Neutralizing antibody constructs against HIV

Abstract

Antigen binding proteins of the invention bind to Human Immunodeficiency Virus (HIV) envelope protein and are useful in treating and preventing HIV infection. In particular, the antigen binding proteins of the V1 / V2 apex region of glycoprotein 120 (gp120) or the gp120-gp41 interface region of gp120 and gp41 as well as having a CD4 domain that binds to the CD4bs of gp120.

Description

[0001] ANTIGEN BINDING PROTEINS FIELD OF THE INVENTIONThe invention is directed to a multimeric antigen binding protein that binds to the HumanImmunodeficiency Virus (HIV) envelope spike complex and its use in treating or preventing HIVinfection. The antigen binding proteins of the invention bind to the V1 / V2 apex region ofglycoprotein 120 (gp120) or the gp120-gp41 interface region of gp120 and gp41 as well as having aCD4 domain that binds to the CD4bs of gp120. The antigen binding proteins of the invention mayalso bind to at least one complex N-glycan on a gp120 or a gp41 protein as well as having a CD4domain that binds to the CD4bs of gp120. BACKGROUND TO THE INVENTION HIV, the virus that over time may result in Acquired Immunodeficiency Syndrome (AIDS), continues to be a serious public health challenge and has claimed 40.1 million lives so far. HIV attacks the body’s immune system, targeting CD4-positive white blood cells, and leaves those infected vulnerable to opportunistic infections such as tuberculosis and fungal infections, severe bacterial infections and some cancers. Globally, 38.4 million people were living with HIV at the end of 2021, with 1.5 million people becoming newly infected (WHO, Key Facts HIV, July 2022). Whilst there is currently no cure for HIV infection, it can be treated with antiretroviral therapy (ART), which includes a number of different types of drugs that prevent the virus from multiplying (nucleoside reverse transcriptase inhibitors (NRTIs), non-nucleoside reverse transcriptase inhibitors (NNRTIs), protease inhibitors, entry inhibitors and integrase inhibitors), allowing the body’s immune system to recover sufficiently for the infected patient to be asymptomatic. 75% of people living with HIV in 2021 received some form of ART. However, ART often requires taking medication every day for life and has the risk of serious and debilitating side effects. Further, increased use of ART has also been accompanied by the emergence of drug resistance, the levels of which have steadily increased in recent years. Broadly neutralizing antibodies (bNAbs) could potentially provide longer-term HIV suppression, but individual bNAbs have only had limited success in previous studies. This is in partbecause antibody-resistant virus either already existed in the patient or emerged soon aftertreatment began (NIH Research Matters, 14 June 2022). Combinations of bNAbs are currently being investigated in the presence or absence of ART (Nature, 606, 368-374, 2022). Further treatment options are needed for HIV infection, in particular drugs that are long- acting and effective against a wide spectrum of HIV strains so that patients taking them are less susceptible to drug resistance. SUMMARY OF THE INVENTIONIn a first aspect of the invention, there is provided a multimeric anti-HIV envelope spike complex-binding protein comprising: i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least oneheavy chain or light chain, wherein the antibody binds to the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface region of a gp120 and a gp41 protein; and ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of at least one of the heavy chains or light chains of the broadly neutralizing antibody. In a second aspect of the invention, there is provided a multimeric anti-HIV envelope spike complex- binding protein comprising: i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least oneheavy chain or light chain, wherein the antibody binds to at least one complex N-glycan on a gp120 protein or a gp41 protein; and ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of at least one of the heavy chains or light chains of the broadly neutralizing antibody. In further aspects of the invention, pharmaceutical compositions comprising anti-HIV envelope spike complex-binding proteins of the invention, methods of preventing HIV infection and methods of treating HIV infection with anti-HIV envelope spike complex-binding proteins of the invention, uses of anti-HIV envelope spike complex-binding proteins of the invention, methods of manufacturing anti-HIV envelope spike complex-binding proteins of the invention and kits comprising anti-HIV envelope spike complex-binding proteins of the invention are also provided. DESCRIPTION OF DRAWINGS / FIGURES FIG. 1 shows schematic designs of example bispecific binding proteins of the invention.Human CD4 domains or variants thereof are fused, either directly or via linkers, to the N-termini the heavy chains (A), the light chains (B) or to the N-termini of the heavy chains (C) or light chains (D) of bNAbs. Such designs facilitate concomitant binding of the human CD4 domain of the bispecificmolecule and gp160 binding domain (or in other words, the envelope spike complex broadneutralizing antibody or fragment) of the bispecific molecule to HIV-1 gp160 (the envelope spike complex) and prevent HIV-1 virions from binding to the cell surface receptors and fusing with the cell membrane (E-F). FIG. 2 shows IC50 values (nM) of soluble CD4 domains (SEQ ID NOs:4-15) against a panelof HIV-1 envelopes in a PSV assay (ACTOne), together with the Tm for each soluble CD4 domain. The horizontal bars indicate geometric mean IC50. FIG. 3 shows that linker length between the CD4 domain and a similar model bNAb to theinvention (V3-bNAb1) heavy chain N-terminus does not particularly affect anti-viral activity in a PSVassay (ACTOne) (A) but does change the PK of the resultant bispecific molecules in a humanized mouse model (Tg32-hFcRn strain) (B). Thermal stability of the CD4 domain also affects the PK of the bispecific molecules (B). FIG. 4 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb1-derived bispecifics (targeting the V1 / V2 Apex) according to the invention summarised inTable 1 below. Where the bispecific contains the CD4 at the HC, the HC sequence includes the linkerand the CD4 domain (e.g. SEQ ID NOs: 74 and 421), equally where the bispecific contains the CD4at the LC, the LC sequence includes the linker and the CD4 domain (e.g. 420 and 422). (A-C) showsanti-viral activity of Apex-bNAb1-derived bispecifics and control molecules against a panel of HIV-1envelopes in a PSV assay (ACTOne cells); (D-F) shows anti-viral activity of Apex-bNAb1-derivedbispecifics with CD4 domain fused at different positions against a panel of HIV-1 envelopes in a PSVassay (ACTOne cells); (G-J) shows anti-viral activity of a Apex-bNAb1-derived bispecific against adiverse panel of 119 HIV-1 envelopes (Seaman et al., J Virol. 2010 Feb;84(3):1439-52.) in a PSV assay (TZM.bl cells). (A), (D), and (G) shows IC50; (H) shows IC80; (B), (E) and (I) shows IC90; and (C), (F) and(J) show MPI.Table 1 – Figure 4 molecule key (SEQ ID NOs:)SEQ ID NO HC LCCDR CDR CDR CDR CDR CDR H1 H2 H3 L1 L2 L3VH VLBispecific1-1 (74)(CD4 at N-terminus of HC)74 254 244 245 246 247 248 249 250 251Bispecific1-2 (420)(CD4 at N-terminus of LC)253 420 244 245 246 247 248 249 250 251Bispecific1-3 (421)(CD4 at C-terminus of HC)421 254 244 245 246 247 248 249 250 251Bispecific1-4 (422) 253 422 244 245 246 247 248 249 250 251 (CD4 at C-terminus of LC) Apex-bNAb1 253 254 244 245 246 247 248 249 250 251CD4 = D1m-K8C-G99C_Fc (SEQ ID NO: 53) Combo = mixture of Apex-bNAb1 and CD4 at 1:1 molar ratio FIG. 5 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb2-derived bispecifics (targeting the V1 / V2 Apex) according to the invention summarized inFigure 5 below. Where the bispecific contains the CD4 at the HC, the HC sequence includes the linker and the CD4 domain (e.g. SEQ ID NOs: 75 and 424), equally where the bispecific contains theCD4 at the LC, the LC sequence includes the linker and the CD4 domain (e.g. 423 and 425). (A-C)shows anti-viral activity of Apex-bNAb2-derived bispecifics and control molecules against a panel ofHIV-1 envelopes in a PSV assay (ACTOne cells); (D-F) shows anti-viral activity of Apex-bNAb2-derived bispecifics with CD4 domain fused at different positions against a panel of HIV-1 envelopesin a PSV assay (ACTOne cells); (G-J) shows anti-viral activity of a Apex-bNAb2-derived bispecificagainst a diverse panel of 119 HIV-1 envelopes (Seaman et al., J Virol. 2010 Feb;84(3):1439-52.) ina PSV assay (TZM.bl cells).Table 2 – Figure 5 molecule key (SEQ ID NOs:)SEQ ID NO HC LCCDR CDR CDR CDR CDR CDR H1 H2 H3 L1 L2 L3VH VLBispecific2-1 (75)(CD4 at N-terminus of HC)75 265 255 256 257 258 259 260 261 262Bispecific2-2 (423)(CD4 at N-terminus of LC)264 423 255 256 257 258 259 260 261 262Bispecific2-3 (424)(CD4 at C-terminus of HC)424 265 255 256 257 258 259 260 261 262Bispecific2-4 (425)(CD4 at C-terminus of LC)264 425 255 256 257 258 259 260 261 262bNAb2 264 265 255 256 257 258 259 260 261 262CD4 = D1m-K8C-G99C_Fc (SEQ ID NO: 53) Combo = mixture of the bNAb and CD4 at 1:1 molar ratio FIG. 6 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb3-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 76 and a LC according to SEQ ID NO: 276) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 7 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb4-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 77 and a LC according to SEQ ID NO: 287) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 8 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb5-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 78 and a LC according to SEQ ID NO: 298) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 9 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb6-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 79 and a LC according to SEQ ID NO: 309) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 10 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb7-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 80 and a LC according to SEQ ID NO: 320) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 11 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb8-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 81 and a LC according to SEQ ID NO: 331) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 12 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb9-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 82 and a LC according to SEQ ID NO: 342) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 13 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb10-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 83 and a LC according to SEQ ID NO: 353) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 14 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb11-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 