL-18BPs) are shown in the listing of sequences attached herewith. Sequences of exemplary wildtype human precursor and mature IL-18, as well as the IL-18 receptor subunits are included in shown in the listing of sequences.Docket No. WRENCH-001 / WO01 The term "IL18 BP", "IL-18BP", "IL18BP", "IL-18BP", “IL-18-BP”, "IL18 binding protein", or "Interleukin 18 binding protein" may optionally include any such protein, or variants, conjugates, or fragments thereof, including but not limited to known or wild type IL-18BP, as described herein, as well as any naturally occurring splice variants, amino acid variants or isoforms. The term IL-18BP is used interchangeably with "IL18 binding protein", "Interleukin 18 binding protein", "IL18 BPa", "interleukin-18-binding protein isoform a", and "interleukin-18 binding protein isoform a precursor”. The term “soluble” form of IL-18BP is also used interchangeably with the terms “IL18 BP soluble” or “fragments of IL-18BP polypeptides”, which may refer broadly to one or more of the following optional polypeptides. The term "soluble" with regard to the form of IL-18BP is also used interchangeably with the terms "secreted" as well as "fragments of IL-18BP polypeptides", which may refer broadly to one or more of the IL-18BP polypeptides disclosed herein. “Ablation” herein is meant a decrease or removal of binding and / or activity. For example, “ablating FcγR binding” means the Fc region amino acid variant has less than 50% starting binding as compared to an Fc region not containing the specific variant, with more than 70-80-90-95-98% loss of binding being preferred, and in general, with the binding being below the level of detectable binding in a Biacore assay. However, unless otherwise noted, the Fc monomers as disclosed herein retain binding to the FcRn. "Modification" herein is meant an amino acid substitution, insertion, and / or deletion in a polypeptide sequence or an alteration to a moiety chemically linked to a protein. For example, a modification may be an altered carbohydrate or PEG structure attached to a protein. By “amino acid modification” herein is meant an amino acid substitution, insertion, and / or deletion in a polypeptide sequence. For clarity, unless otherwise noted, the amino acid modification is always to an amino acid coded for by DNA, e g., the 20 amino acids that have codons in DNA and RNA. “Amino acid substitution” or “substitution” herein means the replacement of an amino acid at a particular position in a parent polypeptide sequence with a different amino acid. In particular, in some embodiments, the substitution is to an amino acid that is not naturally occurring at the particular position, either not naturally occurring within the organism or in any organism. For example, the substitution E272Y or 272Y refers to a variant polypeptide, in this case an Fc variant, in which the glutamic acid at position 272 is replaced with tyrosine. For clarity, a protein which has been engineered to change the nucleic acid coding sequence but not to change the starting amino acid (for example exchanging CGG (encoding arginine) to CGA (still encoding arginine) to increase host organism expression levels) is not an “amino acid substitution”; that is, despite the creation of a new gene encoding the same protein, if the protein has the same amino acid at the particular position that it started with, it is not an amino acid substitution. “Amino acid insertion" or "insertion" as used herein means the addition of an amino acid residue or sequence at a particular position in a parent polypeptide sequence. For example, -233E designates an insertion of glutamic acid after position 233 and before position 234. Additionally, -233ADE or A233ADE designates an insertion of AlaAspGlu after position 233 and before position 234.Docket No. WRENCH-001 / WO01 “Amino acid deletion” or “deletion” as used herein means the removal of an amino acid residue or sequence at a particular position in a parent polypeptide sequence. For example, E233-, E233#, E233(), E233_, or E233del designates a deletion of glutamic acid at position 233. Additionally, EDAZ33- or EDA233¹ designates a deletion of the sequence GluAspAla that begins at position 233. “Variant protein”, “protein variant”, “mutein”, or “variant” as used herein means a protein that differs from that of a parent protein by virtue of at least one modification. Protein variant may refer to the protein itself, a composition comprising the protein, the amino acid sequence that encodes it, or the DNA sequence that encodes it Preferably, the protein variant has at least one amino acid modification compared to the parent protein, e.g. from about one to about seventy amino acid modifications, and preferably from about one to about five amino acid modifications compared to the parent, The modification can be an addition, deletion, or substitution. As described below, in some embodiments the parent protein, for example an Fc parent polypeptide, is a human wild type sequence, such as the Fc region from IgG1, IgG2, IgG3 or IgG4. The protein variant sequence herein will preferably possess at least about 80% identity with a parent protein sequence, and most preferably at least about 90% identity, more preferably at least about 95-98-99% identity. “Variant,” as used herein can also refer to particular amino acid modifications (e g, substitutions, deletions, insertions) in a variant protein (e.g., a variant Fc domain), for example, heterodimerization variants, ablation variants, etc.. As used herein, “Protein” means at least two covalently attached amino acids, which includes proteins, polypeptides, oligopeptides and peptides. When a biologically functional molecule comprises two or more proteins, each protein may be referred to as a “monomer” or as a “subunit”; and the biologically functional molecule may be referred to as a “complex”. Accordingly, “protein” in this context is used interchangeably with “polypeptide” and includes peptides as well. “Residue” as used herein means a position in a protein and its associated amino acid identity. For example, Asparagine 297 (also referred to as Asn297 or N297) is a residue at position 297 in the human antibody IgG1. “IgG subclass modification” or “isotype modification” as used herein means an amino acid modification that converts one amino acid of one IgG isotype to the corresponding amino acid in a different, aligned IgG isotype. For example, because IgG1 comprises a tyrosine and IgG2 a phenylalanine at EU position 296, a F296Y substitution in IgG2 is considered an IgG subclass modification. “Non-naturally occurring modification” as used herein with respect to an IgG domain means an amino acid modification that is not isotypic. For example, because none of the IgGs comprise a serine at position 434, the substitution 434S in IgGl, IgG2, IgG3, or IgG4 (or hybrids thereof is considered a non-naturally occurring modification. “Amino acid” and “amino acid identity” as used herein means one of the 20 naturally occurring amino acids that are coded for by DNA and RNA.Docket No. WRENCH-001 / WO01 “Effector function” as used herein means a biochemical event that results from the interaction of an antibody Fc region with an Fc receptor or ligand. Effector functions include but are not limited to ADCC, ADCP, and CDC. By “IgG Fc ligand” or “Fc ligand” as used herein is meant a molecule, preferably a polypeptide, from any organism that binds to the Fc region of an IgG antibody to form an Fc / Fc ligand complex. Fc ligands include but are not limited to FcγRIs, FcγRIIs, FcγRIIIs, FcRn, C1q, C3, mannan binding lectin. Mannose receptor, staphylococcal protein A, streptococcal protein G, and viral FcγR. Fc ligands also include Fc receptor homologs (FcRH), which are a family of Fc receptors that are homologous to the FcγRs (Davis et al., 2002, Immunological Reviews 190:123-136, entirely incorporated by reference) Fc ligands may include undiscovered molecules that bind Fc. Particular IgG Fc ligands are FcRn and Fc gamma receptors. “FcRn” or “neonatal Fc receptor” as used herein means a protein that binds the IgG antibody Fc region and is encoded at least in part by an FcRn gene. The FcRn may be from any organism, including but not limited to humans, mice, rats, rabbits, and monkeys. As is known in the art, the functional FcRn protein comprises two polypeptides, often referred to as the heavy chain and light chain. The light chain is beta-2-microglobulin (β2- microglobulin) and the heavy chain is encoded by the FcRn gene. Unless otherwise noted herein, FcRn or an FcRn protein refers to the complex of FcRn heavy chain with β2-microglobulin. A variety of Fc variants can be used to increase binding to the FcRn, and in some cases, to increase serum half-life. In general, unless otherwise noted, the Fc monomers of the invention retain binding to the FcRn (and, as noted below, can include amino acid variants to increase binding to the FcRn). “Parent polypeptide” as used herein means a starting polypeptide that is subsequently modified to generate a variant. The parent polypeptide may be a naturally occurring polypeptide (i.e., a wildtype polypeptide), or a variant or engineered version of a naturally occurring polypeptide. Parent polypeptide may refer to the polypeptide itself, compositions that comprise the parent polypeptide, or the amino acid sequence that encodes it. “Fc” or “Fc region” or “Fc domain” as used herein means the polypeptide comprising the constant region of an antibody, in some instances, excluding all of the first constant region immunoglobulin domain (e.g., CH1) or a portion thereof, and in some cases, optionally including all or part of the hinge. For IgG, the Fc domain comprises immunoglobulin domains CH2 and CH3 (Cγ2 and Cγ3), and optionally all or a portion of the hinge region between CH1 (Cγ1) and CH2 (Cγ2). Thus, in some cases, the Fc domain includes, from N- to C- terminus, CH2-CH3 and hinge-CH2-CH3. In some embodiments, the Fc domain is that from IgGI, IgG2, IgG3 or IgG4, with IgGI hinge-CH2-CH3 and IgG4 hinge-CH2-CH3 finding particular use in many embodiments. Additionally, in certain embodiments, wherein the Fc domain is a human IgG1 Fc domain, the hinge includes a C220S amino acid substitution. Furthermore, in some embodiments where the Fc domain is a human IgG4 Fc domain, the hinge includes a S228P amino acid substitution. Although the boundaries of the Fc region may vary, the human IgG heavy chain Fc region is usually defined to include residues E216, C226, or A231 to its carboxyl-terminus, wherein the numbering is according to the EU index as in Kabat. In someDocket No. WRENCH-001 / WO01 embodiments, as is more fully described below, amino acid modifications are made to the Fc region, for example to alter binding to one or more FcγR or to the FcRn. By “hinge” or “hinge region” or “antibody hinge region” or “immunoglobulin hinge region” herein is meant the flexible polypeptide comprising the amino acids between the first and second heavy chain constant domains of an antibody. Structurally, the IgG CH1 domain ends at EU position 215, and the IgG CH2 domain begins at residue EU position 231, Thus for IgG the antibody hinge is herein defined to include positions 216 (E216 in IgG1) to 230 (P230 in IgG1), wherein the numbering is according to the EU index as in Kabat. In some embodiments, for example in the context of an Fc region, the hinge (full length or a fragment of the hinge) is included, generally referring to positions 216-230. As noted herein, pI variants can be made in the hinge region as well. As will be appreciated by those in the art, the exact numbering and placement of the heavy constant region domains can be different among different numbering systems. A useful comparison of heavy constant region numbering according to EU and Kabat is as below, see Edelman et al., 1969, Proc Natl Acad Sci USA 63:78-85 and Kabat et al., 1991, Sequences of Proteins of Immunological Interest, 5thEd., United States Public Health Service, National Institutes of Health, Bethesda, entirely incorporated by reference. “Fc variant” or “variant Fc” as used herein means a protein comprising an amino acid modification in an Fc domain. The modification can be an addition, deletion, or substitution. The Fc variants of the present invention are defined according to the amino acid modifications that compose them. Thus, for example, N434S or 434S is an Fc variant with the substitution for serine at position 434 relative to the parent Fc polypeptide, wherein the numbering is according to the EU index. Likewise, M428L / N434S defines an Fc variant with the substitutions M428L and N434S relative to the parent Fc polypeptide. The identity of the WT amino acid may be unspecified, in which case the aforementioned variant is referred to as 428L / 434S. It is noted that the order in which substitutions are provided is arbitrary, that is to say that, for example, 428L / 434S is the same Fc variant as 434S / 428L, and so on. For all positions discussed herein that relate to antibodies or derivatives and fragments thereof (e.g., Fc domains), unless otherwise noted, amino acid position numbering is according to the EU index. The “EU index” or “EU index as in Kabat” or “EU numbering” scheme refers to the numbering of the EU antibody (Edelman et al., 1969, Proc Natl Acad Sci USA 63:78-85, hereby entirely incorporated by reference). The modification can be an addition, deletion, or substitution. “Fusion protein” as used herein means the covalent joining of at least two proteins or protein domains. Fusion proteins may comprise artificial sequences, e.g. a domain linker, an Fc domain (e.g., a variant Fc domain), an IL-7 (e.g., a variant IL-18), an anti-IL-18BP binding protein, etc. as described herein. By “Fc fusion protein” or “immunoadhesin” herein is meant a protein comprising an Fc region, generally linked (optionally through a domain linker, as described herein) to one or more different protein domains. Accordingly, an “IL- 18-Fc fusion” includes an Fc domain linked (optionally through a domain linker) to an IL-18, as described herein. In some instances, two Fc fusion proteins can form a homodimeric Fc fusion protein or a heterodimeric Fc fusion protein. In some embodiments, one monomer of a heterodimeric fusion protein includes an Fc domainDocket No. WRENCH-001 / WO01 alone (e.g., an “empty Fc domain”) and the other monomer is an Fc fusion, comprising a variant IL-18 or anti- IL-18BP antibody, as outlined herein. In some embodiments, one monomer of a heterodimeric fusion protein is an Fc fusion, comprising a variant IL-18, and the other monomer is an Fc fusion, comprising an anti-IL-18BP antibody, as outlined herein. In other embodiments, both the first and second monomers are Fc fusion proteins that include an Fc domain and an IL-18. In other embodiments, both the first and second monomers are Fc fusion proteins that include an Fc domain and an anti-IL-18BP antibody. “Position” as used herein means a location in the sequence of a protein. Positions may be numbered sequentially, or according to an established format, for example the EU index for numbering of antibody domains (e.g., a CH1, CH2, CH3 or hinge domain). “Strandedness” in the context of the monomers of the heterodimeric proteins of the invention herein means that, similar to the two strands of DNA that “match”, heterodimerization variants are incorporated into each monomer so as to preserve, create, and / or enhance the ability to “match” to form heterodimers. For example, if some pI variants are engineered into monomer A (e.g. making the pI higher), then steric variants that are “charge pairs” that can be utilized as well do not interfere with the pI variants, e.g., the charge variants that make a pI higher are put on the same “strand” or “monomer” to preserve both functionalities. Similarly, for “skew” variants that come in pairs of a set as more fully outlined below, the skilled artisan will consider pI in deciding into which strand or monomer that incorporates one set of the pair will go, such that pI separation is maximized using the pI of the skews as well. “Wild type,” “wildtype”, “wild-type”, or “WT” herein means an amino acid sequence or a nucleotide sequence that is found in nature, including allelic variations. A WT protein has an amino acid sequence or a nucleotide sequence that has not been intentionally modified. The various proteins, antibodies, binding proteins, and fusion proteins provided herein are generally isolated or recombinant. “Isolated,” when used to describe the various polypeptides disclosed herein, means a polypeptide that has been identified and separated and / or recovered from a cell or cell culture from which it was expressed. Ordinarily, an isolated polypeptide will be prepared by at least one purification step. An “isolated protein” refers to a protein which is substantially free of other proteins from a cell culture such as host cell proteins. “Recombinant” means the proteins are generated using recombinant nucleic acid techniques in exogeneous host cells. “Percent (%) amino acid sequence identity” with respect to a protein sequence is defined as the percentage of amino acid residues in a candidate sequence that are identical with the amino acid residues in the specific (parental) sequence, after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity, and not considering any conservative substitutions as part of the sequence identity Alignment for purposes of determining percent amino acid sequence identity can be achieved in various ways that are within the skill in the art, for instance, using publicly available computer software such as BLAST, BLAST-2, ALIGN or Megalign (DNASTAR) software Those skilled in the art can determine appropriate parameters for measuring alignment, including any algorithms needed to achieve maximal alignment over theDocket No. WRENCH-001 / WO01 full length of the sequences being compared. One particular program is the ALIGN-2 program outlined at paragraphs