84 and a LC according to SEQ ID NO: 364) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 15 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb12-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 85 and a LC according to SEQ ID NO: 375) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 16 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb13-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 86 and a LC according to SEQ ID NO: 386) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 17 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb14-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 87 and a LC according to SEQ ID NO: 397) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 18 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb15-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 88 and a LC according to SEQ ID NO: 408) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 19 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-bNAb16-derived bispecifics according to the invention (targeting the V1 / V2 Apex, containing a HCincluding a linker + CD4 domain as per SEQ ID NO: 89 and a LC according to SEQ ID NO: 419) andcontrol molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).FIG. 20 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface- bNAb17-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 60 and a LC according to SEQID NO: 100) and control molecules (A-C) against a panel of HIV-1 envelopes in a PSV assay(ACTOne cells) and (D-G) against a diverse panel of 119 HIV-1 envelopes.FIG. 21 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface-bNAb18-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 61 and a LC according to SEQID NO: 111) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 22 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface-bNAb19-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 62 and a LC according to SEQID NO: 122) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 23 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface-bNAb20-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 63 and a LC according to SEQID NO: 133) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 24 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface-bNAb21-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 64 and a LC according to SEQID NO: 144) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 25 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface-bNAb22-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 65 and a LC according to SEQID NO: 155) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells). FIG. 26 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface-bNAb23-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 66 and a LC according to SEQID NO: 166) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 27 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface-bNAb24-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 67 and a LC according to SEQID NO: 177) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 28 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of InterfacebNAb25-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 68 and a LC according to SEQID NO: 188) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 29 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of InterfacebNAb26-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 69 and a LC according to SEQID NO: 199) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 30 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of InterfacebNAb27-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 70 and a LC according to SEQID NO: 210) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 31 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of InterfacebNAb29-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 71 and a LC according to SEQID NO: 221) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 32 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of InterfacebNAb30-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 72 and a LC according to SEQID NO: 232) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). FIG. 33 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of InterfacebNAb31-derived bispecifics according to the invention (targeting the gp120-gp41 interface,containing a HC including a linker + CD4 domain as per SEQ ID NO: 73 and a LC according to SEQID NO: 243) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOnecells). DETAILED DESCRIPTION OF THE INVENTION DEFINITIONS “Affinity”, also referred to as “binding affinity”, is the strength of binding at a single interaction site, i.e., of one molecule, e.g., an antigen binding protein, to another molecule, e.g., its target antigen, at a single binding site. The binding affinity of an antigen binding protein to its target may be determined by equilibrium methods (e.g., enzyme-linked immunoabsorbent assay (ELISA) or radioimmunoassay (RIA)), or kinetics (e.g., BIACORE analysis). “Alternative antibody formats” include alternative scaffolds in which one or more CDRs of the antigen binding protein can be arranged onto a suitable non-immunoglobulin protein scaffold 5 or skeleton, such as an affibody, a SpA scaffold, an LDL receptor class A domain, an avimer (see, e.g., U.S. Patent Application Publication Nos. 2005 / 0053973, 2005 / 0089932, 2005 / 0164301) or an EGF domain. “Antibody” is used herein to refer to a heterotetrameric glycoprotein with an approximate molecular weight of 150,000 daltons. An intact antibody is composed of two identical heavy chains (HCs) and two identical light chains (LCs) linked by covalent disulphide bonds. This H2L2 structure folds to form a ‘Y’ shape with three functional domains comprising two antigen-binding fragments, known as ‘Fab’ fragments (the ‘top’ of the ‘Y’), and a fragment 9crystallisable 99‘Fc’ (the ‘bottom’ of the ‘Y’). The Fab fragment is composed of the variable domain at the amino-terminus, variable heavy (VH) or variable light (VL), and the constant domain at the carboxyl terminus, CH1 (heavy) and CL (light). The Fc fragment is composed of two domains formed by dimerization of paired CH2 and CH3 regions. The Fc may elicit effector functions by binding to receptors on immune cells or by binding C1q, the first component of the classical complement pathway. The five classes of antibodies IgM, IgA, IgG, IgE and IgD are defined by distinct heavy chain amino acid sequences, which are called µ, α, γ, ε and δ respectively; each heavy chain can pair with either a Κ or λ light chain. The majority of antibodies in the serum belong to the IgG class, there are four isotypes of human IgG (IgG1, IgG2, IgG3 and IgG4), the sequences of which differ mainly in their hinge region. In an embodiment, an anti-CD4bs antibody, as used herein, refers to an antibody that binds to a CD4 binding site “Antigen binding antibody fragments” or “antigen binding fragments” or “antibody fragments” as used herein include Fab, F(ab’)2, Fv, disulphide linked Fv, single chain Fv (scFv), disulphide-linked scFv, diabodies, TANDABS, etc. and modified versions of any of the foregoing (for a summary of alternative “antibody” formats see Holliger and Hudson, Nature Biotechnology, 23(9), 1126-1136, 2005). “Antigen binding protein of the invention” and “anti-HIV envelope spike complexbinding protein” are used interchangeably herein and refer to antibodies and fragments thereof, alternative antibody formats, and other protein constructs, such as domains, that are capable ofbinding to the HIV envelope spike complex comprised of gp120 and gp41, or in other words arecapable of binding to either gp120 or gp41. The HIV env gene encodes a gene product of around850 amino acids. The primary env product is the protein gp160 (or envelope glycoprotein gp160)which is gets cleaved into gp120 (about 480 amino acids) and gp41 (about 345 amino acids) in theendoplasmic reticulum by the cellular protease furin. Gp120 (or gp120) is a 120 kDa glycoproteinthat is part of the outer layer of HIV. It presents itself as viral membrane spikes consisting of three molecules of gp120 linked together and anchored to the membrane by gp41 protein. Gp120 is essential for viral infection as it facilitates HIV entry into the host cell through its interaction with cellsurface receptors. Gp41 is a transmembrane protein that contains several sites within its ectodomainthat are required for infection of host cells. The amino acid sequence of an exemplary gp160 from HIV clone WITO is provided below (SEQ ID NO: 55): MKVMGTKKNYQHLWRWGIMLLGMLMMSSAAEQLWVTVYYGVPVWREANTTLFCASDAKAYDTEVHNVWAT HACVPTDPNPQEVVMGNVTEDFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTA NVTMREEMKNCSFNTTTVIRDKIQKEYALFYKLDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPA GFAILKCNNKTFNGKGPCRNVSTVQCTHGIKPVVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCT RPGNNTRRSINIGPGRAFYATGAIIGDIRKAHCNISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDP EVVMHTFNCGGEFFYCNSTQLFNSTWFNNGTSTWNSTADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCS SNITGLILTRDGGSNSSQNETFRPGGGNMKDNWRSELYKYKVVKIEPLGIAPTRAKRRVVQREKRAVTLGAVFLG FLGAAGSTMGAASLTLTVQARLLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQARVLAIERYLKDQQLLGI WGCSGKLICTTTVPWNTSWSNKSYDYIWNNMTWMQWEREIDNYTGFIYTLIEESQNQQEKNELELLELDKWA SLWNWFNITNWLWYIKLFIMIIGGLVGLRIVCAVLSIVNRVRQGYSPLSFQTRLPNPRGPDRPEETEGEGGERDR DRSARLVNGFLAIIWDDLRSLCLFSYHRLRDLLLIVARVVEILGRRGWEILKYWWNLLKYWSQELKNSAVSLLNV TAIAVAEGTDRVIEIVQRAVRAILHIPTRIRQGFERALL The amino acid of an exemplary gp120 is provided below (SEQ ID NO: 56): AEQLWVIVYYGVPVWREANTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVMGNVTEDFNMWKNNMV EQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTANVTMREEMKNCSFNTTTVIRDKIQKEYALFYK LDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGKGPCRNVSTVQCTHGIKP VVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCTRPGNNTRRSINIGPGRAFYATGAIIGDIR KAHCNISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDPEVVMHTFNCGGEFFYCNSTQLFNSTWFNNGTS TWNSTADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCSSNITGLILTRDGGSNSSQNETFRPGGGNMKDN WRSELYKYKVVKIEPLGIAPTRAKRRVVQREKRThe amino acid of an exemplary gp41 is provided below (SEQ ID NO: 57):AVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVER YLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNE QELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEG IEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQEL KNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL “Antigen binding site” and “paratope” are used interchangeably herein and refer to a particular site on an antigen binding protein that makes contact with and is capable of specifically binding to a site (i.e., epitope) on an antigen, e.g., HIV gp120. The antigen binding site may be formed by a single variable domain, or paired VH / VL domains as can be found on a standard antibody. Single-chain Fv (ScFv) domains can also provide antigen binding sites. “Avidity” also referred to as functional affinity, is the cumulative strength of binding at multiple interaction sites, e.g., the sum total of the strength of binding of two molecules (or more) to one another at multiple sites, e.g., taking into account the valency of the interaction. A “bispecific molecule” or “bispecific antigen binding protein” as used herein is an antigen binding protein that is capable of binding to two different epitopes on the same antigen, i.e.,HIV gp160 protein / envelope spike complex. In particular, one epitope comprises part of or thewhole of the V1 / V2 Apex region of gp120 or the interface region of gp120 and gp41, and the otherepitope comprises part of or the whole of the CD4 binding site of gp120. “Broadly neutralizing antibody” or “bNAb” as used herein, is meant an antibody that neutralizes more than one HIV-1 virus species (from diverse clades and different strains within aclade) in a neutralization assay. A broadly neutralizing antibody may neutralize at least 2, 3, 4, 5, 6,7, 8, 9 or more different strains of HIV-1, the strains belonging to the same or different clades. “CD4 binding site” or “CD4-binding site” or “CD4bs” refers to a site on the HIV envelope protein gp120 that binds to CD4. (Cluster of differentiation factor 4). CD4 is a T-cell surface protein that serves as the primary receptor site for HIV during HIV infection. The CD4 binding site on gp120 is a highly conserved, discontinuous and conformational that comprises residues on either side of the HIV V4 loop (Curr HIV / AIDS Rep, 9(1): 52-63, 2021) that binds to CD4. A “CD4 domain” as used herein is a soluble recombinant form of human CD4 (Cluster of differentiation factor 4, a transmembrane glycoprotein found on T-cells), or a fragment thereof, that mimics the activity of native membrane-anchored human CD4 in its binding interactions with the HIV envelope protein. A CD4 domain of the present invention binds to the CD4-binding site of HIV gp120 and may block the ability of HIV gp120 to bind membrane-anchored CD4, e.g., on CD4+ T cells. A CD4 domain of the invention may induce a structural rearrangement in gp120 uponbinding, including a structural rearrangement of part or all of the V1 / V2 Apex region of gp120(PMID: 37993719). This structural rearrangement in gp120 results in a high affinity binding site for achemokine coreceptor (CXCR4 and / or CCR5) being exposed. Native CD4 comprises four domains that are exposed on the extracellular surface of the cell, D1, D2, D3 and D4; a transmembrane domain; and a cytoplasmic tail domain. D1 and D3 resemble Ig variable domains and D2 and D4 resemble Ig constant domains. CD4 domains of the invention include one or more of domains D1 toD4 of CD4, or variants thereof. Examples of CD4 domains of the Invention include wild-type D1(SEQ ID NO:3); “mD1.22” / D1m (SEQ ID NO:4), which is a variant of D1 of CD4 (Chen et al, JVI88(2): 1125-39, 2014); wild-type D1D2 (SEQ ID NO:1); “mD1.22-D2” (SEQ ID NO:2), which is a variant of D1D2 (Fetzer et al., Journal of Virology, 92(12), 2018); and further variants of mD1.22 (SEQ ID NOs:5-21). “CDRs” are defined as the complementarity determining region amino acid sequences of an antigen binding protein. These are the hypervariable regions of immunoglobulin heavy and light chains. There are three heavy chain and three light chain CDRs (or CDR regions) in the variable portion of an immunoglobulin. In one embodiment, the CDRs are defined based on the Kabat definition. In another embodiment, the CDRs are defined based on the Chothia definition. In a further embodiment, the Chothia definition is from Discovery Studio which uses the definitions fromChothia and Lesk, Jmol Biol. 196(4):901-17 (1987) and Morea et al, Methods, 20:267-279 (2000). In another embodiment, the Chothia definition is based on the Chothia from Abysis definition. In a further embodiment, the CDRs are defined based on the IMGT definition. In another embodiment, the CDRs are defined based on the Honegger definition. In another embodiment, theCDRs are defined based on the contact definition. Thus, “CDRs” as used herein refers to all threeheavy chain CDRs, all three light chain CDRs, all heavy and light chain CDRs, or at least two CDRs. “Domain” refers to a folded polypeptide structure that retains its tertiary structure independent of the rest of the polypeptide. Generally, domains are responsible for discrete functional properties of polypeptides and in many cases may be added, removed or transferred to other polypeptides without loss of function of the remainder of the protein and / or of the domain. “Effector Function” as used herein refers to one or more of antibody-mediated effects including antibody-dependent cell-mediated cytotoxicity (ADCC), antibody-mediated complement activation including complement-dependent cytotoxicity (CDC), complement-dependent cell- mediated phagocytosis (CDCP), antibody dependent complement-mediated cell lysis (ADCML), and Fc-mediated phagocytosis or antibody-dependent cellular phagocytosis (ADCP). “Epitope” as used herein refers to the portion of an antigen (e.g., gp120) that makescontact with and is capable of specifically binding to a particular site (paratope) on an antigen binding protein. An epitope may be linear or conformational / discontinuous. A conformational / discontinuous epitope comprises amino acid residues that are separated by other sequences, i.e., it does not comprise a continuous sequence in the antigen’s primary amino acid sequence, but instead relies on the tertiary folding of the polypeptide. Although the residues within a confirmational / discontinuous epitope may be from different regions of the polypeptide chain, they are in close proximity in the three-dimensional structure of the antigen. In the case of multimeric antigens, a conformational or discontinuous epitope may include residues from different polypeptide chains. Particular residues comprised within an epitope can be determined through computer modelling programs or via three-dimensional structures obtained through methods known in the art, such as X-ray crystallography. Epitope mapping can be carried out using various techniques known to persons skilled in the art as described in publications such as Methods in Molecular Biology ‘Epitope Mapping Protocols’, by Mike Schutkowski and Ulrich Reineke (volume 524, 2009) and Johan Rockberg and Johan Nilvebrant (volume 1785, 2018). Exemplary methods include peptide-based approaches such as pepscan whereby a series of overlapping peptides are screened for binding using techniques such as ELISA or by in vitro display of large libraries of peptides or protein mutants, e.g., on phage. Detailed epitope information can be determined by structural techniques including X-ray crystallography, solution nuclear magnetic resonance (NMR) spectroscopy and cryogenic-electron microscopy (cryo- EM). Mutagenesis, such as alanine scanning, is an effective approach whereby loss of binding analysis is used for epitope mapping. Another method is hydrogen / deuterium exchange (HDX) combined with proteolysis and liquid-chromatography mass spectrometry (LC-MS) analysis to characterize discontinuous or conformational epitopes. “Half-life” or “t1 / 2” refers to the time required for the serum concentration of an antigen binding protein to reach half of its original value. The serum half-life of proteins can be measured by pharmacokinetic studies according to the method described by Kim et al., 1994, Eur. J. of Immuno. 24: 542-548. According to this method, radio-labelled protein is injected intravenously into mice and its plasma concentration is periodically measured as a function of time, for example, at about 3 minutes to about 72 hours after the injection. Other methods for pharmacokinetic analysis and determination of the half-life of a molecule will be familiar to those skilled in the art. “HIV envelope spike complex” or “ENV” or “spike complex” refers to a trimeric viralmembrane-associated glycoprotein (gp) or ‘spike’ comprised of non-covalently linked heterodimersof surface gp120 and transmembrane gp41. It is found on both the viral membrane and the cellmembrane of infected host cells and is encoded by the Env gene. The env gene encodes the gp160polypeptide which forms a homotrimer and is cleaved into gp120 and gp41 polypeptides. Gp120 is a surface (SU) glycoprotein responsible for binding to receptor molecules and the transmembrane I glycoprotein, gp41, mediates fusion of the viral membrane with the plasma cell membrane. Over half of the mass of the trimeric envelope ‘spike’ is an N-linked glycan shield that hides most amino acid-based epitopes on gp120. Binding of the cell surface receptor CD4 to HIV gp120 induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor (CXCR4 and / or CCR5), on gp120. Following gp120 binding to CXCR4 or CCR5 further conformational changes are triggered which results in gp120 disengaging from gp41, allowing for the fusion peptide of gp41 to be inserted into the cell membrane, which in turn triggers a sequence of structural changes resulting in membrane fusion (Dimitrov et al., Biochemistry 44(37): 12471-12479, 2005). “Human immunodeficiency virus (HIV)” has been characterized into two types: HIV-1 and HIV-2. HIV-1 is more virulent and more infective than HIV-2 and is the cause of the majority of HIV infections globally, whereas HIV-2 is limited to a much smaller number of people, mostly inWest Africa (Gilbert et al., Statistics in Medicine 22(4): 573-593). Thus, “HIV” may mean HIV-1 andHIV-2, or just “HIV-1”. HIV virions are spherical with viral glycoprotein “spikes”, the HIV envelopeprotein, protruding outwards. A conical capsid exists within the virion, enclosing a ribonucleoprotein complex comprising two copies of positive-sense single stranded RNA tightly bound to nucleocapsidproteins and enzymes needed for viral replication. “Symptoms” of HIV include raised temperature(fever), sore throat, body rash, tiredness, joint pain, muscle pain, swollen glands, weight loss, chronic diarrhoea, night sweats, skin problems, recurrent infections, headaches. A“linker” is a suitable structure that can be used to join together the CD4 domain andantibody or fragment of the invention. A linker may be a chemical linker such as PEG, or an aminoacid sequence, that links one domain in a polypeptide to another domain in a polypeptide. Forexample, a linker within the meaning of the invention includes an amino acid sequence that joins a CD4 domain to a bNAb heavy chain or a bNAb light chain. In an embodiment, the linker is not cleavable under intracellular conditions. “Multimeric antigen binding protein” or “Multispecific antigen binding protein”refers to an antigen binding protein that comprises at least two different polypeptide chains having different antigen binding sites. Each of these antigen-binding sites is capable of binding to a different epitope, which may be present on