[0279] to

[0280] of US Patent Publication No.20160244525, hereby incorporated by reference. The degree of identity between an amino acid sequence provided herein (“invention sequence”) and the parental amino acid sequence is calculated as the number of exact matches in an alignment of the two sequences, divided by the length of the “invention sequence,” or the length of the parental sequence, whichever is the shortest. The result is expressed in percent identity. The percent identity between two amino acid sequences can be determined using the algorithm of E. Meyers and W. Miller (Comput. Appl. Biosci., 4:11-17 (1988)) which has been incorporated into the ALIGN program (version 2.0), using a PAM120 weight residue table, a gap length penalty of 12 and a gap penalty of 4. In addition, the percent identity between two amino acid sequences can be determined using the Needleman and Wunsch (J. Mol. Biol., 48:444- 453 (1970)) algorithm which has been incorporated into the GAP program in the GGG software package (available commercially), using either a BLOSUM 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3,4, 5, or 6. In some embodiments, two or more amino acid sequences are at least 50%, 60%, 70%, 80%, or 90% identical. In some embodiments, two or more amino acid sequences are at least 95%, 97%, 98%, 99%, or even 100% identical. In general, the percentage identity for comparison between amino acid sequences is at least 75%, at least 80%, at least 90%, with at least about 95, 96, 97, 98 or 99% percent identity being preferred. The percentage identity may be along the whole amino acid sequence, for example the entire protein sequence, such as a heavy chain or along a portion of a heavy chain. For example, included within the definition of the anti- IL-18BP antibodies disclosed herein are those that share identity along the entire variable region (for example, where the identity is 95 or 98% identical along the variable region, and in some embodiments at least 95% or at least 98%). “Fused” or “covalently linked” means that the components (e g., an IL-18 and an Fc domain, or an anti-IL-18BP antibody and an Fc domain) are linked by peptide bonds, either directly or indirectly via domain linkers, as outlined herein. The strength, or affinity, of specific binding can be expressed in terms of the dissociation constant (KD) of the interaction, wherein a smaller KD represents greater affinity, and a larger KD represents lower affinity. Binding properties can be determined by methods well known in the art such as bio-layer interferometry (BLI) and surface plasmon resonance-based methods (SPR). One such method entails measuring the rates of antigen- binding site / antigen or receptor / ligand complex association and dissociation, wherein rates depend on the concentration of the complex partners, the affinity of the interaction, and geometric parameters that equally influence the rate in both directions. Thus, both the association rate (ka) and the dissociation rate (kd) can be determined, and the ratio of kd / ka is equal to the dissociation constant KD (See Nature 361.186-187 (1993) and Davies et al. (1990) Annual Rev Biochem 59:439-473). Specific binding for a particular molecule or an epitope can be exhibited, for example, by a molecule (e.g., IL-18) having a KD for its binding partner (e.g., IL-18 receptor) of at least about 10-4M, at least about 10-Docket No. WRENCH-001 / WO015M, at least about 10-6M, at least about 10-7M, at least about 10-8M, at least about 10-9M, alternatively at least about 10-10M, at least about 10-11M, at least about 10-12M, or greater. Typically, an antigen binding molecule that specifically binds an antigen will have a KD that is 20, 50, 100, 500, 1000, 5,000, 10,000 or more times greater for a control molecule relative to the antigen or epitope. III. Variant IL-18 Proteins In some aspects, provided herein are IL-18 variant proteins wherein specific residues are mutated based in part on their proximity to certain cysteine residues, resulting in the formation of new disulfide bridges and a more compact structure. Such mutations were designed to increase the stability, expression yield, and overall utility of the resulting variant IL-18 proteins. As further described below, additional benefits may be conferred by fusing such variant IL-18 proteins with an Fc region, creating IL-18-Fc fusion variants, including with combinations of single-domain anti-IL-18BP antibodies. In some aspects provided herein are variant IL-18 proteins and compositions. Variant IL-18s as described herein can comprise a modification at one or more amino acid positions selected from the group consisting of L9, V11, N14, C38, I49, V62, C68, C76, K79, F101, S117, S119, Y120, Y123, C127, Q154, and E156, as compared to wildtype human IL-18; functional fragments of such variant IL-18s; variants of such variant IL-18s that include 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 additional amino acid modifications; and variants that are at least 90, 91, 92, 93, 95, 95, 96, 97, 98, or 99% identical to such variant IL-18s. In some embodiments, the variant IL-18 protein comprises a modification at one or more amino acid positions selected from the group consisting of L9, E156, K79, Y120, S117, and S119, as compared to wildtype human IL-18. the variant IL-18 protein comprises amino acid substitutions selected from the group consisting of: L9 / E156, V11 / Q154, I49 / V62, V62 / F101, K79 / Y120, K79 / Y123, S117, S119, and N14, as compared to wildtype human IL-18. In some embodiments, the variant IL-18 protein comprises amino acid substitutions at residues C38, C68, C76, and C127. In some embodiments, the variant IL-18 protein comprises an amino acid substitution at residues C38 and / or C68, as compared to wildtype human IL-18. In some embodiments, the variant IL-18 protein further comprises an amino acid substitution at C127, as compared to wildtype human IL-18. In these embodiments, the variant IL-18 protein may further comprise an amino acid substitution resulting in a cysteine residue, wherein that cysteine residue forms a disulfide bond with C76 or C127. In some embodiments, the amino acid substitution resulting in a cysteine residue comprises S117C or S119C, wherein that cysteine residue forms a disulfide bond with C76. In some embodiments, the amino acid substitution resulting in a cysteine residue comprises N14C, wherein that cysteine residue forms a disulfide bond with C127. In some embodiments, the amino acid substitution resulting in a cysteine is positioned within 3, 2, or 1 angstrom of C76 or C127. In some embodiments, the variant IL-18 protein comprises amino acid substitutions at residues C38, C68, C76, and C127. In some embodiments, the variant IL18 protein comprises amino acid substitutions selected from the group consisting of: L9 / E156, V11 / Q154, I49 / V62, V62 / F101, K79 / Y120, K79 / Y123, S117, S119, and N14.Docket No. WRENCH-001 / WO01 The numbering of such IL-18 modifications described herein are based on the human IL-18 mature form sequence (SEQ ID NO: 552) as shown in FIG.1A, wherein the first amino acid of the sequence ("Y") is amino acid position 1. Provided herein are compositions that include such a variant IL18 having one or more amino acid substitutions that may increase stability and / or activity, as well as improve production of the variant IL-18. Such amino acid substitutions may also increase stability and / or activity, as improve production, of variant IL-18 fusion proteins, such as variant IL-18s fused to an Fc region, as further described herein. In certain embodiments, the IL-18 variant includes one or more modifications to improve thermostability compared to wildtype human IL-18. In some embodiments, the IL-18 variant possesses one or more modifications that improve stability in the context of cysteine engineering (such as by removing unpaired cysteines, e.g., the removal of C38, C68, C76, and C127 (“4CS”); adding new cysteines; and / or introducing new disulfide bridges). Residues which may be modified to improve stability include L9, V11, N14, C38, I49, V62, C68, C76, K79, F101, S117, S119, Y120, Y123, C127, Q154, and E156. In some embodiments, the residues which may be modified to improve thermostability include L9 / E156, K78 / Y120, S117, S119, or N14. In some embodiments, the residues which may be modified to improve thermostability include L9C / E156C, K78C / Y120C, S117C, S119C, or N14C. In some embodiments, the variant IL-18 protein has a melting temperature of at least 50C. In some embodiments, the variant IL-18 protein has a melting temperature of at least 60C. In some embodiments, the variant IL-18 protein has a melting temperature of at least 70C. In some embodiments, the IL-18 variant protein exhibits increased activation of the IL-18 receptor- mediated signaling compared to human IL-18 (4CS). Residues which may be modified to increase activation of the IL-18 receptor-mediated signaling include S117, e.g., S117C. In such embodiments, S117C may form a disulfide bond with C76. In some embodiments, the variant IL-18 protein exhibits decreased activation of the IL18 receptor- mediated signaling compared to wildtype IL-18. Residues which may be modified to decrease activation of the IL-18 receptor-mediated signaling include N14, e.g., N14C. In such embodiments, N14C may form a disulfide bond with C127. In certain embodiments, the IL-18 variant includes one or more modifications to improve production yield. Such modifications are intended to improve yield and / or decrease molecular heterogeneity. Residues which may be modified to improve production include L9, V11, N14, C38, I49, V62, C68, C76, K79, F101, S117, S119, Y120, Y123, C127, Q154, and E156. In some embodiments, the residues which may be modified to improve production yield include L9 / E156, K78 / Y120, S117, S119, or N14. In some embodiments, the residues which may be modified to improve production yield include L9C / E156C, K78C / Y120C, S117C, S119C, or N14C. In one embodiment, an IL-18 variant protein comprises a sequence selected from Table 13. In some embodiments, an IL-18 variant protein comprises an additional 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid modifications from a sequence selected from Table 13. In some embodiments, an IL-18 variant protein is at least 90%, 95%, 98%, 99%, or 100% identical to a sequence selected from Table 13.Docket No. WRENCH-001 / WO01 IV. Anti-IL-18BP Binding Antibodies a. Interleukin 18 Binding Protein (IL-18BP) The IL-18BP gene is localized to the human chromosome 11, and is only expressed as a secreted protein, as no exon coding for a transmembrane domain is present in the 8.3 kb genomic sequence comprising the IL-18BP gene. Four isoforms of IL-18BP generated by alternative mRNA splicing have been identified in humans so far. They were designated IL-18BP a, b, c, and d, all sharing the same N-terminus and differing in the C-terminus (Novick, D. et al., Immunity, 10.127-136, (1999)). These isoforms vary in their ability to bind IL-18 (Kim, S.H. et al., PNAS, 97(3): 1190-1195 (2000)). Of the four human IL-18BP (hIL-18BP) isoforms, isoforms a and c are known to have a neutralizing capacity for IL-18. The most abundant IL-18BP isoform, isoform a, exhibits a high affinity for IL-18 with a rapid on-rate and a slow off-rate, and a dissociation constant (Kd) of approximately 0.4 nM (Kim et al.). IL-18BPb and IL-18BPd isoforms lack a complete Ig domain and lack the ability to bind or neutralize IL18. Two mouse isoforms of IL-18BP, resulting from mRNA splicing and found in various cDNA libraries and have been expressed, purified, and assessed for binding and neutralization of IL-18 biological activities (Kim et al). Human and mouse IL-18BP share 60.8% amino acid similarity. Murine IL-18BPc and IL-18BPd isoforms, possessing the identical Ig domain, also neutralize >95% murine IL-18 at a molar excess of two. However, murine IL-18BPd, which shares a common C-terminal motif with human IL-18BPa, also neutralizes human IL-18. Molecular modeling identified a large mixed electrostatic and hydrophobic binding site in the Ig domain of IL-18BP, which could account for its high affinity binding to the ligand (Kim et al.). IL-18BP is a secreted protein of 194 amino acids in length, with a signal peptide (spanning from amino acid 1 to 30), and a secreted chain (spanning from amino acid 41 to 171) and 4 potential N-glycosylation sites but no transmembrane domains. The full-length human IL-18BP isoform a protein is shown in SEQ ID NO: 555. The present disclosure provides formulations comprising antibodies and binding proteins that specifically bind to IL-18BP proteins. IL-18BP is constitutively expressed in the spleen and belongs to the immunoglobulin superfamily. The residues involved in the interaction of IL-18 with IL-18BP have been described through computer modelling (Kim et al.) based on the interaction between the similar protein IL-1β) with the IL-IR type I (Vigers, G. P A. et al., Nature, 386:190-194 (1997)), and by co-crystallization studies (Detry, S., et al, Journal of Biological Chemistry, 298(5), 101908 (2022)). IL-18BP functions as an inhibitor of the proinflammatory cytokine, IL-18. As described further herein, IL-18 modulates immune system functions including induction of IFNγ production, Th1 differentiation, NK cell activation, and cytotoxic T lymphocyte (CTL) responses (Tominaga, K, et al., International Immunology, 12(2): 151-160 (2000) and Senju, H., et al., Int J Biol Sci., 14(3):331-340 (2018)). IL-18BP binds IL-18, prevents the binding of IL-18 to its receptor, and thus inhibits IL-18 induced T and NK cell activation and proliferation, and pro-inflammatory cytokine production, resulting in reduced T and NK cell activity and T-helper type I immune responses. IL-18BP abolishes IL-18 induction of IFN-γ and IL-18Docket No. WRENCH-001 / WO01 activation of NF-xB in vitro. In addition, IL-18BP inhibits induction of IFN-γ in mice injected with LPS terminus (Novick, D., et al., Immunity, 10:127-136 (1999)). IL-18 is constitutively present in many cells (Puren et al., PNAS, 96:2256-2261 (1999)) and circulates in healthy humans (Urushihara et al.2000), representing a unique phenomenon in cytokine biology. Due to the high affinity of IL-18 to IL-18BP (Kd of ~400 pM) as well as the high concentration of IL-18BP found in the circulation (20-fold molar excess over IL-18), it has been hypothesized that most, if not all of the IL-18 molecules in the circulation are bound to IL-18BP. Thus, the circulating IL-18BP that competes with cell surface receptors for IL-18 may act as a natural anti-inflammatory and an immunosuppressive molecule. b. Anti-IL-18BP Antibodies The present disclosure further provides antibodies, antigen binding domains, and binding proteins that specifically bind to interleukin 18 binding protein (IL-18BP), and which may contain a number of specific, enumerated sites of CDRs. Such antibodies, antigen binding domains, and binding proteins result in increased levels of circulating IL-18. The inventor has recognized that because IL-18BP is a soluble circulating protein (and not a membrane-associated protein), and given the high rate of IL-18BP synthesis as it is found at 20-fold molar excess over IL-18, the strategy of using a pH-sensitive blocking antibody, over a standard blocking antibody, to release IL-18 from IL-18BP, and to increase IL-18BP clearance represents a promising approach that enables lower antibody doses and less frequent dosing. In certain diseases, immune function can be compromised due to a deficiency in IL-18. For instance, some cancers exhibit an overexpression of IL-18BP, resulting in nearly 20 times more IL-18BP than free IL- 18. This overexpression significantly diminishes the amount of circulating IL-18, enabling the cancer to evade immune responses. According to at least some embodiments of the disclosure, the anti-IL-18BP antibodies (including antigen-binding fragments) bind to IL-18BP, release endogenous IL-18 from IL-18BP, and block the interaction of IL-18 and IL-18BP, thereby releasing increased levels of free IL-18. The heightened IL-18 levels restore and enhance immune function, promoting the activation, proliferation, and secretion of cytokines and chemokines by various immune cells such as T cells, NK cells, NKT cells, Myeloid cells, Dendritic cells, MAIT T cells, γδ T cells, and / or innate lymphoid cells (ILCs). This therapeutic approach holds promise for treating diseases such as cancer and pathogen infections, utilizing anti-IL-18BP antibodies to restore immune function. Accordingly, anti-IL-18BP antibodies according to the disclosure find use in treating diseases such as cancer. The disclosure provides anti-IL-18BP antibodies. IL-18BP, also called Interleukin-18 binding protein, UniProtKB / Swiss-Prot (095998) or HGNC (5987) NCBI Entrez Gene (10068), relates to amino acid and nucleic acid sequences shown in RefSeq accession identifier NG 029021 I, NM 001039659 I, NP 001034748 I, NC 000011 10 Chromosome 11 Reference GRCh38 p13 Primary Assembly accession identifier. NM 001039660 2 and NP 001034749 I and NC 000011 9 Chromosome 11 Reference GRCh38 p13 Primary Assembly accession identifier: NP 001034748 1, NM 001039659.2, NP 005690.2NM 005699.3 NP 001034748.1NM 001039659.2, NP 005690.2, NM 005699.3, NP 001138529.1 NM 001145057.1, NPDocket No. WRENCH-001 / WO01 001138527.1, NM 001145055.1. In some embodiments, the antibodies of the invention are specific for IL- 18BP. The present disclosure provides single domain anti-IL-18BP antibodies. (For convenience, “anti-IL- 18BP antibodies” and “IL-18BP antibodies” are used interchangeably). The anti-IL-18BP antibodies of the invention specifically bind to human IL-18BP, and preferably the secreted chain of human IL-18BP (SEQ ID NO: 556), including, e.g., anti-IL-18BP antibodies including those with CDRs identical to those shown in Table 16. Single-domain anti-IL-18BP antibodies may also commonly be referred to as VHHs and nanobodies. VHHs are a distinct class of antibody fragments derived from heavy-chain-only antibodies prevalent in camelids such as camels, llamas, and alpacas. Specifically, VHHs are defined by their single-variable domain structure, which sets them apart from conventional antibodies characterized by two heavy chains and two light chains. This single-domain architecture imparts unique advantages to VHHs, including their diminutive size, exceptional stability, solubility, and remarkable specificity and affinity for target antigens. Further, this single-domain architecture allows for multiple VHHs to be fused to other proteins, such as an Fc region, resulting in multispecific proteins and bivalent and tetravalent fusion proteins, as further described herein. The inventors have recognized and appreciated that VHHs are particularly useful as an anti-IL-18BP antibody. Such single-domain antibodies are easier to produce, in part due to a reduction in complexity and lack of unintended VH / VL pairing. Further, up to four VHHs may be fused directly to an Fc, but only two for IgG. Increasing the possible valency from bivalent to tetravalent is particularly beneficial as a single molecule can bind to multiple IL-18BP molecules and thus remove larger quantities of IL-18BP from circulation. The anti-IL-18BP antibodies of the disclosure (including antigen-binding fragments) compete with IL- 18 to prevent the binding of IL-18 with IL-18BP. For example, the single-domain antibodies may bind to IL- 18 at the same epitope as for IL-18 / IL-18BP and thus may displace IL-18 from IL-18BP, resulting in an increased level of IL-18 in circulation. As IL-18 and IL-18BP associate and disassociate with one another, IL- 18BP will more readily bind to single-domain antibodies of the disclosure. Such antibodies can be used in treating diseases such as cancer and pathogen infection. The present disclosure provides anti-IL-18BP antibodies having pH-sensitive binding affinities to IL- 18BP. For soluble protein antigens such as IL-18BP, the concentration of that protein antigen in an extracellular fluid depends on the equilibrium between its production and its removal via endocytosis and lysosomal degradation. Administration of a specific antibody can profoundly increase the half-life of an antigen by trapping it in an antigen–antibody complex that is recycled by FcRn in endosomes. The inventor has recognized that this issue can be addressed by the use of antibodies that are pH-sensitive and release bound antigen in acidified endosomes during antibody recycling. A conventional high-affinity antibody usually binds an antigen and remains in complex with the antigen for a long time. This effect results from a desired mechanism for a low dissociation rate. However, once the antibody and antigen are bound, the antibody is unable to target and bind to additional antigens. In contrast to conventional antibodies, pH-sensitive antibodies can release their antigens upon internalization into endosomes.Docket No. WRENCH-001 / WO01 For example, an antibody that has a high binding affinity for its antigen at (e.g.) pH 6.5 or pH 7.4 will bind well to antigens in the tumor microenvironment and blood, respectively. However, once the antibody-antigen complex is internalized through endocytosis into endosomes (having an acidic environment with a pH of 5.8), the pH-sensitive binding between the antibody and antigen may be disrupted, leading to dissociation and subsequent degradation of the antigen. Following dissociation, the antibodies may be released into the lumen of the endosomes and are subsequently recycled and reused to bind their target again. For example, antibodies may be transported back to the cell surface, or released into the extracellular environment, where they can bind to new antigens and participate in subsequent immune responses, while the antigens remain in the endosome and are subject to degradation. In this way, antibodies of the disclosure can work in cycles of antigen binding — endocytosis — antigen releasing — recycling into the extracellular fluid — antigen binding, and which may be commonly referred to as “recycling antibodies” or “antigen clearance-enhancing antibodies”. Such recycling antibodies have particular utility in the context of single-domain antibodies, IL-18BP, and anti-IL-18BP antibody-Fc fusion proteins, as further described herein. Accordingly, in some embodiments, the binding affinity of the IL-18BP antibody for IL-18BP is pH- sensitive. In such embodiments, the binding affinity of an anti-IL-18BP antibody for IL-18BP may be 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, or 100-fold less at a pH of 5.8 or lower, as compared to the binding affinity at a pH of 6.5 or above. In some embodiments, the binding affinity of the anti- IL-18BP antibody for IL-18BP is 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, or 100-fold less at a pH of 5.8 or lower, as compared to the binding affinity at a pH of 7.4 or above. In some embodiments, the binding affinity of the anti-IL-18BP antibody for IL-18BP is 100-fold, 200-fold, 300-fold, 400-fold, 500-fold, 600-fold, 700-fold, 800-fold, 900-fold, or 1000-fold less at a pH of 5.8 or lower, as compared to the binding affinity at a pH of 6.5 or 7.4 or above. Specific binding for IL-18BP or a IL-18BP epitope can be exhibited, for example, by an antibody having a KD of at least about 10-5M, at least about 10-6M, at least about 10-7M, at least about 10-8M, at least about 10-9M, alternatively at least about 10-10M, at least about 10-11M, at least about 10-12M, at least about 10-13M, at least about 10-14M, or greater, where KD refers to a dissociation rate of a particular antibody-antigen interaction. Typically, an antibody that specifically binds an antigen will have a KD that is 20-, 50-, 100-, 500- , 1000-, 5,000-, 10,000-, 100,000- or more times greater for a control molecule relative to the IL-18BP antigen or epitope. However, as supported by the Examples, for optimal binding to IL-18BP, the antibodies of the disclosure preferably have a KD (also referred to as the binding affinity) of less than 50nM, less than 40nM, less than 30nM, less than 20nM, less than 10 nM, less than 5nM, less than 1nM, or less than 100pM, at a pH of 6.5 – 7.4. In some embodiments, the antibodies of the disclosure preferably bind to human IL-18BP with a KD of less than 50nM, less than 40nM, less than 30nM, less than 20nM, less than 10 nM, less than 5nM, less than 1nM, or less than 100 pM, at a pH of 6.5 – 7.4, wherein KD is determined by known methods, e.g. surfaceDocket No. WRENCH-001 / WO01 plasmon resonance (SPR, e.g. Biacore instrument), Bio-Layer interferometry (BLI, e.g. Octet instrument), ELISA, KinExA, and most typically BLI or SPR at 25 or 37C. Also, specific binding for a particular antigen or an epitope can be exhibited, for example, by an antibody having a KA or Ka for an IL-18BP antigen or epitope of at least 20-, 50-, 100-, 500-, 1000-, 5,000-, 10,000-, 100,000- or more times greater for the epitope relative to a control, where KA or Ka refers to an association rate of a particular antibody-antigen interaction. The disclosure provides antigen binding domains, including single domain antibodies, which contain a number of specific, enumerated sets of CDRs, as provided in Table 16. As discussed herein, the disclosure further provides variants of the above components, including variants in the CDRs, as outlined above. In one aspect, a single domain anti-IL-18BP binding protein comprises an amino acid sequence of any of the clones of Table 15. In one aspect, a single domain anti-IL-18BP binding protein comprises or consist of a CDR-H1 having a sequence selected from any CDR-H1 in Table 16. In one aspect, a single domain anti-IL- 18BP binding protein comprises or consist of a CDR-H2 having a sequence selected from any CDR-H2 in Table 16. In one aspect, a single domain anti-IL-18BP binding protein comprises or consist of a CDR-H3 having a sequence selected from any CDR-H3 in Table 16. In one aspect, a single domain anti-IL-18BP binding protein comprises a CDR-H1, a CDR-H2, and a CDR-H3 selected from any CDR-H1, any CDR-H2, and any CDR-H3 in Table 16, wherein the selected CDR-H1, CDR-H2, and CDR-H3 are paired according to Table 17. VHH-21 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 1, the CDR-H2 has an amino acid sequence of SEQ ID NO: 51, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 101, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 301, the CDR-H2 