the same antigen or different antigens. In an embodiment, the multi-specific antigen binding proteins of the invention are bispecific molecules capable of binding to two different epitopes on the HIV envelope protein. In particular,one epitope may comprise part of or the whole of to the V1 / V2 loop of a gp120 protein or thegp120-gp41 interface of a gp120 and a gp41 protein and the other epitope may comprise part of orthe whole of the CD4 binding site of gp120 (through binding of the CD4 domain portion of themolecule). Symmetric formats of MSABPs combine multiple binding specificities in a single polypeptide chain or single HL pair including Fc-fusion proteins of fragment-based formats and formats whereby antibody fragments are fused to regular antibody molecules. Examples of symmetric formats may include DVD-Ig, TVD-Ig, CODV-Ig, (scFv)4-Fc, IgG-(scFv)2, Tetravalent DART-Fc, F(ab)4CrossMab, IgG-HC-scFv, IgG-LC-scFv, mAb-dAb etc. Amultimeric antigen binding protein described herein, for example, a bispecific antigenbinding protein having a broadly neutralizing anti-HIV envelope spike complex antibody and a CD4domain, may be encoded by one or more isolated nucleic acid sequences. Production of a multimericantigen binding protein, such as a bispecific antigen binding protein, may be achieved in a cell orliving organism by delivering exogenous isolated nucleic acids encoding the multimeric antigenbinding protein, for example, a heavy chain and a light chain of a broadly neutralizing anti-HIVenvelope spike complex antibody and a CD4 domain. Production of a multimeric antigen bindingprotein, such as a bispecific antigen binding protein, may be achieved in a cell in vitro or in vivo bydelivering exogenous isolated nucleic acids encoding the multimeric antigen binding protein, forexample, a heavy chain and a light chain of a broadly neutralizing anti-HIV envelope spike complexantibody and a CD4 domain. A subject in need may be delivered one or more nucleic acids encodingan multimeric antigen binding protein provided herein, such as a heavy chain and a light chain of abroadly neutralizing anti-HIV envelope spike complex antibody and a CD4 domain. The heavy chainand the light chain of the antibody may be delivered by the same or separate nucleic acids. Thenucleic acids may be DNA or RNA. The nucleic acids encoding the multimeric antigen binding proteinmay be delivered to the subject naked (i.e. without an encapsulating particle) or packaged (i.e. encapsulated in liposomes or polymer-based vehicles). The nucleic acids encoding the multimeric antigen binding protein may be delivered without a delivery vehicle (i.e., “naked”) or delivered with a viral or non-viral delivery vehicle (i.e., as a viral vector, adsorbed to or encapsulated in liposomes or polymer-based vehicles, and the like). The nucleic acid may include elements such as a poly-A tail, a 5’ and / or 3’ untranslated region (UTR). The nucleic acids may be mRNA. The mRNA may include a cap structure. The mRNA may be self-replicating RNA. The nucleic acid coding for the multimeric antigen binding proteins may be modified orunmodified. The nucleic acids coding for the multimeric antigen binding proteins may comprise atleast one chemical modification. Nucleic acids (e.g., mRNAs) can be modified to enhance stability by including one or more chemical modifications. Such chemical modifications include, but are not limited to, a modified nucleotide, a modified sugar backbone, and the like. Also provided herein is amethod of producing a multimeric antigen binding protein in a cell, tissue, or organism comprisingcontacting said cell, tissue, or organism with a composition comprising an isolated nucleic acidcomprising at least one chemical modification and which encodes the multimeric antigen bindingprotein. Also provided herein is a method of producing a multimeric antigen binding protein in a cell,tissue or organism comprising contacting said cell, tissue or organism with a composition comprising a polynucleotide comprising at least one chemical modification and which encodes a multimericantigen binding protein. Also provided herein is a method of producing a multimeric antigen bindingprotein in a cell, in vitro or in vivo, comprising contacting said cell with a composition comprising a nucleic acid comprising at least one chemical modification and which encodes a multimeric antigen binding protein. “Neutralizes” as used throughout the present specification means that the biological activity of HIV is reduced in the presence of an antigen binding protein as described herein incomparison to the biological activity of HIV in the absence of the antigen binding protein, in vitro orin vivo. For example, a neutralizing antigen binding protein of the invention may inhibit HIV entry into a target cell and reduce viral load in a patient infected with HIV. “Percent identity” or “% identity” between a query amino acid sequence and a subject amino acid sequence is the “Identities” value, expressed as a percentage, that is calculated using a suitable algorithm (e.g., BLASTP, FASTA, Needleman-Wunsch, Smith-Waterman, LALIGN, or GenePAST / KERR) or software (e.g., DNASTAR Lasergene, GenomeQuest, EMBOSS needle or EMBOSS infoalign), over the entire length of the query sequence after a pair-wise global sequence alignment has been performed using a suitable algorithm (e.g., Needleman-Wunsch or GenePAST / KERR) or software (e.g. DNASTAR Lasergene or GenePAST / KERR). Importantly, a query amino acid sequence may be described by an amino acid sequence disclosed herein, in particular in one or more of the claims. The query sequence may be 100% identical to the subject sequence, or it may include up to a certain integer number of amino acid alterations as compared to the subject sequence such that the % identity is less than 100%. For example, the query sequence is at least 50, 60, 70, 75, 80, 85, 90, 95, 96, 97, 98, or 99% identical to the subject sequence. In the case of amino acid sequences such alterations include at least one amino acid residue deletion, substitution (including conservative and non-conservative substitutions), or insertion, wherein said alterations may occur at the amino- or carboxy-terminal positions of the query sequence or anywhere between those terminal positions, interspersed either individually among the amino acid residues in the query sequence or in one or more contiguous groups within the query sequence. For antibody sequences, the % identity may be determined across the entire length of the query sequence, including the CDRs. Alternatively, the % identity may exclude one or more or all of the CDRs, for example all of the CDRs are 100% identical to the subject sequence and the % identity variation is in the remaining portion of the query sequence, e.g., the framework sequence, so that the CDR sequences are fixed and intact. “Protein scaffold” as used herein includes, but is not limited to, an immunoglobulin (Ig) scaffold, for example an IgG scaffold, which may be a four chain or two chain antibody, or which may comprise only the Fc region of an antibody, or which may comprise one or more constant regions from an antibody, which constant regions may be of human origin. The protein scaffold may be an Ig scaffold, for example an IgG, or IgA scaffold. The IgG scaffold may comprise some or all the domains of an intact antibody (i.e., CH1, CH2, CH3, VH, VL). The antigen binding protein may comprise an IgG scaffold selected from IgG1, IgG2, IgG3, IgG4 or IgG4PE. For example, the scaffold may be IgG1. The scaffold may consist of, or comprise, the Fc region of an antibody, or is a part thereof. The protein scaffold may be a non-Ig scaffold. The protein scaffold may be a derivative of ascaffold selected from one or more of CTLA-4, lipocalin, Protein A derived molecules such as Z-domain of Protein A (Affibody, SpA), A-domain (Avimer / Maxibody); heat shock proteins such as GroEl and GroES; transferrin (trans-body); ankyrin repeat protein (DARPin); peptide aptamer; Ctype lectin domain (Tetranectin); human γ-crystallin and human ubiquitin (affilins); PDZ domains; scorpion toxin kunitz type domains of human protease inhibitors; and fibronectin / adnectin; whichhas been subjected to protein engineering in order to obtain binding to an antigen, such as gp120 orgp41. “Single variable domain” refers to a folded polypeptide domain comprising sequences characteristic of antibody variable domains. It therefore includes complete antibody variable domains such as VH, VHH and VL and modified antibody variable domains, for example, in which one or more loops have been replaced by sequences that are not characteristic of antibody variabledomains, or antibody variable domains that have been truncated or comprise N- or C-terminalextensions, as well as folded fragments of variable domains that retain at least the binding activity and specificity of the full-length domain. A single variable domain as defined herein is capable of binding an antigen or epitope independently of a different variable region or domain. A “domain antibody” or “DAB” may be considered the same as a human “single variable domain”. A single variable domain may be a human single variable domain, but also includes single variable domains from other species such as rodent (for example, as disclosed in WO 00 / 29004), nurse shark and Camelid VHHs Camelid VHHs are immunoglobulin single variable domain polypeptides that are derived from species including camel, llama, alpaca, dromedary, and guanaco, which produce heavychain only antibodies naturally devoid of light chains. Such VHH domains may be humanised17according to standard techniques available in the art, and such domains are considered to be “single variable domains”. “Stabilizing mutation” refers to a change of an amino acid residue in a polypeptide sequence that increases the thermal thermostability of said polypeptide. Increased thermostability may be reflected in a melting temperature (Tm) increase of, for example, between 1 and 50 ºC. CD4 domains with stabilizing mutations include SEQ ID NOs:5-21. A “variant sequence” substantially retains the biological characteristics of the unmodified protein. In the case of an antibody sequence disclosed herein, the VH or VL (or HC or LC) sequence may be a variant sequence with up to 10 amino acid substitutions, additions or deletions. Forexample, the variant sequence may have up to 9, 8, 7, 6, 5, 4, 3, 2 or 1 amino acid substitution(s),addition(s) or deletion(s). The sequence variation may exclude one or more or all of the CDRs, for example the CDRs are the same as the VH or VL (or HC or LC) sequence and the variation is in the remaining portion of the VH or VL (or HC or LC) sequence, so that the CDR sequences are fixed and intact. “V3 loop region”, “V3 / glycan” or “V3” as used herein refers to the third variable region (V3) of HIV gp120. Comparison of predicted amino acid sequences from several different isolates has shown that sequence heterogeneity of gp120 is clustered in five variable regions (designated V1, V2, V3, V4, and V5.) The V3 region contains post-translational modifications, such as glycosylation, and is essential for viral infectivity. The V3 region, although only 35 amino acids long, exhibits considerable sequence variability. Additionally, variability in potential N-linked glycosylation sites allow for further variability in the variable regions of gp120. Together, the V3 region and the N- linked glycosylation sites within and adjacent to the region are understood to comprise the “V3 loop region,” “V3 / glycan” or V3” as used herein. For example, one site of glycosylation (e.g., 30 oligomannose such as Man-5 to Man-9) is centered on amino acid residue N332 of gp120. Othersites of potential N-linked glycosylation within and adjacent to the V3 loop region include K295,N301, N386, N392 of gp120. The V3 loop is generally considered to be in the region between cysteine residues C296 and C331 of gp120, while some N-linked glycosylation sites are located directly adjacent to the V3 loop. The V3 loop comprises a highly conserved tetrapeptide sequence, GPGR (residues 312 to 315) (Ivanhoff et al., Virology, 187(2) 1992). HIV-1 cellular entry depends on the interaction of the V3 loop region with an HIV co-receptor, commonly CCR5 or CXCR4. The V3 loop comprises: (i) the base (residues 296–299), (ii) the stem (residues 300–303 and 321–326), and (iii) the crown (residues 304–320) (Friedrich et al., Nature Communications 12, 6705 (2021)). A consensus sequence of the V3 region of gp120 (Milich et al., J Virol., 67(9):5623-5634 (1993)) is provided below: CTRPNNNTRKSIHIGPGRAFYTTGEIIGDIRQAHC (SEQ ID NO: 54) It is understood that the consensus sequence describes the highest frequency of residues emerging on each position of this region across multiple subtypes, but that the V3 loop region of a particular strain may exhibit sequence variability. A “V3-bNAb” or “anti-V3 bNAb” is a bNAb that binds within the V3 loop region. A V3- bNAb may also be referred to herein as an anti-V3 antibody. A V3-bNAb may bind the N332 glycan in the V3 loop region and / or other N-linked glycosylation sites within and adjacent to the V3 loop region. “V1 / V2 Apex”, “V1 / V2 loop”, “V2 Apex” or “Apex” as used herein refers to an important region of gp120 known in the art that contains the receptor binding site which interactswith host cell receptors like CD4 and coreceptors like CCR5 or CXCR4. The Apex region plays acrucial role in the initial stages of HIV infection by mediating the attachment of the virus to targetcells and facilitating viral entry. A consensus sequence of the Apex region of gp120 is providedbelow: CTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSC (SEQID NO: 58) It is understood that the consensus sequence describes the highest frequency of residues emerging on each position of this region across multiple subtypes, but that this region of a particular strain may exhibit sequence variability. An “Apex-bNAb” or “anti-Apex bNAb” is a bNAb that binds within the V1 / V2 Apex region.An Apex-bNAb may also be referred to herein as an anti-Apex antibody. An Apex bNAb may bind atleast one complex N-glycan.“gp120-gp41 interface” or “interface” as used herein refers to a conformational non-continuous epitope located across the complex of gp120 and gp41 known in the art. A consensus,non-continuous sequence of the interface region of gp120-gp41 is provided below:SDAKAYDTVPTDPNPQTKAKRRVVNASWSNKSLEQIWN (SEQ ID NO: 59)It is understood that the consensus sequence describes the highest frequency of residues emerging on each position of this region across multiple subtypes, but that this region of a particular strain may exhibit sequence variability. An “Interface-bNAb” or “anti-interface bNAb” is a bNAb that binds within the gp120-gp41 interface region. Given that the interface epitope is a non-continuous epitope across a complexof gp120 and gp41, it is possible that an interface-bNAb may bind gp120, gp41 or across bothgp120 and gp41. An interface-bNAb may also be referred to herein as an anti-interface antibody. AnInterface bNAb may bind at least one complex N-glycan.An “N-glycan” or “N-linked glycan” is an oligosaccharide (also known as a glycan)attached to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein) via aprocess called N-glycosylation. N-glycans can be further modified by enzymes in the Golgi includingglycosyltransferases and glycosidases which gives rise to the three main types of N-glycans whichare known by the skilled person: high mannose N-glycans, complex N-glycans and hybrid N-glycans.STATEMENT OF THE INVENTIONA multimeric antigen binding protein of the invention binds to the Human ImmunodeficiencyVirus (HIV) envelope spike complex. Multimeric antigen binding proteins of the invention that bind tothe V1 / V2 apex region of gp120 or the gp120-gp41 interface region of gp120 and gp41 as well ashaving a CD4 domain that binds to the CD4bs of gp120 have been shown to effectively neutralize HIV and exhibit significantly better anti-viral activity than monospecific molecules that only bind tothe V1 / V2 apex region of gp120, the gp120-gp41 interface region of gp120 and gp41, or the CD4bsof gp120, and mixtures of these monospecific molecules. Without being bound by any particular theory, we postulate that the bispecific molecules of the invention bind the two different epitopes in the same or neighboring HIV envelope protein trimers at the same time, such that the bispecific molecules achieve stronger binding (increasedavidity) to the HIV envelope proteins. This may be as a result of the high local concentration of thebispecific molecules’ binding sites (paratopes) being “pre-positioned” around their target binding sites (epitopes) on the HIV envelope compared to their monospecific counterparts, which in turnleads to stronger anti-viral activity. In addition, we believe that CD4-induced conformational changeof the envelope spike complex (also referred to as gp160) exposes new epitopes for the bNAbportion of the binding proteins, which overcomes the low susceptibility of insensitive envelopes. This is particularly surprising in view of literature evidence. For antibodies that bind to a CD4-induced epitope, such as 17b which binds to the co-receptor binding site, or 7B2 that binds to the heptad repeat of gp41, soluble CD4 (sCD4) has beenshown to agonize their activity to neutralize HIV (PMID 30650070) or ability to deliver cytotoxic immunoconjugates into infected cells (PMID 34358190). Therefore, as a logical step, fusion of sCD4 to these antibodies have been made and shown further enhancement of activities (PMID 12584309, 20158904 and 34358190). But sCD4 also antagonizes bNAbs (broadly neutralizing antibodies) such as PGT128 from the V3 / glycan family that binds to the high mannose patch at the V3 loop, the V1 / V2 apex family which only binds to a closed trimer, and the interface family that binds the gp41 / gp120 interface. Surprisingly, as disclosed herein, when CD4 is fused to representative members of these families, we observed strong anti-viral synergy: the fused CD4-bNAb bispecifics neutralized HIV with stronger potency and broader spectrum than the mixture of CD4 with these bNAbs as well as the CD4 and individual bNAbs alone. Accordingly, in one aspect of the invention, there is provided a multimeric anti-HIV envelopespike complex -binding protein comprising: i. a means for binding to the V1 / V2 loop of a gp120 protein or the gp120-gp41interface of a gp120 and a gp41 protein and neutralizing at least 2 different strains of HIV-1; and ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of said means for binding.In some embodiments, the means for binding to the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein and neutralizing at least 2 different strains of HIV-1 isa broadly neutralizing antibody or fragment thereof. For example, the means for binding to theV1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein andneutralizing at least 2 different strains of HIV-1 may be any of the bispecific binding proteinsexemplified in Examples 6 and 7 and Figures 4-33, as well as those bispecific binding proteins withsequences as per Tables 3 and 4. Accordingly, in one aspect of the invention there is provided a multimeric anti-HIV envelope spike complex-binding protein comprising: i. a broadly neutralizing anti-HIV envelope spike complex, comprising at least oneheavy chain or light chain, wherein the antibody binds to the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein; and ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.In some embodiments, wherein the antibody binds to the V1 / V2 loop of a gp120 protein. Inother words the antibody is an anti-apex broad neutralizing antibody. In some embodiments theantibody binds the gp120-gp41 interface of a gp120 and a gp41 protein. In other words, theantibody is an anti-interface broad neutralizing antibody. In some embodiments, the broadly neutralizing antibody binds to at least one complex N-glycan at the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41protein. In some embodiments, the broadly neutralizing antibody binds to at least one complex N-glycan at the V1 / V2 loop of a gp120. In some embodiments, the broadly neutralizing antibody bindsto at least one complex N-glycan at the gp120-gp41 interface of a gp120 and a gp41 protein.Experiments disclosed herein demonstrate a role for complex N-glycan binding in thesynergistic effect seen in antigen binding proteins of the invention. In particular, when a compoundcalled kifunensine, which prevents the modification of N-glycans into complex N-glycans, is added toa PSV assay, the synergistic effect of the bispecific proteins tested is lost. Without being bound bytheory, it is postulated that a broadly neutralizing antibody (or fragment thereof) alone has a certainaffinity to at least one N-glycan as well as its “main” affinity to the target epitope (having a certainamino acid binding sequence) within the HIV envelope spike protein complex. Thus, if the targetepitope is not present at 100% identity, the HIV envelope spike protein complex is resistant tobinding because the affinity for the N-glycan only is too low. However, in multimeric antigen bindingproteins of the invention, the addition of a CD4 domain allows for anchoring the antibody to the HIVenvelope spike protein complex. As a result, the antibody is located very closely to a small numberof N-glycans which the antibody can bind to, creating the observed synergy (e.g. greatly improved IC50 compared to the antibody alone, the CD4 domain alone or a mixture of the two components). As such, N-glycan binding also facilitates improved binding of the antibody portion of the multimeric protein to a target sequence, which allows, a greater breadth of binding across different HIVenvelopes having sequence variation at a particular epitope and