has an amino acid sequence of SEQ ID NO: 351, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 401, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 151, the CDR-H2 has an amino acid sequence of SEQ ID NO: 201, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 251, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 1; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 51; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 101, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 301; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 351; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 401, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 151; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 201; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 251, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 500 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 500. VHH-22 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 2, the CDR-H2 has an amino acid sequence of SEQ ID NO: 52, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 102, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 302, the CDR-H2 has an amino acid sequence of SEQ ID NO: 352, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 402, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 152, the CDR-H2 has an amino acid sequence of SEQ ID NO: 202, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 252, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 2; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 52; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 102, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 302; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 352; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 402, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 152; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 202; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 252, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 501 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 501. VHH-23 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 3, the CDR-H2 has an amino acid sequence of SEQ ID NO: 53, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 103, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 303, the CDR-H2 has an amino acid sequence of SEQ ID NO: 353, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 403, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 153, the CDR-H2 has an amino acid sequence of SEQ ID NO: 203, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 253, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 3; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 53; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 103, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 303; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 353; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 403, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 153; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 203; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 253, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 502 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 502. VHH-24 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 4, the CDR-H2 has an amino acid sequence of SEQ ID NO: 54, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 104, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 304, the CDR-H2 has an amino acid sequence of SEQ ID NO: 354, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 404, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 154, the CDR-H2 has an amino acid sequence of SEQ ID NO: 204, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 254, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 4; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 54; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 104, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 304; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 354; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 404, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 154; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 204; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 254, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 503 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 503. VHH-25 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 5, the CDR-H2 has an amino acid sequence of SEQ ID NO: 55, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 105, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 305, the CDR-H2 has an amino acid sequence of SEQ ID NO: 355, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 405, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 155, the CDR-H2 has an amino acid sequence of SEQ ID NO: 205, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 255, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 5; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 55; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 105, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 305; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 355; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 405, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 155; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 205; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 255, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 504 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 504. VHH-26 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 6, the CDR-H2 has an amino acid sequence of SEQ ID NO: 56, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 106, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 306, the CDR-H2 has an amino acid sequence of SEQ ID NO: 356, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 406, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 156, the CDR-H2 has an amino acid sequence of SEQ ID NO: 206, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 256, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 6; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 56; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 106, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 306; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 356; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 406, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 156; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 206; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 256, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 505 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 505. VHH-27 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 7, the CDR-H2 has an amino acid sequence of SEQ ID NO: 57, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 107, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 307, the CDR-H2 has an amino acid sequence of SEQ ID NO: 357, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 407, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 157, the CDR-H2 has an amino acid sequence of SEQ ID NO: 207, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 257, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 7; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 57; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 107, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 307; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 357; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 407, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 157; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 207; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 257, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 506 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 506. VHH-28 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 8, the CDR-H2 has an amino acid sequence of SEQ ID NO: 58, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 108, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 308, the CDR-H2 has an amino acid sequence of SEQ ID NO: 358, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 408, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 158, the CDR-H2 has an amino acid sequence of SEQ ID NO: 208, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 258, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 8; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 58; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 108, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 308; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 358; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 408, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 158; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 208; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 258, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 507 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 507. VHH-H10 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 9, the CDR-H2 has an amino acid sequence of SEQ ID NO: 59, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 109, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 309, the CDR-H2 has an amino acid sequence of SEQ ID NO: 359, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 409, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 159, the CDR-H2 has an amino acid sequence of SEQ ID NO: 209, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 259, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 9; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 59; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 109, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 309; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 359; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 409, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 159; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 209; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 259, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 508 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 508. WB94 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 10, the CDR-H2 has an amino acid sequence of SEQ ID NO: 60, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 110, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 310, the CDR-H2 has an amino acid sequence of SEQ ID NO: 360, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 410, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 160, the CDR-H2 has an amino acid sequence of SEQ ID NO: 210, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 260, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 10; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 60; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 110, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 310; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 360; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 410, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 160; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 210; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 260, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 509 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 509. WB95 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 11, the CDR-H2 has an amino acid sequence of SEQ ID NO: 61, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 111, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 311, the CDR-H2 has an amino acid sequence of SEQ ID NO: 361, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 411, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 161, the CDR-H2 has an amino acid sequence of SEQ ID NO: 211, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 261, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 11; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 61; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 111, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 311; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 361; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 411, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 161; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 211; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 261, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 510 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 510. WB96 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 12, the CDR-H2 has an amino acid sequence of SEQ ID NO: 62, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 112, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 312, the CDR-H2 has an amino acid sequence of SEQ ID NO: 362, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 412, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 162, the CDR-H2 has an amino acid sequence of SEQ ID NO: 212, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 262, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 12; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 62; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 112, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 312; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 362; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 412, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 162; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 212; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 262, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 511 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 511. WB101 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 13, the CDR-H2 has an amino acid sequence of SEQ ID NO: 63, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 113, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 313, the CDR-H2 has an amino acid sequence of SEQ ID NO: 363, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 413, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 163, the CDR-H2 has an amino acid sequence of SEQ ID NO: 213, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 263, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 13; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 63; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 113, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 313; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 363; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 413, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 163; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 213; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 263, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 512 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 512. WB104 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 14, the CDR-H2 has an amino acid sequence of SEQ ID NO: 64, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 114, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 314, the CDR-H2 has an amino acid sequence of SEQ ID NO: 364, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 414, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 164, the CDR-H2 has an amino acid sequence of SEQ ID NO: 214, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 264, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 14; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 64; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 114, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 314; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 364; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 414, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 164; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 214; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 264, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 513 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 513. WB111 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 15, the CDR-H2 has an amino acid sequence of SEQ ID NO: 65, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 115, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 315, the CDR-H2 has an amino acid sequence of SEQ ID NO: 365, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 415, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 165, the CDR-H2 has an amino acid sequence of SEQ ID NO: 215, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 265, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 15; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 65; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 115, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 315; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 365; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 415, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 165; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 215; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 265, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 514 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 514. VHH-B12 In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 16, the CDR-H2 has an amino acid sequence of SEQ ID NO: 66, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 116, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 316, the CDR-H2 has an amino acid sequence of SEQ ID NO: 366, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 416, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 166, the CDR-H2 has an amino acid sequence of SEQ ID NO: 216, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 266, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 16; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 66; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 116, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 316; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 366; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 416, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 166; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 216; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 266, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 515 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 515. WB131 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 17, the CDR-H2 has an amino acid sequence of SEQ ID NO: 67, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 117, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 317, the CDR-H2 has an amino acid sequence of SEQ ID NO: 367, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 417, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 167, the CDR-H2 has an amino acid sequence of SEQ ID NO: 217, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 267, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 17; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 67; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 117, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 317; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 367; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 417, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 167; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 217; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 267, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 516 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 516. WB134 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 18, the CDR-H2 has an amino acid sequence of SEQ ID NO: 68, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 118, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 318, the CDR-H2 has an amino acid sequence of SEQ ID NO: 368, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 418, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 168, the CDR-H2 has an amino acid sequence of SEQ ID NO: 218, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 268, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 18; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 68; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 118, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 318; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 368; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 418, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 168; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 218; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 268, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 517 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 517. WB181 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 19, the CDR-H2 has an amino acid sequence of SEQ ID NO: 69, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 119, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 319, the CDR-H2 has an amino acid sequence of SEQ ID NO: 369, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 419, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 169, the CDR-H2 has an amino acid sequence of SEQ ID NO: 219, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 269, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 19; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 69; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 119, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 319; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 369; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 419, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 169; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 219; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 269, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 518 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 518. WB182 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 20, the CDR-H2 has an amino acid sequence of SEQ ID NO: 70, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 120, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 320, the CDR-H2 has an amino acid sequence of SEQ ID NO: 370, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 420, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 170, the CDR-H2 has an amino acid sequence of SEQ ID NO: 220, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 270, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 20; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 70; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 120, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 320; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 370; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 420, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 170; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 220; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 270, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 519 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 519. WB185 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 21, the CDR-H2 has an amino acid sequence of SEQ ID NO: 71, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 121, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 321, the CDR-H2 has an amino acid sequence of SEQ ID NO: 371, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 421, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 171, the CDR-H2 has an amino acid sequence of SEQ ID NO: 221, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 271, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 21; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 71; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 121, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 321; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 371; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 421, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 171; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 221; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 271, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 520 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 520. WB186 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 22, the CDR-H2 has an amino acid sequence of SEQ ID NO: 72, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 122, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 322, the CDR-H2 has an amino acid sequence of SEQ ID NO: 372, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 422, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 172, the CDR-H2 has an amino acid sequence of SEQ ID NO: 222, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 272, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 22; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 72; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 122, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 322; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 372; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 422, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 172; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 222; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 272, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 521 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 521. WB187 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 23, the CDR-H2 has an amino acid sequence of SEQ ID NO: 73, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 123, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 323, the CDR-H2 has an amino acid sequence of SEQ ID NO: 373, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 423, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 173, the CDR-H2 has an amino acid sequence of SEQ ID NO: 223, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 273, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 23; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 73; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 123, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 323; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 373; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 423, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 173; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 223; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 273, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 522 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 522. WB190 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 24, the CDR-H2 has an amino acid sequence of SEQ ID NO: 74, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 124, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 324, the CDR-H2 has an amino acid sequence of SEQ ID NO: 374, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 424, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 174, the CDR-H2 has an amino acid sequence of SEQ ID NO: 224, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 274, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 24; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 74; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 124, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 324; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 374; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 424, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 174; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 224; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 274, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 523 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 523. WB195 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 25, the CDR-H2 has an amino acid sequence of SEQ ID NO: 75, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 125, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 325, the CDR-H2 has an amino acid sequence of SEQ ID NO: 375, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 425, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 175, the CDR-H2 has an amino acid sequence of SEQ ID NO: 225, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 275, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 25; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 75; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 125, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 325; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 375; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 425, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 175; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 225; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 275, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 524 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 524. WB196 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 26, the CDR-H2 has an amino acid sequence of SEQ ID NO: 76, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 126, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 326, the CDR-H2 has an amino acid sequence of SEQ ID NO: 376, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 426, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 176, the CDR-H2 has an amino acid sequence of SEQ ID NO: 226, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 276, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 26; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 76; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 126, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 326; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 376; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 426, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 176; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 226; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 276, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 525 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 525. WB202 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 27, the CDR-H2 has an amino acid sequence of SEQ ID NO: 77, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 127, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 327, the CDR-H2 has an amino acid sequence of SEQ ID NO: 377, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 427, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 177, the CDR-H2 has an amino acid sequence of SEQ ID NO: 227, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 277, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 27; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 77; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 127, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 327; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 377; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 427, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 177; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 227; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 277, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 526 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 526. WB203 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 28, the CDR-H2 has an amino acid sequence of SEQ ID NO: 78, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 128, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 328, the CDR-H2 has an amino acid sequence of SEQ ID NO: 378, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 428, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 178, the CDR-H2 has an amino acid sequence of SEQ ID NO: 228, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 278, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 28; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 78; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 128, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 328; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 378; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 428, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 178; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 228; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 278, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 527 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 527. WB204 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 29, the CDR-H2 has an amino acid sequence of SEQ ID NO: 79, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 129, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 329, the CDR-H2 has an amino acid sequence of SEQ ID NO: 379, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 429, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 179, the CDR-H2 has an amino acid sequence of SEQ ID NO: 229, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 279, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 29; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 79; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 129, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 329; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 379; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 429, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 179; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 229; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 279, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 528 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 528. WB207 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 30, the CDR-H2 has an amino acid sequence of SEQ ID NO: 80, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 130, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 330, the CDR-H2 has an amino acid sequence of SEQ ID NO: 380, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 430, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 180, the CDR-H2 has an amino acid sequence of SEQ ID NO: 230, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 280, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 30; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 80; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 130, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 330; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 380; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 430, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 180; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 230; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 280, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 529 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 529. WB208 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 31, the CDR-H2 has an amino acid sequence of SEQ ID NO: 81, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 131, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 331, the CDR-H2 has an amino acid sequence of SEQ ID NO: 381, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 431, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 181, the CDR-H2 has an amino acid sequence of SEQ ID NO: 231, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 281, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 31; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 81; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 131, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 331; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 381; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 431, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 181; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 231; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 281, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 530 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 530. WB209 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 32, the CDR-H2 has an amino acid sequence of SEQ ID NO: 82, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 132, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 332, the CDR-H2 has an amino acid sequence of SEQ ID NO: 382, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 432, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 182, the CDR-H2 has an amino acid sequence of SEQ ID NO: 232, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 282, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 32; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 82; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 132, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 332; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 382; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 432, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 182; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 232; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 282, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 531 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 531. WB210 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 33, the CDR-H2 has an amino acid sequence of SEQ ID NO: 83, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 133, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 333, the CDR-H2 has an amino acid sequence of SEQ ID NO: 383, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 433, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 183, the CDR-H2 has an amino acid sequence of SEQ ID NO: 233, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 283, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 33; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 83; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 133, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 333; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 383; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 433, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 183; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 233; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 283, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 532 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 532. WB211 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 34, the CDR-H2 has an amino acid sequence of SEQ ID NO: 84, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 134, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 334, the CDR-H2 has an amino acid sequence of SEQ ID NO: 384, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 434, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 184, the CDR-H2 has an amino acid sequence of SEQ ID NO: 234, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 284, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 34; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 84; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 134, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 334; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 384; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 434, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 184; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 234; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 284, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 533 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 533. WB217 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 35, the CDR-H2 has an amino acid sequence of SEQ ID NO: 85, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 135, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 335, the CDR-H2 has an amino acid sequence of SEQ ID NO: 385, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 435, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 185, the CDR-H2 has an amino acid sequence of SEQ ID NO: 235, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 285, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 35; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 85; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 135, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 335; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 385; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 435, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 185; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 235; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 285, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 534 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 534. WB219 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 36, the CDR-H2 has an amino acid sequence of SEQ ID NO: 86, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 136, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 336, the CDR-H2 has an amino acid sequence of SEQ ID NO: 386, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 436, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 186, the CDR-H2 has an amino acid sequence of SEQ ID NO: 236, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 286, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 36; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 86; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 136, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 336; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 386; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 436, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 186; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 236; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 286, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 535 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 535. WB220 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 37, the CDR-H2 has an amino acid sequence of SEQ ID NO: 87, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 137, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 337, the CDR-H2 has an amino acid sequence of SEQ ID NO: 387, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 437, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 187, the CDR-H2 has an amino acid sequence of SEQ ID NO: 237, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 287, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 37; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 87; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 137, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 337; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 387; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 437, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 187; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 237; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 287, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 536 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 536. WB221 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 38, the CDR-H2 has an amino acid sequence of SEQ ID NO: 88, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 138, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 338, the CDR-H2 has an amino acid sequence of SEQ ID NO: 388, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 438, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 188, the CDR-H2 has an amino acid sequence of SEQ ID NO: 238, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 288, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 38; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 88; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 138, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 338; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 388; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 438, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 188; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 238; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 288, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 537 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 537. WB222 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 39, the CDR-H2 has an amino acid sequence of SEQ ID NO: 89, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 139, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 339, the CDR-H2 has an amino acid sequence of SEQ ID NO: 389, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 439, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 189, the CDR-H2 has an amino acid sequence of SEQ ID NO: 239, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 289, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 39; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 89; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 139, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 339; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 389; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 439, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 189; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 239; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 289, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 538 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 538. WB223 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 40, the CDR-H2 has an amino acid sequence of SEQ ID NO: 90, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 140, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 340, the CDR-H2 has an amino acid sequence of SEQ ID NO: 390, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 440, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 190, the CDR-H2 has an amino acid sequence of SEQ ID NO: 240, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 290, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 40; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 90; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 140, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 340; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 390; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 440, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 190; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 240; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 290, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 539 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 539. WB224 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 41, the CDR-H2 has an amino acid sequence of SEQ ID NO: 91, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 141, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 341, the CDR-H2 has an amino acid sequence of SEQ ID NO: 391, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 441, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 191, the CDR-H2 has an amino acid sequence of SEQ ID NO: 241, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 291, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 41; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 91; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 141, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 341; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 391; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 441, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 191; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 241; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 291, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 540 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 540. WB225 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 42, the CDR-H2 has an amino acid sequence of SEQ ID NO: 92, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 142, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 342, the CDR-H2 has an amino acid sequence of SEQ ID NO: 392, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 442, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 192, the CDR-H2 has an amino acid sequence of SEQ ID NO: 242, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 292, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 42; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 92; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 142, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 342; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 392; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 442, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 192; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 242; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 292, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 541 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 541. WB226 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 43, the CDR-H2 has an amino acid sequence of SEQ ID NO: 93, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 143, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 343, the CDR-H2 has an amino acid sequence of SEQ ID NO: 393, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 443, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 193, the CDR-H2 has an amino acid sequence of SEQ ID NO: 243, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 293, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 43; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 93; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 143, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 343; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 393; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 443, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 193; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 243; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 293, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 542 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 542. WB227 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 44, the CDR-H2 has an amino acid sequence of SEQ ID NO: 94, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 144, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 344, the CDR-H2 has an amino acid sequence of SEQ ID NO: 394, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 444, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 194, the CDR-H2 has an amino acid sequence of SEQ ID NO: 244, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 294, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 44; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 94; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 144, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 344; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 394; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 444, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 194; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 244; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 294, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 543 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 543. WB228 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 45, the CDR-H2 has an amino acid sequence of SEQ ID NO: 95, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 145, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 345, the CDR-H2 has an amino acid sequence of SEQ ID NO: 395, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 445, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 195, the CDR-H2 has an amino acid sequence of SEQ ID NO: 245, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 295, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 45; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 95; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 145, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 345; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 395; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 445, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 195; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 245; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 295, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 544 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 544. WB229 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 46, the CDR-H2 has an amino acid sequence of SEQ ID NO: 96, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 146, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 346, the CDR-H2 has an amino acid sequence of SEQ ID NO: 396, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 446, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 196, the CDR-H2 has an amino acid sequence of SEQ ID NO: 246, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 296, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 46; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 96; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 146, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 346; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 396; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 446, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 196; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 246; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 296, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 545 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 545. WB230 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 47, the CDR-H2 has an amino acid sequence of SEQ ID NO: 97, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 147, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 347, the CDR-H2 has an amino acid sequence of SEQ ID NO: 397, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 447, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 197, the CDR-H2 has an amino acid sequence of SEQ ID NO: 247, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 297, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 47; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 97; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 147, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 347; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 397; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 447, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 197; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 247; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 297, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 546 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 546. WB240 (B12) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 48, the CDR-H2 has an amino acid sequence of SEQ ID NO: 98, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 148, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 348, the CDR-H2 has an amino acid sequence of SEQ ID NO: 398, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 448, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 198, the CDR-H2 has an amino acid sequence of SEQ ID NO: 248, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 298, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 48; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 98; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 148, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 348; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 398; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 448, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 198; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 248; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 298, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 547 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 547. WB263 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 49, the CDR-H2 has an amino acid sequence of SEQ ID NO: 99, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 149, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 349, the CDR-H2 has an amino acid sequence of SEQ ID NO: 399, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 449, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 199, the CDR-H2 has an amino acid sequence of SEQ ID NO: 249, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 299, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 49; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 99; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 149, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 349; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 399; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 449, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 199; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 249; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 299, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 548 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 548. WB267 (H10) In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 50, the CDR-H2 has an amino acid sequence of SEQ ID NO: 100, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 150, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 350, the CDR-H2 has an amino acid sequence of SEQ ID NO: 400, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 450, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence of SEQ ID NO: 200, the CDR-H2 has an amino acid sequence of SEQ ID NO: 250, and the CDR-H3 has an amino acid sequence of SEQ ID NO: 300, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 50; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%,Docket No. WRENCH-001 / WO01 99%, or 100% identical to SEQ ID NO: 100; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 150, wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 350; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 400; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 450, wherein the numbering is according to Chothia. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising: (a) a CDR-H1 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 200; (b) a CDR-H2 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 250; and (c) a CDR-H3 that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 300, wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a single domain IL-18BP binding protein or antibody comprising an amino acid sequence of SEQ ID NO: 549 and that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 549. Antibodies of the disclosure have various beneficial features. In one aspect, the antibody or binding protein prevents the interaction of IL-18BP with IL-18. In one aspect, the single domain anti-IL-18BP antibody does not interfere with IL-18 binding to its receptors, thereby enabling the activity of endogenous IL-18. In one aspect, the receptors are located on effector T cells or NK cells, thereby enabling the activity of endogenous IL-18. In one aspect, the antibody or binding protein restores IL-18-mediated signaling that was inhibited by the interaction of IL-18 and IL-18BP. In one aspect, the antibody or binding protein binds to IL-18BP in a pH- dependent manner. In one aspect, the antibody antagonizes at least one immune inhibitory effect of IL-18BP. In one aspect, the antibody or binding protein blocks the IL-18 : IL-18BP binding interaction. In one aspect, the antibody or binding protein competes for binding with an antibody that binds to human IL-18BP of SEQ ID NO: 555 and / or the secreted chain of human IL-18BP of SEQ ID NO: 556 and or that competes for binding to IL-18. In one aspect, the antibody or binding protein dissociates from IL-18BP within the acidic environment of endosomes, thereby resulting in an increased clearance of IL-18BP. In one aspect the binding affinity of the antibody or binding protein for IL-18BP is pH-sensitive. In one aspect, the pH sensitivity results in a decreased binding affinity for IL-18BP at a pH of 5.8, compared to a pH of 6.5 or 7.4. In one aspect, the binding affinity of the anti-IL-18BP antibody for IL-18BP is 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80- fold, 90-fold, or 100-fold less at a pH of 5.8 or lower, as compared to the binding affinity at a pH of 6.5 or above. In one aspect, the binding affinity of the antibody or binding protein for IL-18BP is 10-fold, 20-fold,Docket No. WRENCH-001 / WO01 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, or 100-fold less at a pH of 5.8 or lower, as compared to the binding affinity at a pH of 7.4 or above. Additional antibodies to human IL-18BP can be done as is well known in the art, using well known methods such as those outlined in the examples. Thus, additional anti-IL-18BP antibodies can be generated by traditional methods such as immunizing mice (sometimes using DNA immunization, for example, such as is used by Aldevron), followed by screening against IL-18BP (including human IL-18BP) protein and hybridoma generation, with antibody purification and recovery. Optional Antibody Engineering The anti-IL-18BP antibodies of the disclosure can be modified, or engineered, to alter the amino acid sequences by amino acid substitutions. In addition to substitutions made to alter binding affinity to FcyRs and / or FcRn and / or increase in vivo serum half-life, additional antibody modifications can be made, as described in further detail below. In some cases, affinity maturation is done. Amino acid modifications in the CDRs are sometimes referred to as “affinity maturation”. An “affinity matured” antibody is one having one or more alteration(s) in one or more CDRs which results in an improvement in the affinity of the antibody for antigen, compared to a parent antibody which does not possess those alteration(s). In some cases, although rare, it may be desirable to decrease the affinity of an antibody to its antigen, but this is generally not preferred. In some embodiments, one or more amino acid modifications are made in one or more of the CDRs of the IL-18BP antibodies of the invention. In general, only 1 or 2 or 3-amino acids are substituted in any single CDR, and generally no more than from 1, 2, 3. 4, 5, 6, 7, 8, 9 or 10 changes are made within a set of CDRs. However, it should be appreciated that any combination of no substitutions, 1, 2, or 3 substitutions in any CDR can be independently and optionally combined with any other substitution. Affinity maturation can be done to increase the binding affinity of the antibody for the IL-18BP antigen by at least about 100% or more, or at least about 104or more, 105more, 106more, 107more, as compared to the “parent” antibody. Preferred affinity matured antibodies will have nanomolar or even picomolar affinities for the IL-18BP antigen. Affinity matured antibodies are produced by known procedures. See, for example, Marks et al., 1992, Biotechnology 10:779-783 that describes affinity maturation by variable heavy chain (VH) and variable light chain (VL) domain shuffling. Random mutagenesis of CDR and / or framework residues is described in: Barbas, et al., PNAS; USA 91:3809-3813 (1994); Shier et al., Gene, 169:147-155 (1995); Yelton et al., J. Immunol., 15S:1994-2004 (1995); Jackson et al, J. Immunol. 154(7):3310-9 (1995); and Hawkins et a / ., J. Mol. Biol., 226:889-896 (1992), for example. Alternatively, amino acid modifications can be made in one or more of the CDRs of the antibodies of the invention that are “silent”, e.g. that do not significantly alter the affinity of the antibody for the antigen. These can be made for a number of reasons, including optimizing expression (as can be done for the nucleic acids encoding the antibodies of the invention).Docket No. WRENCH-001 / WO01 Thus, included within the definition of the CDRs and antibodies of the invention are variant CDRs and antibodies, that is, the antibodies of the invention can include amino acid modifications in one or more of the CDRs of the enumerated antibodies of the invention. In addition, as outlined below, amino acid modifications can also independently and optionally be made in any region outside the CDRs, including framework and constant regions. V. Multi-Specific Binding Proteins Embodiments of the disclosure further provide multispecific binding proteins that can bind to one or more target antigens, such as IL-18BP. In one aspect, provided herein is a multispecific binding protein comprising a first domain and a second domain according to the present disclosure. The multispecific binding protein can, in some instances, bind to two, three, four, or more different proteins. In some embodiments, the first domain comprises a single domain IL-18BP binding protein as described herein. In some embodiments, the second domain, an optional third domain, and / or an optional fourth domain binds to a target molecule that is not IL-18BP. In some embodiments, the second domain, an optional third domain, and / or an optional fourth domain comprise a variant IL18 protein. In some embodiments, the multispecific protein is a bispecific protein. In some embodiments, the multispecific protein is a trispecific protein. In some embodiments, the single domain IL-18BP binding protein described herein and the second domain described herein are coupled via chemical coupling, gene fusion, or a non-covalent association. In some embodiments, the single domain IL-18BP binding protein described herein and the second domain described herein are coupled via chemical coupling. In some embodiments, the single domain IL-18BP binding protein described herein and the second domain described herein are coupled via gene fusion. In some embodiments, the single domain IL-18BP binding protein described herein and the second domain described herein are coupled via non-covalent association. The domain or the domains that do not bind to IL-18BP can bind to a target antigen. The target antigen can be, for example, a cell surface molecule. Cell surface molecules include, but are not limited to, proteins, lipids, and / or polysaccharides. In some embodiments, a target antigen can be present on a tumor cell, a virally infected cell, a bacterially infected cell, a damaged red blood cell, an arterial plaque cell, a fibrotic tissue cell, etc. A target antigen can be involved in and / or associated with a disease, disorder, or condition. In particular, a target antigen can be associated with a proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, a graft-versus-host disease or a host-versus-graft disease. A tumorous disease can be, for example, a cancer. Cancers can be primary cancers or metastatic cancers. In some embodiments, a target antigen is a tumor associated antigen (TAA) expressed on a tumor cell. Alternatively in some embodiments, a target antigen is associated with a pathogen or a parasite (such as a virus, a bacterium, a fungus, etc.), a self-antigen, etc.Docket No. WRENCH-001 / WO01 In some embodiments, a target antigen is a tumor associated antigen (TAA) and the TAA can be, for example, a B-cell maturation antigen (BCMA), carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (Her2), epithelial cell adhesion molecule (EpCAM), CD20, CD26, CD123, CD30, CD33, CD47, CD52, CD133, glycoprotein A33 (gpA33), mucins, tumor associated glycoprotein-72 (TAG-72), type IX collagen (CIX), glutamate carboxypeptidase II (PSMA), folate-binding protein, GD2, GD3, GM2, vascular endothelial growth factor (VEGF), vascular endothelial growth factor receptor (VEGFR), integrin, αVβ3, α5β1, ERBB2, ERBB3, mesenchymal epithelial transition (MET), insulin-like growth factor-I receptor (IGFIR), ephrin type-A receptor 3 (EPHA3), TRAIL receptor 1 (TRAILR1), TRAIL receptor 2 (TRAILR2), receptor activator of nuclear factor kappa beta (RANKL), fibroblast activation protein (FAP), claudin 18.2, mesothelin, receptor tyrosine kinase like orphan receptor 1 (ROR1), epidermal growth factor receptor variant III (EGFRVIII), six-transmembrane epithelial antigen of the prostate-2 (STEAP2), orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), tenascin, etc. In some embodiments, the target antigen is a immune checkpoint such as Cytotoxic T-lymphocyte-associated protein 4 (CTLA-4), Programmed cell death protein 1 (PD-1), Programmed death-ligand 1 (PD-L1), Lymphocyte-activation gene 3 (LAG-3), T cell immunoglobulin and mucin-domain containing-3 (TIM-3), T cell immunoglobulin and ITIM domain (TIGIT), V-domain Ig suppressor of T cell activation (VISTA), IL-18BP, etc.). In some embodiments, the multispecific binding protein can be produced by linking a single domain IL-18BP binding domain described herein and one or more other domain(s) described herein together using a linker. The linker can comprise, for example, a Gly-Ser linker. The length of the linker is such that it can associate intermolecularly two or more domains. Examples of linkers for use in the multispecific binding proteins described herein include, but are not limited to, (GS)n, (GGS)n, (GGGS)n, (GGSG)n, (GGSGG)n, (GGGGS)n, (GGGGG)n, or (GGG)n, wherein, for each, n is 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10. In one instance, the linker can be (GGGGS)4 or (GGGGS)3. A multispecific binding protein can optionally contain an Fc domain. Examples of Fc domains include, but are not limited to, an IgG1, IgG4, etc. Further descriptions of Fc domains fused to embodiments of the disclosure, such as anti-IL-18BP antibodies and variant IL18 proteins, are provided below. A multispecific binding protein, in some embodiments, comprises a half-life extension domain. Examples of half-life extension domains include, but are not limited to, an Fc domain, human serum albumin, or an albumin-targeting polypeptide. Such half-life extension domains improve the utility of the multispecific binding protein. VI. Fusion Proteins Embodiments of the disclosure, such as variant IL-18 proteins, anti-IL-18BP antibodies, and combinations thereof may be fused to an Fc domain, resulting in various novel Fc fusion proteins. The inventor has recognized that such fusion proteins have numerous advantages, including the combination of two mechanisms to enhance IL-18 signaling: 1) stable IL-18 muteins that can activate IL-18 receptors, and 2) anDocket No. WRENCH-001 / WO01 IL-18BP binder that releases endogenous IL-18, thus unleashing the cytokine’s biological activity. In addition, a fusion protein containing an IL-18 mutein that has enhanced stability, and a VHH that exhibits high thermostability, are likely to result in a stable protein with a desirable developability profile. a. Fc Fusion Proteins In one aspect, a fusion protein is a heterodimeric Fc fusion protein. Such a heterodimeric fusion protein includes a first monomer and a second monomer comprising a first Fc domain and a second Fc domain, respectively. As will be described in further detail below, the first and second monomers may further comprise variant IL18 proteins and / or anti-IL-18BP antibodies, thus providing Fc-fusion proteins. As will be appreciated, discussion herein of components of the fusion proteins encompassed by the present disclosure is applicable to both homodimeric and heterodimeric Fc fusion proteins as appropriate, unless otherwise specified. The Fc domains can be derived from IgG Fc domains, e.g., IgG1, IgG2, IgG3 or IgG4 Fc domains, with IgG1 Fc domains finding particular use in the invention. As described herein, IgG1 Fc domains may be used, often, but not always in conjunction with ablation variants to ablate effector function. Similarly, when low effector function is desired, IgG4 Fc domains may be used. In some embodiments, the first Fc domain and second Fc domain comprise complementary pairs of amino acid substitutions that improve thermostability. Such substitutions employ a “knob in hole” strategy in which one domain is modified with a “knob” mutation while the other is modified with a corresponding “hole” mutation (see, e.g., FIG.1A). The knob can refer to a bulky amino acid substitution that creates a protrusion in the Fc region. The “hole” mutation involves a complementary amino acid substitution in the opposing domain of the Fc region, creating a depression or cavity in the Fc region. When the two domains are paired together, the knob from one domain fits into the hole of the other, resulting in a stable heterodimeric fusion protein. Accordingly, in such embodiments, the first Fc domain can comprise a set of amino acid substitutions (the knob) selected from the group consisting of S354C and T366W. In such embodiments, the second Fc domain can comprise a set of amino acid substitutions (the hole) selected from the group consisting of Y349C, T366S, L368A, and Y407V. In some embodiments, the Fc Knob is selected from Table 14 (SEQ ID NO: 567). In some embodiments, the Fc Hole is selected from Table 14 (SEQ ID NO: 568). In some embodiments, the Fc is selected from Table 14 (SEQ ID NO: 569). In some embodiments, the Fc Knob is at least 90%, 95%, 98%, 99%, or 100% identical to its sequence from Table 14 (SEQ ID NO: 567). In some embodiments, the Fc Hole is at least 90%, 95%, 98%, 99%, or 100% identical to its sequence from Table 14 (SEQ ID NO: 568). In some embodiments, the Fc is at least 90%, 95%, 98%, 99%, or 100% identical to its sequence from Table 14 (SEQ ID NO: 569). For any of the dimeric fusion proteins described herein, the carboxy-terminal portion of each chain defines a constant region primarily responsible for effector function. Kabat et al. collected numerous primary sequences of the variable regions of heavy chains and light chains. Based on the degree of conservation of the sequences, they classified individual primary sequences into the CDRs and the framework and made a listDocket No. WRENCH-001 / WO01 thereof (see SEQUENCES OF IMMUNOLOGICAL INTEREST, 5thedition, NIH publication, No.91-3242, E A. Kabat et al, entirely incorporated by reference). Throughout the present specification, the Kabat numbering system is generally used when referring to a residue in the variable domain (approximately, residues 1-107 of the light chain variable region and residues 1-113 of the heavy chain variable region) and the EU numbering system for Fc regions (e.g., Kabat et al, supra (1991)). In the IgG subclass of immunoglobulins, there are several immunoglobulin domains in the heavy chain. By “immunoglobulin (Ig) domain” herein is meant a region of an immunoglobulin having a distinct tertiary structure. Of interest in the present Fc fusion proteins are the heavy chain domains, including the constant heavy (CH) domains and the hinge domains. In the context of IgG antibodies, the IgG isotypes each have three CH regions. Accordingly, “CH” domains in the context of IgG are as follows: “CH1” refers to positions 118-215 according to the EU index as in Kabat. “Hinge” refers to positions 216-230 according to the EU index as in Kabat. “CH2” refers to positions 231-340 according to the EU index as in Kabat, and “CH3” refers to positions 341-447 according to the EU index as in Kabat. As shown in Table 1 below, the exact numbering and placement of the heavy chain domains can be different among different numbering systems. As shown herein and described below, the pI variants can be in one or more of the CH regions, as well as the hinge region, discussed below. Table 1 EU Numbering Kabat NumberingAs discussed herein, amino acid substitutions can be made to alter functional properties of fusion proteins. For example, proteins or single-domain antibodies fused to an Fc region may be engineered to include modifications within the Fc region, typically to alter one or more functional properties of the antibody, such as serum half-life, complement fixation, Fc receptor binding, and / or antigen-dependent cellular cytotoxicity. In some embodiments, each of the first and second monomers include an Fc domain that has the formula hinge-CH2-CH3. In some embodiments, each of the first and second monomers include an Fc domain that has the formula CH2-CH3. In some embodiments, amino acid substitutions can be made in the Fc region, in general for altering binding to FcγR receptors. By “Fc gamma receptor”, “Fcγ”, or “Fcgamma” as used herein is meant any member of the family of proteins that bind the IgG antibody Fc region and is encoded by an FcγR gene. In humans this family includes but is not limited to FcγRI (CD64), including isoforms FcγRIa, FcγRlb, and FcγRIc, FcγRII (CD32), including isoforms FcyRlla (including allotypes H I 3 l and R131), FcγRIIb (including FcγRIIb-i andDocket No. WRENCH-001 / WO01 FcγRIIb-2), and FcγRIIc; and FcTRIII (CD l6), including isoforms FcyRIIIa (including allotypes V158 and F158) and FcγRIIIb (including allotypes FcγRIIIb-NA I and FcγRIIIb-NAZ) (Jefferis et al, 2002, Immunol Lett 82:57-65, entirely incorporated by reference), as well as any undiscovered human FcγRs or FcγR isoforms or allotypes. An FcγR may be from any organism, including but not limited to humans, mice, rats, rabbits, and monkeys. Mouse FcγRs include but are not limited to FcγRI (CD64), FcγRII (CD32), FcγRIII-I (CD16), and FcγRIII-2 (CD16-2), as well as any undiscovered mouse FcγRs or FcγR isoforms or allotypes. There are a number of useful Fc substitutions that can be made to alter binding to one or more of the FcγR receptors. Substitutions that result in increased binding as well as decreased binding can be useful. For example, it is known that increased binding to FcγRIIIa generally results in increased ADCC (antibody dependent cell-mediated cytotoxicity; the cell mediated reaction wherein nonspecific cytotoxic cells that express FcγRs recognize bound antibody on a target cell and subsequently cause lysis of the target cell. Similarly, decreased binding to FcγRIIb (an inhibitory receptor) can be beneficial as well in some circumstances. Amino acid substitutions that find use in the present invention include those listed in U. S. Ser. No.11 / 124,620 (particularly FIG.41) and U.S. Patent No.6,737,056, both of which are expressly incorporated herein by reference in their entirety and specifically for the variants disclosed therein. Particular variants that find use include, but are not limited to, 236A, 239D, 239E, 332E, 332D, 239D / 332E, 267D, 267E, 328F, 267E / 328F, 236A / 332E, 239D / 332E / 330Y, 239D, 332E / 330L, 299T and 297N. In addition, the fusion proteins of the invention may be modified to increase their biological half-life. Various approaches are possible. For example, one or more of the following mutations can be introduced: T252L, T254S, T256F, as described in U.S. Pat. No.6,277,375 to Ward. Alternatively, to increase the biological half-life, the Fc region can be altered within the CH1 or CL region to contain a salvage receptor binding epitope taken from two loops of a CH2 domain of an Fc region of an IgG, as described in U.S. Pat. Nos.5,869,046 and 6,121,022 by Presta et al. Additional mutations to increase serum half-life are disclosed in U.S. Patent Nos. 8,883,973, 6,737,056 and 7,371,826, and include 428L, 434A, 434S, and 428L / 434S. In yet other embodiments, the Fc region is altered by replacing at least one amino acid residue with a different amino acid residue to alter the effector functions of the antibody. For example, one or more amino acids selected from amino acid residues 234, 235, 236, 237, 297, 318, 320 and 322 can be replaced with a different amino acid residue such that the antibody has an altered affinity for an effector ligand but retains the antigen-binding ability of the parent antibody. The effector ligand to which affinity is altered can be, for example, an Fc receptor or the C1 component of complement. This approach is described in further detail in U S. Pat Nos.5,624,821 and 5,648,260, both by Winter et al. In another example, one or more amino acids selected from amino acid residues 329, 331, and 322 can be replaced with a different amino acid residue such that the fusion protein has altered Clq binding and / or reduced or abolished complement dependent cytotoxicity (CDC). This approach is described in further detail in U.S. Pat Nos.6,194,551 by Idusogie et al. In another example, one or more amino acid residues within aminoDocket No. WRENCH-001 / WO01 acid positions 231 and 239 are altered to thereby alter the ability of the fusion protein to fix complement. This approach is described further in PCT Publication WO 94 / 29351 by Bodmer et al. In yet another example, the Fc region is modified to increase the ability of the antibody to mediate antibody dependent cellular cytotoxicity (ADCC) and / or to increase the affinity of the antibody for an FcY receptor by modifying one or more amino acids at the following positions: 238, 239, 248, 249, 252, 254, 255, 256, 258, 265, 267, 268, 269, 270, 272, 276, 278, 280, 283, 285, 286, 289, 290, 292, 293, 294, 295, 296, 298, 301, 303, 305, 307, 309, 312, 315, 320, 322, 324, 326, 327, 329, 330, 331, 333, 334, 335, 337, 338, 340, 360, 373, 376, 378, 382, 388, 389, 398, 414, 416, 419, 430, 434, 435, 437, 438, or 439. This approach is described further in PCT Publication WO 00 / 42072 by Presta. Moreover, the binding sites on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn have been mapped and variants with improved binding have been described (see Shields, R. L. et al. (2001) J. Biol. Chem.276:6591-6604). Specific mutations at positions 256, 290, 298, 333, 334 and 339 are shown to improve binding to FcγRIII. Additionally, the following combination mutants are shown to improve FcγRIII binding: T256A / S298A, S298A / E333A, S298A / K224A, and S298A / E333A / K334A Furthermore, mutations such as M252Y / SZ54T / TZ56E or M428L / N434S improve binding to FcRn and increase antibody circulation half-life (see Chan CA and Carter PJ (2010) Nature Rev. Immunol.10:301-316). In some embodiments, specific residues of an Fc region fused to one or more proteins or antibodies of the disclosure are mutated to exhibit higher affinity to FcRn at a pH of 6 or below, e.g., pH 5.8. After being taken up into cells via pinocytosis or receptor-mediated endocytosis, antibodies are sorted into endosomes. Within the slightly acidic environment of the endosome, the Fc may bind to FcRn, protecting the antibody from degradation. The antibody-FcRn complex may then be recycled back to the cell surface, where it is released into the bloodstream. Such Fc mutations will thus result in increased half-life of the fusion protein. Accordingly, an increased affinity for FcRn at a pH of 6 or below will increase the percentage of antibodies that are recycled and reused, increasing potency. In some embodiments, the Fc will comprise modifications at one or more amino acids position selected from the group consisting of M252, S254, T256, T307, L309, M428 and N434, as compared to wild-type Fc. In one embodiment, the variant Fc has a modification at M252, S254, T256. In one embodiment, the variant Fc has a modification at M428 and L434. In one embodiment, the variant Fc has a modification at M252 and M428. In one embodiment, the variant Fc has a modification at M252, S254, and N434. In one embodiment, the variant Fc has a modification at T307 and M428. In one embodiment, the variant Fc has a modification at T307 and N434. In one embodiment, the variant Fc has a modification at L309 and M428. In one embodiment, the variant Fc has a modification at L309 and N434. In such embodiments, the modifications increase the affinity of the fusion protein to FcRn at a pH of 6 or below, e.g., a pH of 5-6. In some embodiments, the variant Fc-VHH fusion protein will exhibit increased thermostability by 1, 2, 5, and up to 10C compared to the wildtype Fc. In some embodiments, the variant Fc-VHH fusion protein will exhibit decreased thermostability by 1, 2, 5 and up to 10C compared to the wildtype Fc. In some embodiments, the variant Fc-VHH fusion will exhibit increased half-life, including human FcRn transgenic mice, as compared to a corresponding wild-type Fc-VHH fusion. In some embodiments, the combination ofDocket No. WRENCH-001 / WO01 the pH-sensitive binding to IL-18BP and Fc variants will augment the clearance of IL-18BP. In some embodiments, the combination of the pH-sensitive binding to IL-18BP and Fc variants will augment the clearance of IL-18BP from human FcRn transgenic mice. In still another embodiment, the glycosylation of a fusion protein is modified. For example, an aglycosylated Fc region can be made (i.e., the antibody lacks glycosylation). Glycosylation can be altered to, for example, increase the affinity of a single domain antibody of the disclosure for antigen or reduce effector function such as ADCC. Such carbohydrate modifications can be accomplished by, for example, altering one or more sites of glycosylation within the antibody sequence, for example N297. For example, one or more amino acid substitutions can be made that result in elimination of one or more variable region framework glycosylation sites to thereby eliminate glycosylation at that site. Additionally or alternatively, a fusion protein can be made that has an altered type of glycosylation, such as a hypofucosylated Fc region having reduced amounts of fucosyl residues or an antibody having increased bisecting GlcNac structures. Such altered glycosylation patterns have been demonstrated to increase the ADCC ability of antibodies. Such carbohydrate modifications can be accomplished by, for example, expressing the fusion protein in a host cell with altered glycosylation machinery. Cells with altered glycosylation machinery have been described in the art and can be used as host cells in which to express recombinant antibodies according to at least some embodiments of the invention to thereby produce an antibody with altered glycosylation. For example, the cell lines Ms704, Ms705, and Ms709 lack the fucosyltransferase gene, FUT8 (u (1,6) fucosyltransferase), such that antibodies expressed in the Ms704, Ms705, and Ms709 cell lines lack fucose on their carbohydrates. The Ms704, Ms705, and Ms709 FUT8 cell lines are created by the targeted disruption of the FUT8 gene in CHO / DG44 cells using two replacement vectors (see U.S. Patent Publication No. 20040110704 by Yamane et al. and Yamane-Ohnuki et al. (2004) Biotechnol Bioeng 87:614- 22). As another example, EP 1,176,195 by Hanai et al. describes a cell line with a functionally disrupted FUT8 gene, which encodes a fucosyl transferase, such that antibodies expressed in such a cell line exhibit hypofucosylation by reducing or eliminating the α 1,6 bond-related enzyme. Hanai et al also describe cell lines which have a low enzyme activity for adding fucose to the N-acetylglucosamine that binds to the Fc region of the antibody or does not have the enzyme activity, for example the rat myeloma cell line YB2 / 0 (ATCC CRL 1662). PCT Publication WO 03 / 035835 by Presta describes a variant CHO cell line, Lec13 cells, with reduced ability to attach fucose to Asn(297)-linked carbohydrates, also resulting in hypofucosylation of antibodies expressed in that host cell (see also Shields, R. L. et al. (2002) J. Biol. Chem. 277.26733-26740). PCT Publication WO 99 / 54342 by Umana et al. describes cell lines engineered to express glycoprotein-modifying glycosyl transferases (e.g., β(1,4)-N-acetylglucosaminyltransferase III (GnTIII)) such that antibodies expressed in the engineered cell lines exhibit increased bisecting GlcNac structures which results in increased ADCC activity of the antibodies (see also Umana et al. (1999) Nat. Biotech. 17:176-180). Alternatively, the fucose residues of the antibody may be cleaved off using a fucosidase enzyme. For example, the fucosidase u-L- fucosidase removes fucosyl residues from antibodies (Tarentino, A L. et al (1975) Biochem.14:5516-23).Docket No. WRENCH-001 / WO01 Another modification of fusion proteins herein that is contemplated by the invention is pegylation or the addition of other water-soluble moieties, typically polymers, e.g., in order to enhance half-life. An Fc region can be pegylated to, for example, increase the biological (e.g., serum) half-life of the fusion protein. To pegylate a fusion protein, the fusion protein, or fragment thereof, typically is reacted with polyethylene glycol (PEG), such as a reactive ester or aldehyde derivative of PEG, under conditions in which one or more PEG groups become attached to the fusion protein or fragment. Preferably, the pegylation is carried out via an acylation reaction or an alkylation reaction with a reactive PEG molecule (or an analogous reactive water-soluble polymer) As used herein, the term “polyethylene glycol” is intended to encompass any of the forms of PEG that have been used to derivatize other proteins, such as mono (C1-C10) alkoxy- or aryloxy-polyethylene glycol or polyethylene glycol-maleimide. In certain embodiments, the fusion protein to be pegylated is an aglycosylated fusion protein. Methods for pegylating proteins are known in the art and can be applied to the fusion proteins according to at least some embodiments of the invention. See for example, EP 0154316 by Nishimura et al. and EP 0401384 by Ishikawa et al. b. Variant IL-18-Fc Fusion Proteins In some aspects, provided herein are variant IL-18-Fc fusion proteins that include a first monomer that includes a variant human IL-18 protein as described herein and a first Fc domain, and a second monomer that includes a second Fc domain. The variant IL-18-Fc fusion proteins are based on the self-assembling nature of the two Fc domains on each monomer leading to variant IL-18-Fc fusion proteins. Heterodimeric IL-18-Fc fusions may be made by altering the amino acid sequence of each monomer as more fully discussed herein. Embodiments of IL-18-Fc fusion proteins as described herein can include a variant IL-18 protein. In some embodiments, the IL-18-Fc fusion protein is a monovalent IL-18-Fc fusion protein that includes one variant IL-18. In such embodiments, the first Fc domain and second Fc domain are configured in an asymmetrical manner. In such embodiments, the first monomer includes an Fc domain and an IL-18 and the second monomer includes an Fc domain alone (i.e., no IL-18, an “empty Fc domain”). In some embodiments, the IL-18-Fc fusion protein is a bivalent IL-18-Fc fusion protein that includes two variant IL-18s. In some embodiments, the IL-18-Fc fusion protein is a tetravalent IL-18-Fc fusion protein that includes four variant IL- 18s. In one aspect, the variant IL-18-Fc fusion protein is a heterodimeric Fc fusion protein. Such heterodimeric variant IL-18-Fc fusion protein include a first monomer and a second monomer, each having an Fc domain with different amino acid sequences (e.g., a monovalent variant IL-18-Fc fusion protein). As will be appreciated, discussion herein of components of the variant IL-18-Fc fusion proteins encompassed by the present disclosure is applicable to both homodimeric and heterodimeric Fc fusion proteins as appropriate, unless otherwise specified. Embodiments of IL-18-Fc fusion proteins as described herein can include a variant IL-18 protein. In some embodiments, the IL-18-Fc fusion protein is a monovalent IL-18-Fc fusion protein that includes one variant IL-18. The variant IL-18s that can be used with the Fc fusion proteins described herein include variantDocket No. WRENCH-001 / WO01 IL-18s that comprise a modification at one or more amino acid positions selected from the group consisting of L9, V11, N14, C38, I49, V62, C68, C76, K79, F101, S117, S119, Y120, Y123, C127, Q154, and E156, as compared to wildtype human IL18; functional fragments of such variant IL-18s; variants of such variant IL- 18s that include 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 additional amino acid modifications; and variants that are at least 90, 91, 92, 93, 95, 95, 96, 97, 98, or 99% identical to such variant IL-18s. In some embodiments, the variant IL-18 protein comprises a modification at one or more amino acid positions selected from the group consisting of L9, E156, K79, Y120, S117, and S119, as compared to wildtype human IL-18. the variant IL-18 protein comprises amino acid substitutions selected from the group consisting of: L9 / E156, V11 / Q154, I49 / V62, V62 / F101, K79 / Y120, K79 / Y123, S117, S119, and N14, as compared to wildtype human IL-18. In some embodiments, the variant IL-18 protein comprises amino acid substitutions at residues C38, C68, C76, and C127. In some embodiments, provided herein is a variant IL-18-Fc fusion protein which is also referred to as “a variant IL-18 x Fab-Fc fusion protein”. Such a variant IL-18 x Fab-Fc fusion protein includes a first monomer containing a variable heavy chain and an Fc domain; a second monomer containing a variant IL-18 protein (e.g., a variant IL18 protein according to embodiments of the disclosure) and an Fc domain, and a third monomer containing a variable light chain such that the variable heavy and light chains form a Fab. In certain embodiments, the variant IL-18 protein comprises a modification at one or more amino acid positions selected from the group consisting of L9, V11, N14, C38, I49, V62, C68, C76, K79, F101, S117, S119, Y120, Y123, C127, Q154, and E156, as compared to wildtype human IL-18. In certain embodiments, the variant IL-18 is directly connected to the Fc domain. In some embodiments, the C-terminus of the IL-18 is directly connected to the N-terminus of the Fc domain. In some embodiments described herein, the variant IL-18 x Fab-Fc fusion protein also includes a second monomer that includes a second Fc domain and a Fab. In certain embodiments, the Fab prevents the interaction of IL-18BP with IL-18. In certain embodiments, the Fab is directly connected to the second Fc domain. In certain embodiments, the Fab is connected to the second Fc domain via a linker, such as but not limited to a domain linker. In some embodiments, the heavy chain of the Fab is directly connected to the second Fc domain. In some embodiments, the heavy chain of the Fab is connected to the second Fc domain via a linker, such as but not limited to a domain linker. In some embodiments, the C-terminus of the heavy chain of the Fab is directly connected to the N-terminus of the second Fc domain. In some embodiments, the light chain of the Fab is not directly connected to the second monomer. In certain embodiments, the light chain of the Fab is not directly connected to the first monomer. In some embodiments, the Fab selectively binds to a tumor associated antigen (TAA). Tumor associated antigens (TAAs) include, but are not limited to, B-cell maturation antigen (BCMA), carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (Her2), epithelial cell adhesion molecule (EpCAM), CD20, CD26, CD123, CD30, CD33, CD47, CD52, CD133, glycoprotein A33 (gpA33), mucins, tumor associated glycoprotein-72 (TAG-72), type IX collagen (CIX), glutamate carboxypeptidase II (PSMA), folate-binding protein, GD2, GD3, GM2, vascular endothelial growth factor (VEGF), vascular endothelial growth factor receptor (VEGFR), integrin, αVβ3, α5β1, ERBB2, ERBB3,Docket No. WRENCH-001 / WO01 mesenchymal epithelial transition (MET), insulin-like growth factor-I receptor (IGFIR), ephrin type-A receptor 3 (EPHA3), TRAIL receptor 1 (TRAILR1), TRAIL receptor 2 (TRAILR2), receptor activator of nuclear factor kappa beta (RANKL), fibroblast activation protein (FAP), claudin 18.2, mesothelin, receptor tyrosine kinase like orphan receptor 1 (ROR1), epidermal growth factor receptor variant III (EGFRVIII), six-transmembrane epithelial antigen of the prostate-2 (STEAP2), orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), tenascin, etc. In some embodiments, the Fab selectively binds to an immune checkpoint such as Cytotoxic T- lymphocyte-associated protein 4 (CTLA-4), Programmed cell death protein 1 (PD-1), Programmed death- ligand 1 (PD-L1), Lymphocyte-activation gene 3 (LAG-3), T cell immunoglobulin and mucin-domain containing-3 (TIM-3), T cell immunoglobulin and ITIM domain (TIGIT), V-domain Ig suppressor of T cell activation (VISTA), IL-18BP, etc.). In some embodiments, the variant IL-18 protein is covalently attached to the N-terminus or the C- terminus of the first or the second Fc domain. In such embodiments, the variant IL-18 protein is covalently attached to the N-terminus or the C-terminus of the first or second Fc domain via a linker, such as a domain linker, such as a glycine-serine linker. While any suitable linker can be used, many embodiments utilize a glycine-serine polymer, including for example (GS)n, (GSGGS)n, (GGGGS)n, and (GGGS)n, where n is an integer of at least one (and generally from 0 to 1 to 2 to 3 to 4 to 5) as well as any peptide sequence that allows for recombinant attachment of the two domains with sufficient length and flexibility to allow each domain to retain its biological function. In some cases, the linker is a charged domain linker. In certain embodiments, the IL-18 fusion protein includes a first monomer, wherein an IL-18 is connected to the Fc domain by a domain linker. In some embodiments, the C-terminus of the IL-18 is connected to the N-terminus of the Fc domain by a domain linker. c. Anti-IL-18BP- Fc Fusion Proteins The present disclosure also provides single-domain anti-IL-18BP antibodies (e.g., VHHs) which are fused with Fc regions to create new bifunctional antibody formats. This fusion strategy combines the antigen- binding specificity of single domain antibodies with the diverse effector functions typically mediated by the Fc region of conventional antibodies. The fusion process can be achieved through various molecular biology techniques, including genetic engineering and recombinant DNA technology. One approach involves genetically linking the coding sequences of VHHs and Fc regions in-frame, enabling their expression as a single polypeptide chain. Alternatively, fusion proteins can be constructed through chemical conjugation or bioconjugation methods, where VHHs and Fc regions are chemically linked post-translationally. These fusion constructs can be designed to optimize the spatial orientation and functional integrity of both domains, ensuring the retention of their individual properties while facilitating synergistic interactions. As described herein, VHHs are defined by their single-variable domain structure, which sets them apart from conventional antibodies characterized by two heavy chains and two light chains. This single-domainDocket No. WRENCH-001 / WO01 architecture imparts unique advantages to VHHs, including their diminutive size, exceptional stability, solubility, and remarkable specificity and affinity for target antigens. The inventors have recognized and appreciated that VHHs, such as those provided herein, are particularly useful as an anti-IL-18BP antibody when fused to an Fc region. Such single-domain antibodies are easier to produce, in part due to a reduction in complexity and lack of unintended VH / VL pairing. Further, up to four VHHs may be fused directly to an Fc, but only two Fabs for IgG. Increasing the possible valency from bivalent to tetravalent is particularly beneficial as a single molecule can bind to more IL-18BP and thus remove it from circulation. In one aspect, provided herein is a VHH-Fc fusion protein which may also be referred to as a “single domain anti-IL-18BP-Fc fusion protein”. Such a VHH-Fc fusion protein includes a first monomer comprising a single domain anti-IL-18BP antibody and a first Fc domain, and a second monomer comprising a second Fc domain. In some embodiments, a VHH-Fc fusion protein comprises (a) a first monomer comprising from N- terminus to C-terminus: a single domain anti-IL-18BP antibody as described herein, and a first Fc domain; and (b) a second monomer comprising a second Fc domain. In some embodiments, the VHH-Fc fusion protein comprises one or more single domain anti-IL-18BP antibodies, such as 1, 2, 3, or 4 single domain anti-IL-18BP antibodies. In some embodiments, the VHH-Fc fusion protein may comprise one or more single domain anti- IL-18BP antibodies, and one or more single domain antibodies that do not bind to IL-18BP. Increasing the number of antibodies per fusion protein results in an increase in the inhibitory ratio between target and fusion protein by increasing the number of relevant binding domains. In some embodiments, the one or more single domain antibodies that do not bind to IL-18BP bind to a tumor-associated antigen (TAA). In some embodiments, the TAA can be any TAA as described herein, e.g., those TAAs with regards to embodiments of multispecific binding proteins as discussed herein. In some embodiments, the VHH selectively binds to an immune checkpoint such as Cytotoxic T-lymphocyte-associated protein 4 (CTLA-4), Programmed cell death protein 1 (PD-1), Programmed death-ligand 1 (PD-L1), Lymphocyte-activation gene 3 (LAG-3), T cell immunoglobulin and mucin-domain containing-3 (TIM-3), T cell immunoglobulin and ITIM domain (TIGIT), V-domain Ig suppressor of T cell activation ( VISTA), IL- 18BP, etc.). In one embodiment, a VHH-Fc fusion protein described herein comprises an amino acid sequence having at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID Nos: 601-603. In some embodiments, the amino acid sequence having at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identity contains substitutions (e.g., conservative substitutions), insertions, or deletions relative to a reference sequence, but retains the ability to bind to DcR3 as of the unmodified sequence. In some embodiments, a total of from 1 to 10 amino acids are substituted, inserted and / or deleted. In some embodiments, substitutions, insertions, or deletions occur in regions outside the complementarity-determining region (CDR).Docket No. WRENCH-001 / WO01 VHH-H10 Fc Fusion Proteins In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises (a) a first monomer comprising from N-terminus to C-terminus: a first single domain anti-IL-18BP antibody or binding protein having an amino acid sequence of SEQ ID NOs: 508-514 or 548-549, and a first Fc domain; and (b) a second monomer comprising a second Fc domain. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises (a) a first monomer comprising from N-terminus to C-terminus: a first single domain anti-IL18-BP antibody or binding protein having an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 508-514 or 548-549, and a first Fc domain; and (b) a second monomer comprising a second Fc domain. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 604. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 604. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 605. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 605. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 606. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 606. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 616. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 616. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 617. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 617. In one aspect, the present disclosure provides a VHH-Fc fusion protein comprising (a) a first monomer comprising from N-terminus to C-terminus: a first single domain anti-IL18-BP antibody or binding protein comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 9-15 or 49-50, the CDR-H2 has an amino acid sequence is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one ofDocket No. WRENCH-001 / WO01 SEQ ID NOs: 59-65 or 99-100, and the CDR-H3 has an amino acid sequence is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 109-115 or 149-150, and a first Fc domain; and (b) a second monomer comprising a second Fc domain; wherein the numbering is according to Kabat. In one aspect, the present disclosure provides a VHH-Fc fusion protein comprising (a) a first monomer comprising from N-terminus to C-terminus: a first single domain anti-IL18-BP antibody or binding protein comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 159-165 or 199-200, the CDR-H2 has an amino acid sequence is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 209-215 or 249-250, and the CDR-H3 has an amino acid sequence is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 259-265 or 299- 300, and a first Fc domain; and (b) a second monomer comprising a second Fc domain; wherein the numbering is according to IMGT. In one aspect, the present disclosure provides a VHH-Fc fusion protein comprising (a) a first monomer comprising from N-terminus to C-terminus: a first single domain anti-IL18-BP antibody or binding protein comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR- H3, wherein the CDR-H1 has an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 309-315 or 349-350, the CDR-H2 has an amino acid sequence is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 359-365 or 399-400, and the CDR-H3 has an amino acid sequence is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 409-415 or 449- 450, and a first Fc domain; and (b) a second monomer comprising a second Fc domain; wherein the numbering is according to Chothia. In one aspect, the first Fc domain is a wild type Fc. In one aspect, the first Fc domain has amino acid substitutions T307E, M428L, and N434A, compared to wild type Fc. In one aspect, the first Fc domain has amino acid substitutions T307E, M428L, and N434A, as compared to wild type Fc. In one aspect, the single domain anti-IL18-BP antibody or binding protein is directly fused to the first Fc domain without a linker. VHH-B12 Fc Fusion Proteins In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises (a) a first monomer comprising from N-terminus to C-terminus: a first single domain anti-IL-18BP antibody or binding protein having an amino acid sequence of any one of SEQ ID NOs: 515-547, and a first Fc domain; and (b) a second monomer comprising a second Fc domain. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises (a) a first monomer comprising from N-terminus to C-terminus: a first single domain anti-IL18-BP antibody or binding protein having an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%,Docket No. WRENCH-001 / WO01 or 100% identical to any one of SEQ ID NOs: 515-547 and a first Fc domain; and (b) a second monomer comprising a second Fc domain. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 601. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 601. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 602. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 602. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 603. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that is at least 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 603. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence of SEQ ID NO: 609. In one aspect, the present disclosure provides a VHH-Fc fusion protein that comprises an amino acid sequence that ...

Claims

Docket No. WRENCH-001 / WO01 CLAIMS 1. A single domain anti-IL-18BP (interleukin-18 binding protein) antibody, comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR-H1 has an amino acid sequence at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID Nos: 1-50, the CDR-H2 has an amino acid sequence at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NO: 51-100, and the CDR-H3 has an amino acid sequence at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NO: 101-150, wherein the numbering is according to Kabat.

2. The single domain anti-IL18BP antibody of claim 1, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 9, the CDR-H2 has an amino acid sequence of any one of SEQ ID Nos: 59-65 or 99-100, and the CDR-H3 has an amino acid sequence of A-R-P-Z1-Z2-H-Z3-P-Z4-Z5-Z6-I-Y-P-Z7- W, wherein Z1 is T, R, H, S, A, or P; Z2 is K or R; Z3 is V, L, I, or R; Z4 is H or N; Z5 is R, E, A, K, F, T, G, L, or I; Z6 is N, R, or S; and Z7 is R, L, or H; wherein the numbering is according to Kabat.

3. The single domain anti-IL18BP antibody of claim 2, wherein the single domain anti-IL18-BP antibody has an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NOs: 508, 514, or 548-549.

4. The single domain anti-IL18BP antibody of claim 1, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 16, the CDR-H2 has an amino acid sequence of A-I-X1-X2-X3-X4-G- X5-T-Y-Y, wherein X1 is Y, H, D, N, P, or R; X2 is K, E, N, Q, T, P, or R; X3 is D, A, G, H, N, or V; X4 is G, A, D, P, R, or V; and X5 is K, Q, E, N, R, or T; and the CDR-H3 has an amino acid sequence of S-A-W-G-Z1- Z2-Z3-Z4-P-Z5-Z6-Z7-Z8-W, wherein Z1=K, R, or I; Z2 is S, A, Q, T, L, or E; Z3 is I, T, L, V, N, or Y; Z4 is V, D, G, H, A, N, or R; Z5 is H, N, R, L, or S; Z6 is F or Y; and Z7=Y, H, N, S, A, or D; wherein the numbering is according to Kabat.

5. The single domain anti-IL18BP antibody of claim 4, wherein the single domain anti-IL18-BP antibody has an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NOs: 515, 518, 529, 533, or 547.

6. The single domain anti-IL-18BP antibody of claim 5, wherein the antibody has a binding affinity to human IL-18BP of 0.1 - 10 nM at pH 7.

4.

7. The single domain anti-IL-18BP antibody of claim 5, wherein the antibody specifically binds to human and chimpanzee IL-18BP.

8. The single domain anti-IL-18BP antibody of a claim 5, wherein the antibody does not interfere with IL-18 binding to IL-18 receptors, thereby enabling the activity of endogenous IL-18.

9. The single domain anti-IL-18BP antibody of claim 5, wherein the antibody antagonizes at least one immune inhibitory effect of IL-18BP.

10. A VHH-Fc fusion protein comprising: (a) a first monomer comprising from N-terminus to C-terminus: the single domain anti-IL18-BP antibody of claim 5, and a first Fc domain; andDocket No. WRENCH-001 / WO01 (b) a second monomer comprising a second Fc domain.

11. The VHH-Fc fusion protein of claim 10, wherein the first monomer of (a) comprises a sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NOs: 611 or 615.

12. The VHH-Fc fusion protein of claim 10, wherein the single domain anti-IL18-BP antibody is covalently attached to the first Fc domain without a linker.

13. The VHH-Fc fusion protein of claim 12, wherein the second monomer of (b) has an identical sequence as the first monomer of (a).

14. The VHH-Fc fusion protein of claim 11, wherein the fusion protein has a melting temperature of at least 60C.

15. The fusion protein of claim 11, wherein the fusion protein increases the activity of endogenous IL-18.

16. The fusion protein of claim 11, wherein the fusion protein has improved binding affinity to FcRn compared to IgG1 and IgG4 at a pH of 7-7.

6.

17. The fusion protein of claim 11, wherein the fusion protein has 10x, 20x, or 40x higher binding affinity to FcRn compared to IgG1 and IgG4 at a pH of 7-7.

6.

18. The fusion protein of claim 11, wherein the fusion protein blocks endogenous IL-18BP produced by peripheral blood mononuclear cells.

19. The fusion protein of claim 11, wherein the fusion protein inhibits tumor growth in a mouse tumor model.

20. The fusion protein of claim 11, wherein the fusion protein does not have any treatment-induced toxicity when administered to a mouse tumor model.

21. A variant human IL-18 (interleukin-18) protein, wherein the variant human IL18 protein comprises a modification at one or more amino acid positions selected from the group consisting of L9, V11, N14, C38, I49, V62, C68, C76, K79, F101, S117, S119, Y120, Y123, C127, Q154, and E156, as compared to wildtype human IL18.

22. The variant human IL-18 protein of claim 21, wherein the variant human IL-18 protein comprises an additional 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid modifications.

33. The variant human IL-18 protein of claim 21 or claim 22, wherein the variant IL-18 protein comprises a modification at one or more amino acid positions selected from the group consisting of L9, E156, K79, Y120, S117, and S119, as compared to wildtype human IL-18.

24. The variant human IL1-8 protein of any one of claims 21-23, wherein the variant IL-18 protein further comprises amino acid substitutions at residues C38 and / or C68, as compared to wildtype human IL-18.

25. The variant human IL-18 protein of claim 24, wherein the variant IL-18 protein further comprises an amino acid substitution at residue C127, as compared to wildtype human IL-18.

26. The variant human IL-18 protein of claim 24 or claim 25, wherein the variant IL-18 protein further comprises an amino acid substitution resulting in a cysteine residue, wherein that cysteine residue forms a disulfide bond with C76 or C127.Docket No. WRENCH-001 / WO01 27. The variant human IL-18 protein of claim 26, wherein the amino acid substitution resulting in a cysteine residue comprises S117C or S119C, wherein that cysteine residue forms a disulfide bond with C76.

28. The variant human IL-18 protein of claim 26, wherein the amino acid substitution resulting in a cysteine residue comprises N14C, wherein that C forms a disulfide bond with C127.

29. The variant human IL-18 protein of any one of claims 26-28, wherein the amino acid substitution resulting in a cysteine is positioned within 3, 2, or 1 angstroms of C76 or C127.

30. The variant human IL-18 protein of any one of claims 21-24, wherein the variant IL18 protein comprises amino acid substitutions at residues C38, C68, C76, and C127.

31. The variant human IL-18 protein of any one of claims 21-30, wherein the variant IL-18 protein comprises amino acid substitutions selected from the group consisting of: L9 / E156, V11 / Q154, I49 / V62, V62 / F101, K79 / Y120, K79 / Y123, S117, S119, and N14.

32. The variant human IL-18 protein of any one of claims 21-31 wherein the variant human IL18 protein has improved thermostability compared to wildtype human IL-18.

33. The variant human IL-18 protein of claim 32, wherein the variant human IL-18 protein has a melting temperature of at least 60C.

34. The variant human IL18 protein of claim 33, wherein the variant human IL18 protein has a melting temperature of at least 70C.

35. The variant human IL-18 protein of any one of claims 21-34, wherein the variant human IL18 protein has an improved ability to activate IL-18 receptor-mediated signaling with , as compared to wildtype human IL-18.

36. The variant human IL-18 protein of any one of claims 21-35, wherein the modification at one or more amino acid positions comprises a substitution resulting in a cysteine residue.

37. The variant human IL-18 protein of claim 36, wherein the cysteine residue forms a disulfide bond within the variant human IL-18 protein, thereby improving thermostability.

38. The variant human IL-18 protein according to any one of claims 21-37, wherein the variant human IL- 18 protein exhibits increased activation of the IL-18 receptor-mediated signaling compared to wildtype IL-18, optionally wherein the variant IL-18 protein comprises an amino acid substitution of S117C.

39. The variant human IL-18 protein according to any one of claims 21-37, wherein the variant human IL- 18 protein exhibits decreased activation of the IL-18 receptor-mediated signaling compared to wildtype IL-18, optionally wherein the variant IL18 protein comprises an amino acid substitution N14C.

40. The variant human IL-18 protein according to any one of claims 21-39, wherein the variant human IL- 18 protein exhibits improved production yield compared to wildtype human IL18.

41. A pharmaceutical composition comprising (a) the variant human IL-18 protein of any one of claims 1- 20 and (b) a pharmaceutically acceptable carrier.

42. A nucleic acid encoding the composition comprising a variant human IL-18 protein of any one of claims 21-40.Docket No. WRENCH-001 / WO01 43. An expression vector comprising the nucleic acid of claim 42.

44. A host cell comprising the nucleic acid of claim 42 or the expression vector of claim 43.

45. A method of making a variant human IL-18 protein comprising culturing the host cell of claim 44 and recovering the variant human IL-18 protein from the cell culture.

46. A single domain anti-IL-18BP (interleukin-18 binding protein) antibody, comprising a variable heavy chain complementarity-determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR-H1 has an amino acid sequence at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID Nos: 1-50, the CDR-H2 has an amino acid sequence at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NO: 51-100, and the CDR-H3 has an amino acid sequence at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NO: 101-150, wherein the numbering is according to Kabat.

47. A single domain anti-IL-18BP antibody, wherein the single domain anti-IL-18BP antibody is at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NOs: 500-549.

48. A single domain anti-IL-18BP antibody, wherein the single domain anti-IL-18BP antibody is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 533 or 547.

49. A single domain anti-IL18BP antibody, comprising a variable heavy chain complementarity- determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 16, the CDR-H2 has an amino acid sequence of A-I-X1-X2-X3-X4-G- X5-T-Y-Y, wherein X1 is Y, H, D, N, P, or R; X2 is K, E, N, Q, T, P, or R; X3 is D, A, G, H, N, or V; X4 is G, A, D, P, R, or V; and X5 is K, Q, E, N, R, or T; and the CDR-H3 has an amino acid sequence of S-A-W-G-Z1- Z2-Z3-Z4-P-Z5-Z6-Z7-Z8-W, wherein Z1=K, R, or I; Z2 is S, A, Q, T, L, or E; Z3 is I, T, L, V, N, or Y; Z4 is V, D, G, H, A, N, or R; Z5 is H, N, R, L, or S; Z6 is F or Y; and Z7=Y, H, N, S, A, or D; wherein the numbering is according to Kabat.

50. A single domain anti-IL18BP antibody, comprising a variable heavy chain complementarity- determining region 1 (CDR-H1), a CDR-H2, and a CDR-H3, wherein the CDR-H1 has an amino acid sequence at least 90% identical to SEQ ID NO: 9, the CDR-H2 has an amino acid sequence of any one of SEQ ID Nos: 59-65 or 99-100, and the CDR-H3 has an amino acid sequence of A-R-P-Z1-Z2-H-Z3-P-Z4-Z5-Z6-I-Y-P-Z7- W, wherein Z1 is T, R, H, S, A, or P; Z2 is K or R; Z3 is V, L, I, or R; Z4 is H or N; Z5 is R, E, A, K, F, T, G, L, or I; Z6 is N, R, or S; and Z7 is R, L, or H; wherein the numbering is according to Kabat.

51. The single domain anti-IL-18BP antibody of any one of claims 46-50, wherein the antibody dissociates from IL-18BP within the acidic environment of endosomes, thereby resulting in an increased clearance of IL- 18BP.

52. The single domain anti-IL-18BP antibody of any one of claims 46-51, wherein the antibody specifically binds to IL-18BP.

53. The single domain anti-IL-18BP antibody of claim 52, wherein the antibody specifically binds to human IL-18BP.Docket No. WRENCH-001 / WO01 54. The single domain anti-IL-18BP antibody of claim 53, wherein the antibody has a binding affinity to human IL-18BP of 0.1 - 10 nM at pH 7.

4.

55. The single domain anti-IL-18BP antibody of claim 53, wherein the antibody specifically binds to mouse IL-18BP.

56. The single domain anti-IL-18BP antibody of claim 53, wherein the antibody specifically binds to chimpanzee IL-18BP.

57. The single domain anti-IL-18BP antibody of claim 53, wherein the antibody specifically binds to human and chimpanzee IL-18BP.

58. The single domain anti-IL-18BP antibody of any one of claims 46-57, wherein the binding affinity of the IL-18BP antibody for IL-18BP is pH-sensitive.

59. The single domain anti-IL-18BP antibody of claim 58, wherein the antibody has a decreased binding affinity for IL-18BP in acidic conditions.

60. The single domain anti-IL-18BP antibody of claim 58 or claim 59, wherein the antibody has a decreased binding affinity for IL-18BP at a pH of 5.8, compared to a pH of 6.5-7.

4.

61. The single domain anti-IL-18BP antibody of any one of claims 58-60, wherein the binding affinity of the anti-IL-18BP antibody for IL-18BP is 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, or 100-fold less at a pH of 5.0-5.8, compared to the binding affinity at a pH of 6.5-7.

4.

62. The single domain anti-IL-18BP antibody of any one of claims 58-61, wherein the binding affinity of the anti-IL-18BP antibody for IL-18BP is 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, or 100-fold less at a pH of 5.8 or lower, as compared to the binding affinity at a pH of 7.4 or above.

63. The single domain anti-IL-18BP antibody according to any one of claims 46-62, wherein the anti-IL- 18BP antibody exhibits a binding affinity or KD of less than 50 nM, 40 nM, 30 nM, 20nM, 10nM, 5nM, 1nM, or 100pM at pH 6.5 – 7.

4.

64. The single domain anti-IL-18BP antibody according to any one of claims 46-63, wherein the anti-IL- 18BP antibody exhibits a binding affinity or KD of less 10nM, 5nM, 1nM, or 100pM at pH 6.5 – 7.

4.

65. The single domain anti-IL-18BP antibody according to any one of claims 46-64, wherein the anti-IL- 18BP antibody exhibits a binding affinity or KD of less than 1nM, or 100pM at pH 6.5 – 7.

4.

66. The single domain anti-IL-18BP antibody of any one of claims 46-65, wherein the antibody prevents the interaction of IL-18BP with IL-18.

67. The single domain anti-IL-18BP antibody of any one of claims 46-66, wherein the antibody does not interfere with IL-18 binding to IL-18 receptors, thereby enabling the activity of endogenous IL-18.

68. The single domain anti-IL-18BP antibody of claim 67, wherein the IL-18 receptors are located on effector T cells or NK cells, thereby enabling the activity of endogenous IL-18.

69. The single domain anti-IL-18BP antibody of any one of claims 46-68, wherein the antibody restores IL-18-mediated signaling that was inhibited by the interaction of IL-18 and IL-18BP.Docket No. WRENCH-001 / WO01 70. The single domain anti-IL-18BP antibody of any one of claims 46-69, wherein the antibody antagonizes at least one immune inhibitory effect of IL-18BP.

71. The single domain anti-IL-18BP antibody of any one of claims 46-70, wherein the antibody blocks the IL-18 : IL-18BP binding interaction.

72. The single domain anti-IL-18BP antibody of any one of claim 46-71, wherein the antibody competes for binding with an antibody that binds to human IL-18BP of SEQ ID NO: 555 and / or the secreted chain of human IL-18BP of SEQ ID NO: 556 and / or that competes for binding to IL-18.

73. The single domain anti-IL-18BP antibody of any one of claims 46-72 that is non-naturally occurring.

74. The single domain anti-IL-18BP antibody of any one of claims 46-73, further comprising a Fc domain.

75. The single domain anti-IL-18BP antibody of claim 74, wherein the Fc domain is covalently attached to the single-domain anti-IL-18BP antibody without a linker.

76. The single domain anti-IL-18BP antibody of any one of claims 46-75, further comprising a half-life extension domain.

77. The single domain anti-IL-18BP antibody of claim 76, wherein the half-life extension domain comprises an albumin-targeting polypeptide.

78. A composition comprising the single domain anti-IL-18BP antibody of any one of claims 46-77.

79. A pharmaceutical composition comprising (a) the single domain anti-IL-18BP antibody of any one of claims 46-77 and (b) a pharmaceutically acceptable carrier.

80. One or more nucleic acids encoding the single domain anti-IL-18BP antibody of any one of claims 46- 77.

81. An expression vector comprising the one or more nucleic acids of claim 80.

82. A host cell comprising the one or more nucleic acids of claim 60 or the expression vector of claim 81.

83. A method of making a single domain anti-IL-18BP antibody comprising culturing the host cell of claim 82 and recovering the single domain anti-IL-18BP antibody from the cell culture.

84. A multispecific binding protein, comprising a first domain and a second domain, wherein: (a) the first domain comprises a variant human IL-18 protein of any one of claims 1-20; and (b) the second domain comprises a single domain anti-IL-18BP antibody of any one of claims 26-57.

85. A multispecific binding protein, comprising a first domain and a second domain, wherein: (a) the first domain comprises the single-domain anti-IL-18BP antibody of any one of claims 26-57; and (b) the second domain binds to a target molecule that is not IL-18BP.

86. The multispecific binding protein of claim 85, wherein the second domain selectively binds to a tumor associated antigen (TAA).

87. The multispecific binding protein of claim 86, wherein the TAA is selected from the group consisting of B-cell maturation antigen (BCMA), carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (Her2), epithelial cell adhesion molecule (EpCAM), CD20,Docket No. WRENCH-001 / WO01 CD26, CD123, CD30, CD33, CD47, CD52, CD133, glycoprotein A33 (gpA33), mucins, tumor associated glycoprotein-72 (TAG-72), type IX collagen (CIX), glutamate carboxypeptidase II (PSMA), folate-binding protein, GD2, GD3, GM2, vascular endothelial growth factor (VEGF), vascular endothelial growth factor receptor (VEGFR), integrin, αVβ3, α5β1, ERBB2, ERBB3, mesenchymal epithelial transition (MET), insulin- like growth factor-I receptor (IGFIR), ephrin type-A receptor 3 (EPHA3), TRAIL receptor 1 (TRAILR1), TRAIL receptor 2 (TRAILR2), receptor activator of nuclear factor kappa beta (RANKL), fibroblast activation protein (FAP), claudin 18.2, mesothelin, receptor tyrosine kinase like orphan receptor 1 (ROR1), epidermal growth factor receptor variant III (EGFRVIII), six-transmembrane epithelial antigen of the prostate-2 (STEAP2), orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), and tenascin.

88. The multispecific binding protein of any one of claims 84-87, wherein the first domain and the second domain are coupled via chemical coupling, gene fusion, or a non-covalent association.

89. The multispecific binding protein of any one of claims 84-88, further comprising a linker.

90. The multispecific binding protein of claim 89, wherein the linker comprises a glycine-serine linker.

91. The multispecific binding protein of claim 90, wherein the glycine-serine linker comprises a sequence of (GS)n, wherein n = 1 to 10.

92. The multispecific binding protein of claim 90, wherein the linker comprises (GS)n, (GGS)n, (GGGS)n, (GGSG)n, (GGSGG)n, (GGGGS)n, (GGGGG)n, or (GGG)n, wherein n = 1 to 10.

93. The multispecific binding protein of claim 90, wherein the linker comprises (GGGGS)4 or (GGGGS)3.

94. The multispecific binding protein of any one of claims 84-93, wherein the multispecific binding protein is a bispecific protein.

95. The multispecific binding protein of any one of claims 84-95, wherein the multispecific binding protein is a trispecific protein.

96. The multispecific binding protein of any one of claims 84-96, wherein the multispecific binding protein binds to four different target molecules.

98. The multispecific binding protein of any one of claims 84-97, further comprising a Fc domain.

99. The multispecific binding protein of any one of claims 84-98, further comprising a half-life extension domain.

100. The multispecific binding protein of claim 99, wherein the half-life extension domain comprises an albumin-targeting polypeptide.

101. The multispecific binding protein of any one of claims 84-100 that is non-naturally occurring.

102. A pharmaceutical composition comprising (a) the multispecific binding protein of any one of claims 84-101 and (b) a pharmaceutically acceptable carrier.

103. One or more nucleic acids encoding the multispecific binding protein of any one of claims 84-101.

104. An expression vector comprising the one or more nucleic acids of claim 103.

105. A host cell comprising the one or more nucleic acids of claim 83 or the expression vector of claim 104.Docket No. WRENCH-001 / WO01 106. A method of making a multispecific binding protein comprising culturing the host cell of claim 105 and recovering the multispecific binding protein from the cell culture.

107. A variant human IL-18-Fc fusion protein, comprising: (a) a first monomer comprising from N-terminus to C-terminus: a variant human IL-18 protein of any one of claims 21-40 and a first Fc domain; and (b) a second monomer comprising a second Fc domain, 108. A VHH-Fc fusion protein comprising: (a) a first monomer comprising from N-terminus to C-terminus: a single domain anti-IL-18BP antibody of any one of claims 46-76 and a first Fc domain; (b) a second monomer comprising a second Fc domain.

109. A VHH-Fc fusion protein having an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NOs 601-603 or 609-615.

110. A VHH-Fc fusion protein comprising: (a) a first monomer having an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NO: 601-603 or 609-615, and (b) a second monomer comprising an identical sequence to the first monomer of (a).

111. A VHH-Fc fusion protein having an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NOs 611 or 615.

112. A VHH-Fc fusion protein having an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NOs 604-606 or 616-617.

113. A VHH-Fc fusion protein comprising: (a) a first monomer having an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to any one of SEQ ID NO: 604-606 or 616-617, and (b) a second monomer comprising an identical sequence to the first monomer of (a).

114. A fusion protein comprising: (a) a first monomer comprising from N-terminus to C-terminus: a variant IL18 molecule having an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 564, and a first Fc domain; and (b) a second monomer comprising from N-terminus to C-terminus: a single domain anti-IL-18BP antibody having an amino acid sequence that is at least 90%, 95%, 98%, 99%, or 100% identical to SEQ ID NO: 533, and a second Fc domain.

115. The Fc fusion protein any one of claims 107-114, wherein the second monomer further comprises one or more variant human IL-18 proteins of any one of claims 21-40.

116. The Fc fusion protein of any one of claims 107-115, wherein the second monomer further comprises one or more single domain anti-IL-18BP antibodies of any one of claims 46-76.

117. The Fc fusion protein of any one of claims 107-116, wherein the first monomer comprises two single domain anti-IL-18BP antibodies.

118. The Fc fusion protein of any one of claims 107-117, wherein the second monomer comprises two single domain anti-IL-18BP antibodies.Docket No. WRENCH-001 / WO01 119. The Fc fusion protein of any one of claims 107-118, wherein the first monomer comprises, from N- terminus to C-terminus: a first single domain anti-IL-18BP antibody of any one of claims 46-76; a first Fc domain; and a second single domain anti-IL-18BP antibody of any one of claims 46-76.

120. An Fc fusion protein, comprising: (a) a first monomer comprising two single domain anti-IL-18BP antibodies of any one of claims 46-76 and a first Fc domain; and (b) a second monomer comprising a single domain anti-IL-18BP antibody of any one of claims 46-76, a variant human IL-18 protein of any one of claims 21-40, and a second Fc domain.

121. A variant IL-18 x Fab-Fc fusion protein comprising: (a) a first monomer comprising from N-terminus to C-terminus: a variable heavy (VH) chain and a first Fc domain; (b) a second monomer comprising from N-terminus to C-terminus: a variant human IL-18 protein of any one of claims 21-40, and a second Fc domain; (c) a third monomer comprising a variable light (VL) chain, wherein the VH and VL form an antigen binding fragment (Fab).

122. A VHH x Fab-Fc fusion protein comprising: (a) a first monomer comprising from N-terminus to C-terminus: a variable heavy (VH) chain and a first Fc domain; (b) a second monomer comprising from N-terminus to C-terminus: a single domain anti-IL-18BP antibody of any one of claims 46-76, and a second Fc domain; (c) a third monomer comprising a variable light (VL) chain, wherein the VH and VL form an antigen binding fragment (Fab).

123. The fusion protein of claim 121 or claim 122, wherein the Fab selectively binds to a tumor-associated antigen (TAA).

124. The fusion protein of any one of claims 121-123, wherein the Fab selectively binds to an immune checkpoint selected from the list consisting of Cytotoxic T-lymphocyte-associated protein 4 (CTLA-4), Programmed cell death protein 1 (PD-1), Programmed death-ligand 1 (PD-L1), Lymphocyte-activation gene 3 (LAG-3), T cell immunoglobulin and mucin-domain containing-3 (TIM-3), T cell immunoglobulin and ITIM domain (TIGIT), and V-domain Ig suppressor of T cell activation (VISTA).

125. The fusion protein of claim 123 or claim 124, wherein the TAA is selected from the group consisting of B-cell maturation antigen (BCMA), carcinoembryonic antigen (CEA), epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (Her2), epithelial cell adhesion molecule (EpCAM), CD20, CD26, CD123, CD30, CD33, CD47, CD52, CD133, glycoprotein A33 (gpA33), mucins, tumor associatedDocket No. WRENCH-001 / WO01 glycoprotein-72 (TAG-72), type IX collagen (CIX), glutamate carboxypeptidase II (PSMA), folate-binding protein, GD2, GD3, GM2, vascular endothelial growth factor (VEGF), vascular endothelial growth factor receptor (VEGFR), integrin, αVβ3, α5β1, ERBB2, ERBB3, mesenchymal epithelial transition (MET), insulin- like growth factor-I receptor (IGFIR), ephrin type-A receptor 3 (EPHA3), TRAIL receptor 1 (TRAILR1), TRAIL receptor 2 (TRAILR2), receptor activator of nuclear factor kappa beta (RANKL), fibroblast activation protein (FAP), claudin 18.2, mesothelin, receptor tyrosine kinase like orphan receptor 1 (ROR1), epidermal growth factor receptor variant III (EGFRVIII), six-transmembrane epithelial antigen of the prostate-2 (STEAP2), orphan G protein–coupled receptor, class C group 5 member D (GPRC5D), carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), and tenascin.

126. The fusion protein of any one of claims 107-125, wherein the fusion protein has a melting temperature of at least 60C.

127. The fusion protein of any one of claims 107-126, wherein the fusion protein has a melting temperature of at least 70C.

128. The fusion protein of any one of claims 107-127, wherein the fusion protein prevents the interaction of IL-18BP with IL-18.

129. The fusion protein of any one of claims 107-128, wherein the fusion protein increases the activity of endogenous IL-18.

130. The fusion protein of any one of claims 107-129, wherein the fusion protein has improved binding affinity to FcRn compared to IgG1 and IgG4 at a pH of 7-7.

6.

131. The fusion protein of claim 130, wherein the fusion protein has 10x, 20x, or 40x higher binding affinity to FcRn compared to IgG1 and IgG4 at a pH of 7-7.

6.

132. The fusion protein of any one of claims 107-131, wherein the fusion protein restores IL-18-mediated signaling that was inhibited by the interaction of IL-18 and IL-18BP.

133. The fusion protein of any one of claims 107-132, wherein the fusion protein antagonizes at least one immune inhibitory effect of IL-18BP.

134. The fusion protein of any one of claims 107-133, wherein the fusion protein blocks the IL-18 : IL- 18BP binding interaction.

135. The fusion protein of any one of claims 107-134, wherein the fusion protein releases IL-18BP within the acidic environment of endosomes, thereby resulting in an increased clearance of IL-18BP.

136. The fusion protein of any one of claims 107-135, wherein the variant IL-18 protein and / or single domain anti-IL-18BP antibody are covalently attached to the N-terminus or the C-terminus of the first or the second Fc domain.

137. The fusion protein of any one of claims 107-136, wherein the first Fc domain and second Fc domain are configured in an asymmetrical manner.

138. The fusion protein of any one of claims 107-137, wherein the first domain and the second domain comprise complementary pairs of amino acid substitutions that improve thermostability.Docket No. WRENCH-001 / WO01 139. The fusion protein of any one of claims 107-138, wherein the first Fc domain comprises a set of amino acid substitutions selected from the group consisting of S354C and T366W.

140. The fusion protein of any one of claims 107-139, wherein the second Fc domain comprises a set of amino acid substitutions selected from the group consisting of Y349C, T366S, L368A, and Y407V.

141. The fusion protein of any one of claims 107-140, wherein the single domain anti-IL-18BP antibody is covalently attached to the N-terminus or the C-terminus of the first or second Fc domain without a linker.

142. The fusion protein of any one of claims 107-140, wherein the variant IL-18 protein and / or single domain anti-IL-18BP antibody are covalently attached to the N-terminus or the C-terminus of the first or the second Fc domain via a linker.

143. The fusion protein of claim 142, wherein the linker comprises a glycine-serine linker.

144. The fusion protein of claim 143, wherein the glycine-serine linker comprises a sequence of (GS)n, wherein n = 1 to 10.

145. The fusion protein of claim 142, wherein the linker comprises (GS)n, (GGS)n, (GGGS)n, (GGSG)n, (GGSGG)n, (GGGGS)n, (GGGGG)n, or (GGG)n, wherein n = 1 to 10.

146. The fusion protein of claim 142, wherein the linker comprises (GGGGS)4 or (GGGGS)3.

147. The fusion protein of any one of claims 107-146, wherein the first and second Fc domains have an identical amino acid sequence.

148. The Fc fusion protein of any one of claims 107-147, wherein an Fc domain is a wild type Fc.

149. The Fc fusion protein of any one of claims 107-146, wherein an Fc domain has amino acid substitutions M428L and N434A, compared to wild type Fc.

150. The Fc fusion protein of any one of claims 107-146, wherein an Fc domain has amino acid substitutions T307E, M428L, and N434A, compared to wild type Fc.

151. The VHH-Fc fusion protein of any one of claims 107-146, wherein the Fc fusion protein has an increased thermostability compared to a VHH-Fc fusion protein with a wild type Fc.

152. A pharmaceutical composition comprising (a) the fusion protein of any one of claims 107-151 and (b) a pharmaceutically acceptable carrier.

153. One or more nucleic acids encoding the fusion protein of any one of claims 107-151.

154. An expression vector comprising the one or more nucleic acids of claim 153.

155. A host cell comprising the one of more nucleic acids of claim 153 or the expression vector of claim 154.

156. A method of making a fusion protein comprising culturing the host cell of claim 155 and recovering the fusion protein from the cell culture.

157. A method of treating a disease or condition in a subject in need thereof comprising administering to the subject a therapeutically effective amount of a variant human IL-18 protein of any one of claims 21-40, a single domain anti-IL-18BP antibody of any one of claims 46-77, a multispecific binding protein of any one of claims 84-101, and / or a fusion protein of any one of claims 106-150.Docket No. WRENCH-001 / WO01 158. The method of claim 157, wherein the disease or condition comprises a cancerous disease, a proliferative disease, a tumorous disease, an inflammatory disease, an immunological disorder, an autoimmune disease, an infectious disease, a viral disease, an allergic reaction, a parasitic reaction, a graft-versus-host disease or a host-versus-graft disease.

159. A method of treating cancer in a patient, comprising administering a composition comprising a variant human IL-18 protein of any one of claims 21-40, a single domain anti-IL-18BP antibody of any one of claims 46-77, a multispecific binding protein of any one of claims 84-101, and / or a fusion protein of any one of claims 106-150.

160. The method of claim 159, wherein said cancer is selected from the group consisting of renal clear cell carcinoma (RCC), lung cancer, NSCLC, lung adenocarcinoma, lung squamous cell carcinoma, gastric adenocarcinoma, ovarian cancer, endometrial cancer, breast cancer, triple negative breast cancer (TNBC), head and neck tumor, colorectal adenocarcinoma, melanoma, and metastatic melanoma.

161. The method of treatment according to claim 159 or claim 160, wherein the patient experiences an increase in tumor growth inhibition of at least about 10%, 20%, 30% 40% 50% 60% 70% 80% 90%, 100%, 125%, 150%, 175%, 200% 225% 250%, 275%, 300%, 325% 350%, 375%, 400%, 425%, 450%, 475%, 50Q%, 525%, 550%, 575%, 600%, 625%, 650%, 675%, 700%, 725%, 750%, 775%, 800%, 825%, 850%, 875%, 900%, 925%, 950%, 975%, or 1000%, as compared to a control or an untreated patient.

162. The method of treatment according to any one of claims 159-161, wherein the patient experiences a decrease in tumor growth inhibition of at least about 10%, 20%, 30% 40% 50% 60% 70% 80% 90%, 100%, 125%, 150%, 175%, 200% 225% 250%, 275%, 300%, 325% 350%, 375%, 400%, 425%, 450%, 475%, 50Q%, 525%, 550%, 575%, 600%, 625%, 650%, 675%, 700%, 725%, 750%, 775%, 800%, 825%, 850%, 875%, 900%, 925%, 950%, 975%, or 1000%, as compared to a control or an untreated patient.

163. A method of reducing a tumor comprising contacting the tumor with a composition comprising a variant human IL-18 protein of any one of claims 21-40, a single domain anti-IL-18BP antibody of any one of claims 46-77, a multispecific binding protein of any one of claims 84-101, and / or a fusion protein of any one of claims 106-150.

164. A method of reducing a tumor in a subject in need thereof comprising administering to the subject a composition comprising a variant human IL-18 protein of any one of claims 21-40, a single domain anti-IL- 18BP antibody of any one of claims 46-77, a multispecific binding protein of any one of claims 84-101, and / or a fusion protein of any one of claims 106-150.

165. A method of treating a subject having a cancer, comprising administering to the subject a composition comprising a variant human IL-18 protein of any one of claims 21-40, a single domain anti-IL-18BP antibody of any one of claims 46-77, a multispecific binding protein of any one of claims 84-101, and / or a fusion protein of any one of claims 106-150.

166. The method of any one of claims 115-123, wherein the subject is a human subject.Docket No. WRENCH-001 / WO01 167. A single domain anti-IL-18BP antibody of any of the preceding claims, wherein the single domain anti- IL18-BP antibody blocks endogenous IL-18BP produced by peripheral blood mononuclear cells.

168. A single domain anti-IL-18BP antibody of any of the preceding claims, wherein the single domain anti- IL-18BP antibody inhibits tumor growth in a mouse tumor model.

169. A single domain anti-IL-18BP antibody of any of the preceding claims, wherein the single domain anti- IL18-BP antibody does not have any treatment-induced toxicity when administered to a mouse tumor model.

170. A single domain anti-IL-18BP antibody of any of the preceding claims, wherein the single domain anti- IL-18BP antibody is useful for treating a hepatocellular carcinoma or a lung adenocarcinoma.

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