further allows for some variation inthe sequence of the broadly neutralizing antibody whilst retaining binding ability.One skilled in the art can ascertain whether an antigen binding protein is binding viacomplex N-glycan binding by methods known in the art. For example, one may analyse the x-raycrystal structure to visualize binding of an antigen binding protein to N-glycans. In another example,one may de-glycosylate HIV virus and / or the HIV envelope spike protein complex using Endo Ftreatment, which uses multiple enzymes that removes N-linked glycans, wherein disruption ofbinding after such treatment suggests N-glycan binding by the antigen binding protein. In anotherexample, the kifunensine experiments disclosed herein may be used in a similar way.In one aspect of the invention there is provided a multimeric anti-HIV envelope spike complex -binding protein comprising: i. a broadly neutralizing anti-HIV envelope spike complex antibody , comprising at leastone heavy chain or light chain, wherein the antibody binds to at least one complex N-glycan on a gp120 or a gp41 protein; andii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.In some embodiments, the antibody binds to the V1 / V2 loop of a gp120 protein. In some embodiments the antibody binds the gp120-gp41 interface of a gp120 and a gp41 protein. Again, in some embodiments, the broadly neutralizing antibody binds to at least onecomplex N-glycan at the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 anda gp41 protein. In some embodiments, the broadly neutralizing antibody binds to at least onecomplex N-glycan at the V1 / V2 loop of a gp120. In some embodiments, the broadly neutralizingantibody binds to at least one complex N-glycan at the gp120-gp41 interface of a gp120 and a gp41 protein. In some embodiments, the binding protein is a bispecific binding protein. Such bispecific binding proteins may be any of the bispecific binding proteins exemplified in Examples 6 and 7 and Figures 4-33, as well as those bispecific binding proteins with sequences as per Tables 3 and 4. The following sections will describe particular features of the multimeric binding proteins of the invention including bispecific binding proteins. CD4 Domains CD4 domains of the invention include SEQ ID NOs: 1-21. In an embodiment of the invention, the CD4 domain is a CD4 D1 domain. In an embodiment, the CD4 domain is a human CD4 domain. CD4 D1 domains include human wild-type D1 (SEQ ID NO:3), mD1.22 (SEQ ID NO:4) also known as D1m, and further variants of mD1.22 (SEQ ID NOs: 5-21). In some embodiments, the CD4 domain has a sequence that is at least 90%, 95%, 97%, 98% or 99% identical to SEQ ID NO: 3 or 4. In an embodiment of the invention, the CD4 domain is a CD4 D1D2 domain. In an embodiment, the CD4 domain is a human CD4 D1D2 domain. CD4 D1D2 domains include human wild-type D1D2 (SEQ ID NO:1) and mD1.22-D2 (SEQ ID NO:2). In some embodiments, the CD4 domain has a sequence that is at least 90%, 95%, 97%, 98% or 99% identical to SEQ ID NO:1 or 2. In an aspect of the invention, a stabilized CD4 domain is provided. In an embodiment of theinvention, a stabilized CD4 D1 domain is provided. In an embodiment, the CD4 domain is thermally stable, i.e., thermostable. In an embodiment, the CD4 domain is a thermostable CD4 D1 domain. In an embodiment of the invention, the CD4 domain comprises one or more stabilizingmutations compared to the wild type sequence. In an embodiment, the stabilizing mutations are inthe CD4 D1 domain. In an embodiment, the CD4 D1 domain comprises at least one mutation at position 5, 23, 55, 79, 96 and / or 98 of SEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises one or more mutations at positions 8, 11, 13, 21, 25, 27, 38, 52, 58, 61, 65, 70, 72, 87, 91 and or 99 of SEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises a mutation at position 8 orSEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises a mutation at positions 11and 72 of SEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises mutation at positions 8 and 99. In an embodiment, the CD4 D1 domain comprises at least one mutation selected from: L5Y, S23N, A55V, I79P, L96V and / or F98V mutations. In an embodiment, the CD4 D1 domain comprises one or more mutations selected from: K8C, K8I, K8V, T11C, E13C, K21C, Q25E, H27C, H27D, G38C,N52W, R58N, R58T, R58V, L61M, G65C, I70C, K72C, E87G, E91H, E91Q, and / or G99C. In anembodiment, the CD4 D1 domain comprises a K8I mutation. In an embodiment, the CD4 D1 domaincomprises a K8V mutation. In an embodiment, the CD4 D1 domain comprises T1C and K72Cmutations. In an embodiment, the CD4 D1 domain comprises K8C and G99C mutations. In all ofthese embodiments, these mutations may be compared to a wild type sequence as per SEQ ID NO: 1 or 3. CD4 domains of the invention comprising novel and inventive stabilizing mutations include SEQ ID NOs:5-21. In some embodiments, the CD4 domain is a SEQ ID NOs: 5-15. In some embodiments, the CD4 domain has a sequence that is at least 90%, 95%, 97%, 98% or 99%identical to SEQ ID NO: 5-21. In some embodiments, the CD4 domain has a sequence that is atleast 90%, 95%, 97%, 98% or 99% identical to SEQ ID NO: 5-15. Increased thermostability may be reflected in a melting temperature (Tm) increase of, for example, between 1 and 50 ºC; in particular between 1 and 30 ºC; in particular between 1 and 25 ºC, in particular between 1 and 21 ºC, more particularly between 5 and 21 ºC. The Tm increase is determined by measuring the Tm of the CD4 domain(s) comprising one or more stabilizing mutations and subtracting the Tm of the corresponding CD4 domain(s) without said mutation(s). For example, measuring the Tm of a stabilized CD4 D1 domain and subtracting the Tm of the wild-type CD4 D1 domain. In an embodiment, the Tm increase is about 8 ºC. In an embodiment, the Tm increase is about 9 ºC. In an embodiment, the Tm increase is about 12 ºC. In an embodiment, the Tm increase is about 21 ºC. In an embodiment, the Tm of the CD4 domain is above 70 ºC. In an embodiment, the Tm of the CD4 domain is between 70 ºC and 95 ºC. In an embodiment, the Tm of the CD4 domain is between 75 ºC and 95 ºC. In an embodiment, the Tm of the CD4 domain is between 75 ºC and 91 ºC. In an embodiment, the Tm of the CD4 domain is about 76 ºC, about 77 ºC, about 78 ºC, about 79 ºC, about 80 ºC, about 81 ºC, about 82 ºC, about 83 ºC, about 84 ºC, about 85 ºC, about 86 ºC, about 87 ºC, about 88 ºC, about 89 ºC, or about 90 ºC. In an embodiment, the Tm of the CD4 domain is about 90 ºC. In an embodiment, the Tm of the CD4 domain is about 89 ºC. Tm may be determined by routine methods known in the art or as set out in the Examples. In an embodiment, Tm is determined using the Prometheus System (NanoTemper, München Germany). In some embodiments of the invention, a CD4 domain as described above may be attacheddirectly to a broadly neutralizing antibody, by “directly” is meant that a CD4 domain is covalentlybonded to a broadly neutralizing antibody without the use of an additional linking chemical orpeptide sequence. In other embodiments, the CD4 domain as described above may be attached by alinker (for example a peptide linker such as those shown in SEQ ID: 30-35).Anti-HIV envelope spike complex broadly neutralizing antibodiesAn antigen binding protein of the invention may comprise a broadly neutralizing antibodyhaving heavy chain CDRs (CDRH1, CDRH2, and CDRH3) as set out in any row of Table 3. An antigenbinding protein of the invention may comprise a broadly neutralizing antibody having light chainCDRs (CDRL1, CDRL2, and CDRL3) as set out in any row of Table 3. An antigen binding protein ofthe invention may comprise a broadly neutralizing antibody having a set of six CDRs (CDRH1,CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3) as set out in any row of Table 3. An antigen binding protein of the invention may comprise a broadly neutralizing antibodyhaving a VH domain as set out in Table 4. An antigen binding protein of the invention may comprisea broadly neutralizing antibody having a VL domain as set out in Table 4. An antigen bindingprotein of the invention may comprise a broadly neutralizing antibody having a pair of variabledomains (a VH and a VL) as set out in any row of Table 4.Table 3: SEQ ID NOs for the complementarity determining regions (CDRs) of broadly neutralizingantibodies CDRH1 CDRH2 CDRH3 CDRL1 CDRL2 CDRL3Interface-bNAb17 90 91 92 93 94 95ecafInterface-bNAb18 101 102 103 104 105 106retnInterface-bNAb19 112 113 114 115 116 117IInterface-bNAb20 123 124 125 126 127 128Interface-bNAb21 134 135 136 137 138 139Interface-bNAb22 145 146 147 148 149 150Interface-bNAb23 156 157 158 159 160 161Interface-bNAb24 167 168 169 170 171 172Interface-bNAb25 178 179 180 181 182 183Interface-bNAb26 189 190 191 192 193 194Interface-bNAb27 200 201 202 203 204 205Interface-bNAb29 211 212 213 214 215 216Interface-bNAb30 222 223 224 225 226 227Interface-bNAb31 233 234 235 236 237 238Apex-bNAb1 244 245 246 247 248 249Apex-bNAb2 255 256 257 258 259 260Apex-bNAb3 266 267 268 269 270 271Apex-bNAb4 277 278 279 280 281 282Apex-bNAb5 288 289 290 291 292 293Apex-bNAb6 299 300 301 302 303 304Apex-bNAb7 310 311 312 313 314 315xApex-bNAb8 321 322 323 324 325 326ep AApex-bNAb9 332 333 334 335 336 337Apex-bNAb10 343 344 345 346 347 348Apex-bNAb11 354 355 356 357 358 359Apex-bNAb12 365 366 367 368 369 370Apex-bNAb13 376 377 378 379 380 381Apex-bNAb14 387 388 389 390 391 392Apex-bNAb15 398 399 400 401 402 403Apex-bNAb16 409 410 411 412 413 414Table 4: SEQ ID NOs for the variable heavy regions (VH) and variable light regions (VL) variable domain pairs), and the full heavy chains (with and without LS mutations) chains (LC) broadly neutralizing antibodies. Variable domain pair Full chain pairVH VL Full HCFull HC Full LC (no LS) (LS) Interface-bNAb17 96 97 98 99 100Interface-bNAb18 107 108 109 110 111Interface-bNAb19 118 119 120 121 122Interface-bNAb20 129 130 131 132 133Interface-bNAb21 140 141 142 143 144Interface-bNAb22 151 152 153 154 155ecafInterface-bNAb23 162 163 164 165 166retnInterface-bNAb24 173 174 175 176 177IInterface-bNAb25 184 185 186 187 188Interface-bNAb26 195 196 197 198 199Interface-bNAb27 206 207 208 209 210Interface-bNAb29 217 218 219 220 221Interface-bNAb30 228 229 230 231 232Interface-bNAb31 239 240 241 242 243Apex-bNAb1 250 251 252 253 254Apex-bNAb2 261 262 263 264 265Apex-bNAb3 272 273 274 275 276Apex-bNAb4 283 284 285 286 287Apex-bNAb5 294 295 296 297 298Apex-bNAb6 305 306 307 308 309Apex-bNAb7 316 317 318 319 320xApex-bNAb8 327 328 329 330 331ep AApex-bNAb9 338 339 340 341 342Apex-bNAb10 349 350 351 352 353Apex-bNAb11 360 361 362 363 364Apex-bNAb12 371 372 373 374 375Apex-bNAb13 382 383 384 385 386Apex-bNAb14 393 394 395 396 397Apex-bNAb15 404 405 406 407 408Apex-bNAb16 415 416 417 418 419 Anti-interface bNAbs In particular, an antigen binding protein of the invention may comprise an anti-interfacebNAb or a fragment thereof (i.e. a broadly neutralizing antibody or fragment binds to the gp120-gp41 interface of a gp120 and a gp41 protein). A fragment may include Fab, F(ab’)2, Fv, disulphide linked Fv, single chain Fv (scFv), disulphide-linked scFv, diabodies, TANDABS, etc. and modifiedversions of any of the foregoing. For example, scFv variants of anti-interface bNAbs have beendescribed in van Dorsten et al. 2021 (PMID: 34603312). An anti-interface bNAb or fragment thereof includes an antibody comprising a set of CDRs (CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3)as set out in rows 1 to 14 of Table 3 (interface bNAbs17-31).An anti-interface bNAb or fragment thereof also includes an antibody comprising a pair ofvariable domains (a VH and VL) set out in rows 1 to 14 of Table 4 (interface bNAbs17-31).An anti-interface bNAb may be an antibody comprising a heavy chain (HC), with or withoutM428L / N434S (EU numbering) ‘LS’ mutations, and a light chain (LC) as set out in rows 1 to 14 ofTable 4 (interface bNAbs17-31). In an embodiment, the HC comprises LS.In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 90, a CDRH2 of SEQ ID NO: 91, a CDRH3 of SEQ ID NO: 92, a CDRL1 of SEQ ID NO: 93, aCDRL2 of SEQ ID NO: 94 and a CDRL3 of SEQ ID NO: 95. In an embodiment, the anti-interfacebNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 101, a CDRH2 of SEQ ID NO: 102, aCDRH3 of SEQ ID NO: 103, a CDRL1 of SEQ ID NO: 104, a CDRL2 of SEQ ID NO: 105 and a CDRL3of SEQ ID NO: 106. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 112, a CDRH2 of SEQ ID NO: 113, a CDRH3 of SEQ ID NO: 114, a CDRL1 ofSEQ ID NO: 115, a CDRL2 of SEQ ID NO: 116 and a CDRL3 of SEQ ID NO: 117. In an embodiment,the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 123, a CDRH2 of SEQ ID NO: 124, a CDRH3 of SEQ ID NO: 125, a CDRL1 of SEQ ID NO: 126, a CDRL2 of SEQ IDNO: 127 and a CDRL3 of SEQ ID NO: 128. In an embodiment, the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 134, a CDRH2 of SEQ ID NO: 135, a CDRH3 of SEQ IDNO: 136, a CDRL1 of SEQ ID NO: 137, a CDRL2 of SEQ ID NO: 138 and a CDRL3 of SEQ ID NO:139. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 145, a CDRH2 of SEQ ID NO: 146, a CDRH3 of SEQ ID NO: 147, a CDRL1 of SEQ ID NO: 148, aCDRL2 of SEQ ID NO: 149 and a CDRL3 of SEQ ID NO: 150. In an embodiment, the anti-interfacebNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 156, a CDRH2 of SEQ ID NO: 157, aCDRH3 of SEQ ID NO: 158, a CDRL1 of SEQ ID NO: 159, a CDRL2 of SEQ ID NO: 160 and a CDRL3of SEQ ID NO: 161. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 167, a CDRH2 of SEQ ID NO: 168, a CDRH3 of SEQ ID NO: 169, a CDRL1 ofSEQ ID NO: 170, a CDRL2 of SEQ ID NO: 171 and a CDRL3 of SEQ ID NO: 172. In an embodiment,the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 178, a CDRH2 of SEQ ID NO: 179, a CDRH3 of SEQ ID NO: 180, a CDRL1 of SEQ ID NO: 181, a CDRL2 of SEQ IDNO: 182 and a CDRL3 of SEQ ID NO: 183. In an embodiment, the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 189, a CDRH2 of SEQ ID NO: 190, a CDRH3 of SEQ IDNO: 191, a CDRL1 of SEQ ID NO: 192, a CDRL2 of SEQ ID NO: 193 and a CDRL3 of SEQ ID NO:194. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 200, a CDRH2 of SEQ ID NO: 201, a CDRH3 of SEQ ID NO: 202, a CDRL1 of SEQ ID NO: 203, aCDRL2 of SEQ ID NO: 204 and a CDRL3 of SEQ ID NO: 205. In an embodiment, the anti-interfacebNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 211, a CDRH2 of SEQ ID NO: 212, aCDRH3 of SEQ ID NO: 213, a CDRL1 of SEQ ID NO: 214, a CDRL2 of SEQ ID NO: 215 and a CDRL3of SEQ ID NO: 216. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 222, a CDRH2 of SEQ ID NO: 223, a CDRH3 of SEQ ID NO: 224, a CDRL1 ofSEQ ID NO: 225, a CDRL2 of SEQ ID NO: 226 and a CDRL3 of SEQ ID NO: 227. In an embodiment,the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 233, a CDRH2 of SEQ ID NO: 234, a CDRH3 of SEQ ID NO: 235, a CDRL1 of SEQ ID NO: 236, a CDRL2 of SEQ IDNO: 237 and a CDRL3 of SEQ ID NO: 238.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 96 and a VL domain having at least 95%sequence identity to SEQ ID NO: 97, optionally wherein the anti-interface bNAb or fragment thereofcomprises a CDRH1 of SEQ ID NO: 90, a CDRH2 of SEQ ID NO: 91, a CDRH3 of SEQ ID NO: 92, aCDRL1 of SEQ ID NO: 93, a CDRL2 of SEQ ID NO: 94 and a CDRL3 of SEQ ID NO: 95.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 107 and a VL domain having at least 95% sequence identity to SEQ ID NO: 108, optionally wherein the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 101, a CDRH2 of SEQ ID NO: 102, a CDRH3 of SEQ IDNO: 103, a CDRL1 of SEQ ID NO: 104, a CDRL2 of SEQ ID NO: 105 and a CDRL3 of SEQ ID NO:106. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 118 and a VL domain having at least 95% sequence identity to SEQ ID NO: 119, optionally wherein the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 112, a CDRH2 of SEQ ID NO: 113, a CDRH3 of SEQ IDNO: 114, a CDRL1 of SEQ ID NO: 115, a CDRL2 of SEQ ID NO: 116 and a CDRL3 of SEQ ID NO:117. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 129 and a VL domain having at least 95%sequence identity to SEQ ID NO: 130, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 123, a CDRH2 of SEQ ID NO: 124, a CDRH3 of SEQ IDNO: 125, a CDRL1 of SEQ ID NO: 126, a CDRL2 of SEQ ID NO: 127 and a CDRL3 of SEQ ID NO:128. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 140 and a VL domain having at least 95%sequence identity to SEQ ID NO: 141, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 134, a CDRH2 of SEQ ID NO: 135, a CDRH3 of SEQ IDNO: 136, a CDRL1 of SEQ ID NO: 137, a CDRL2 of SEQ ID NO: 138 and a CDRL3 of SEQ ID NO:139. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 151 and a VL domain having at least 95%sequence identity to SEQ ID NO: 152, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 145, a CDRH2 of SEQ ID NO: 146, a CDRH3 of SEQ IDNO: 147, a CDRL1 of SEQ ID NO: 148, a CDRL2 of SEQ ID NO: 149 and a CDRL3 of SEQ ID NO:150. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 162 and a VL domain having at least 95%sequence identity to SEQ ID NO: 163, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 156, a CDRH2 of SEQ ID NO: 157, a CDRH3 of SEQ IDNO: 158, a CDRL1 of SEQ ID NO: 159, a CDRL2 of SEQ ID NO: 160 and a CDRL3 of SEQ ID NO:161. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 173 and a VL domain having at least 95%sequence identity to SEQ ID NO: 174, optionally wherein the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 167, a CDRH2 of SEQ ID NO: 168, a CDRH3 of SEQ IDNO: 169, a CDRL1 of SEQ ID NO: 170, a CDRL2 of SEQ ID NO: 171 and a CDRL3 of SEQ ID NO:172. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 184 and a VL domain having at least 95%sequence identity to SEQ ID NO: 185, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 178, a CDRH2 of SEQ ID NO: 179, a CDRH3 of SEQ IDNO: 180, a CDRL1 of SEQ ID NO: 181, a CDRL2 of SEQ ID NO: 182 and a CDRL3 of SEQ ID NO:183. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 195 and a VL domain having at least 95%sequence identity to SEQ ID NO: 196, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 189, a CDRH2 of SEQ ID NO: 190, a CDRH3 of SEQ IDNO: 191, a CDRL1 of SEQ ID NO: 192, a CDRL2 of SEQ ID NO: 193 and a CDRL3 of SEQ ID NO:194. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 206 and a VL domain having at least 95%sequence identity to SEQ ID NO: 207, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 200, a CDRH2 of SEQ ID NO: 201, a CDRH3 of SEQ IDNO: 202, a CDRL1 of SEQ ID NO: 203, a CDRL2 of SEQ ID NO: 204 and a CDRL3 of SEQ ID NO:205. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 217 and a VL domain having at least 95%sequence identity to SEQ ID NO: 218, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 211, a CDRH2 of SEQ ID NO: 212, a CDRH3 of SEQ IDNO: 213, a CDRL1 of SEQ ID NO: 214, a CDRL2 of SEQ ID NO: 215 and a CDRL3 of SEQ ID NO:216. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 228 and a VL domain having at least 95%sequence identity to SEQ ID NO: 229, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 222, a CDRH2 of SEQ ID NO: 223, a CDRH3 of SEQ IDNO: 224, a CDRL1 of SEQ ID NO: 225, a CDRL2 of SEQ ID NO: 226 and a CDRL3 of SEQ ID NO:227. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domainhaving at least 95% sequence identity to SEQ ID NO: 239 and a VL domain having at least 95%sequence identity to SEQ ID NO: 240, optionally wherein the anti-interface bNAb or fragmentthereof comprises a CDRH1 of SEQ ID NO: 233, a CDRH2 of SEQ ID NO: 234, a CDRH3 of SEQ IDNO: 235, a CDRL1 of SEQ ID NO: 236, a CDRL2 of SEQ ID NO: 237 and a CDRL3 of SEQ ID NO:238.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain ofSEQ ID NO: 96 and a VL domain of SEQ ID NO: 97. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 107 and a VL domain of SEQ ID NO: 108.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ IDNO: 118 and a VL domain of SEQ ID NO: 119. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 129 and a VL domain of SEQ ID NO: 130.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ IDNO: 140 and a VL domain of SEQ ID NO: 141. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 151 and a VL domain of SEQ ID NO: 152.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ IDNO: 162 and a VL domain of SEQ ID NO: 163. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 173 and a VL domain of SEQ ID NO: 174.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ IDNO: 184 and a VL domain of SEQ ID NO: 185. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 195 and a VL domain of SEQ ID NO: 196.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ IDNO: 206 and a VL domain of SEQ ID NO: 207. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 217 and a VL domain of SEQ ID NO: 218.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ IDNO: 228 and a VL domain of SEQ ID NO: 229. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 239 and a VL domain of SEQ ID NO: 240.In an embodiment, the anti-interface bNAb or fragment thereof, comprises a heavy chain(HC) having at least 95% sequence identity to SEQ ID NO: 98 or 99 and a light chain (LC) having atleast 95% sequence identity to SEQ ID NO: 100. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 109 or 110and a LC having at least 95% sequence identity to SEQ ID NO: 111. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQID NO: 120 or 121 and a LC having at least 95% sequence identity to SEQ ID NO: 122. In anembodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95%sequence identity to SEQ ID NO: 131 or 132 and a LC having at least 95% sequence identity to SEQID NO: 133. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC havingat least 95% sequence identity to SEQ ID NO: 142 or 143 and a LC having at least 95% sequenceidentity to SEQ ID NO: 144. In an embodiment, the anti-interface bNAb or fragment thereof,comprises a HC having at least 95% sequence identity to SEQ ID NO: 153 or 154 and a LC having atleast 95% sequence identity to SEQ ID NO: 155. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 164 or 165and a LC having at least 95% sequence identity to SEQ ID NO: 166. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQID NO: 175 or 176 and a LC having at least 95% sequence identity to SEQ ID NO: 177. In anembodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95%sequence identity to SEQ ID NO: 186 or 187 and a LC having at least 95% sequence identity to SEQID NO: 188. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC havingat least 95% sequence identity to SEQ ID NO: 197 or 198 and a LC having at least 95% sequenceidentity to SEQ ID NO: 199. In an embodiment, the anti-interface bNAb or fragment thereof,comprises a HC having at least 95% sequence identity to SEQ ID NO: 208 or 209 and a LC having atleast 95% sequence identity to SEQ ID NO: 210. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 219 or 220and a LC having at least 95% sequence identity to SEQ ID NO: 221. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQID NO: 230 or 231 and a LC having at least 95% sequence identity to SEQ ID NO: 232. In anembodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95%sequence identity to SEQ ID NO: 241 or 242 and a LC having at least 95% sequence identity to SEQID NO: 243. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a heavy chain(HC) of SEQ ID NO: 98 or 99 and a light chain (LC) of SEQ ID NO: 100. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 109 or 110 and a LC of SEQ IDNO: 111. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ IDNO: 120 or 121 and a LC of SEQ ID NO: 122. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a HC of SEQ ID NO: 131 or 132 and a LC of SEQ ID NO: 133. In anembodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 142 or143 and a LC of SEQ ID NO: 144. In an embodiment, the anti-interface bNAb or fragment thereof,comprises a HC of SEQ ID NO: 153 or 154 and a LC of SEQ ID NO: 155. In an embodiment, theanti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 164 or 165 and a LC of SEQID NO: 166. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQID NO: 175 or 176 and a LC of SEQ ID NO: 178. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a HC of SEQ ID NO: 186 or 187 and a LC of SEQ ID NO: 188. In anembodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 197 or198 and a LC of SEQ ID NO: 199. In an embodiment, the anti-interface bNAb or fragment thereof,comprises a HC of SEQ ID NO: 208 or 209 and a LC of SEQ ID NO: 210. In an embodiment, theanti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 219 or 220 and a LC of SEQID NO: 221. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQID NO: 230 or 231 and a LC of SEQ ID NO: 232. In an embodiment, the anti-interface bNAb orfragment thereof, comprises a HC of SEQ ID NO: 241 or 242 and a LC of SEQ ID NO: 243.Anti-apex bNAbs In particular, an antigen binding protein of the invention may comprise an anti-apex bNAb ora fragment thereof (i.e. a broadly neutralizing antibody or fragment binds to the V1 / V2 loop of agp120 protein)). A fragment may include Fab, F(ab’)2, Fv, disulphide linked Fv, single chain Fv (scFv), disulphide-linked scFv, diabodies, TANDABS, etc. and modified versions of any of the foregoing. For example, scFv variants of anti-apex bNAbs have been described in van Dorsten et al.2022 (PMID: 34935437). An anti-apex bNAb or fragment thereof includes an antibody comprising aset of CDRs (CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3) as set out in rows 15 to 30 ofTable 3 (Apex bNAb1-16).An anti-apex bNAb or fragment thereof also includes an antibody comprising a pair ofvariable domains (a VH and VL) set out in rows 15 to 30 of Table 4 (Apex-bNAb1-16).An anti- apex bNAb may be an antibody comprising a heavy chain (HC), with or withoutM428L / N434S (EU numbering) ‘LS’ mutations, and a light chain (LC) as set out in rows 15 to 30 ofTable 4 (Apex bNAb1-16). In an embodiment, the HC comprises LS.In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 244, a CDRH2 of SEQ ID NO: 245, a CDRH3 of SEQ ID NO: 246, a CDRL1 of SEQ ID NO: 247, aCDRL2 of SEQ ID NO: 248 and a CDRL3 of SEQ ID NO: 249. In an embodiment, the anti-apex bNAbor fragment thereof comprises a CDRH1 of SEQ ID NO: 255, a CDRH2 of SEQ ID NO: 256, a CDRH3 of SEQ ID NO: 257, a CDRL1 of SEQ ID NO: 258, a CDRL2 of SEQ ID NO: 259 and a CDRL3 of SEQ ID NO: 260. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 266, a CDRH2 of SEQ ID NO: 267, a CDRH3 of SEQ ID NO: 268, a CDRL1 of SEQ ID NO:269, a CDRL2 of SEQ ID NO: 270 and a CDRL3 of SEQ ID NO: 271. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 277, a CDRH2 of SEQ ID NO:278, a CDRH3 of SEQ ID NO: 279, a CDRL1 of SEQ ID NO: 280, a CDRL2 of SEQ ID NO: 281 and aCDRL3 of SEQ ID NO: 282. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 288, a CDRH2 of SEQ ID NO: 289, a CDRH3 of SEQ ID NO: 290, a CDRL1 ofSEQ ID NO: 291, a CDRL2 of SEQ ID NO: 292 and a CDRL3 of SEQ ID NO: 293. In an embodiment,the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 299, a CDRH2 of SEQ ID NO: 300, a CDRH3 of SEQ ID NO: 301, a CDRL1 of SEQ ID NO: 302, a CDRL2 of SEQ ID NO: 303 and a CDRL3 of SEQ ID NO: 304. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 310, a CDRH2 of SEQ ID NO: 311, a CDRH3 of SEQ ID NO: 312,a CDRL1 of SEQ ID NO: 313, a CDRL2 of SEQ ID NO: 314 and a CDRL3 of SEQ ID NO: 315. In anembodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 321, a CDRH2 of SEQ ID NO: 322, a CDRH3 of SEQ ID NO: 323, a CDRL1 of SEQ ID NO: 324, a CDRL2 ofSEQ ID NO: 325 and a CDRL3 of SEQ ID NO: 326. In an embodiment, the anti-apex bNAb orfragment thereof comprises a CDRH1 of SEQ ID NO: 332, a CDRH2 of SEQ ID NO: 333, a CDRH3 ofSEQ ID NO: 334, a CDRL1 of SEQ ID NO: 335, a CDRL2 of SEQ ID NO: 336 and a CDRL3 of SEQ IDNO: 337. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ IDNO: 343, a CDRH2 of SEQ ID NO: 344, a CDRH3 of SEQ ID NO: 345, a CDRL1 of SEQ ID NO: 346, aCDRL2 of SEQ ID NO: 347 and a CDRL3 of SEQ ID NO: 348. In an embodiment, the anti-apex bNAbor fragment thereof comprises a CDRH1 of SEQ ID NO: 354, a CDRH2 of SEQ ID NO: 355, a CDRH3of SEQ ID NO: 356, a CDRL1 of SEQ ID NO: 357, a CDRL2 of SEQ ID NO: 358 and a CDRL3 of SEQID NO: 359. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 365, a CDRH2 of SEQ ID NO: 366, a CDRH3 of SEQ ID NO: 367, a CDRL1 of SEQ ID NO:368, a CDRL2 of SEQ ID NO: 369 and a CDRL3 of SEQ ID NO: 370. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 376, a CDRH2 of SEQ ID NO:377, a CDRH3 of SEQ ID NO: 378, a CDRL1 of SEQ ID NO: 379, a CDRL2 of SEQ ID NO: 380 and aCDRL3 of SEQ ID NO: 381. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 387, a CDRH2 of SEQ ID NO: 388, a CDRH3 of SEQ ID NO: 389, a CDRL1 ofSEQ ID NO: 390, a CDRL2 of SEQ ID NO: 391 and a CDRL3 of SEQ ID NO: 392. In an embodiment,the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 398, a CDRH2 of SEQ ID NO: 399, a CDRH3 of SEQ ID NO: 400, a CDRL1 of SEQ ID NO: 401, a CDRL2 of SEQ ID NO: 402 and a CDRL3 of SEQ ID NO: 403. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 409, a CDRH2 of SEQ ID NO: 410, a CDRH3 of SEQ ID NO: 411,a CDRL1 of SEQ ID NO: 412, a CDRL2 of SEQ ID NO: 413 and a CDRL3 of SEQ ID NO: 414.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 250 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 251, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 244, a CDRH2 of SEQ ID NO: 245, a CDRH3 of SEQ ID NO: 246, a CDRL1 ofSEQ ID NO: 247, a CDRL2 of SEQ ID NO: 248 and a CDRL3 of SEQ ID NO: 249.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 261 and a VL domain having at least 95% sequence identity to SEQ ID NO: 262, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 255, a CDRH2 of SEQ ID NO: 256, a CDRH3 of SEQ ID NO: 257, a CDRL1 ofSEQ ID NO: 258, a CDRL2 of SEQ ID NO: 259 and a CDRL3 of SEQ ID NO: 260.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 272 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 273, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 266, a CDRH2 of SEQ ID NO: 267, a CDRH3 of SEQ ID NO: 268, a CDRL1 ofSEQ ID NO: 269, a CDRL2 of SEQ ID NO: 270 and a CDRL3 of SEQ ID NO: 271.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 283 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 284, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 277, a CDRH2 of SEQ ID NO: 278, a CDRH3 of SEQ ID NO: 279, a CDRL1 ofSEQ ID NO: 280, a CDRL2 of SEQ ID NO: 281 and a CDRL3 of SEQ ID NO: 282.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 294 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 295, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 288, a CDRH2 of SEQ ID NO: 289, a CDRH3 of SEQ ID NO: 290, a CDRL1 ofSEQ ID NO: 291, a CDRL2 of SEQ ID NO: 292 and a CDRL3 of SEQ ID NO: 293.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 305 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 306 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 299, a CDRH2 of SEQ ID NO: 300, a CDRH3 of SEQ ID NO: 301, a CDRL1 ofSEQ ID NO: 302, a CDRL2 of SEQ ID NO: 303 and a CDRL3 of SEQ ID NO: 304.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 316 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 317 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 310, a CDRH2 of SEQ ID NO: 311, a CDRH3 of SEQ ID NO: 312, a CDRL1 ofSEQ ID NO: 313, a CDRL2 of SEQ ID NO: 314 and a CDRL3 of SEQ ID NO: 315.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 327 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 328 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 321, a CDRH2 of SEQ ID NO: 322, a CDRH3 of SEQ ID NO: 323, a CDRL1 ofSEQ ID NO: 324, a CDRL2 of SEQ ID NO: 325 and a CDRL3 of SEQ ID NO: 326. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 338 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 339 optionally wherein the anti-apex bNAb or fragment thereof comprises acomprises a CDRH1 of SEQ ID NO: 332, a CDRH2 of SEQ ID NO: 333, a CDRH3 of SEQ ID NO: 334,a CDRL1 of SEQ ID NO: 335, a CDRL2 of SEQ ID NO: 336 and a CDRL3 of SEQ ID NO: 337.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 349 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 350 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 343, a CDRH2 of SEQ ID NO: 344, a CDRH3 of SEQ ID NO: 345, a CDRL1 ofSEQ ID NO: 346, a CDRL2 of SEQ ID NO: 347 and a CDRL3 of SEQ ID NO: 348.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 360 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 361 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 354, a CDRH2 of SEQ ID NO: 355, a CDRH3 of SEQ ID NO: 356, a CDRL1 ofSEQ ID NO: 357, a CDRL2 of SEQ ID NO: 358 and a CDRL3 of SEQ ID NO: 359.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 371 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 372 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 365, a CDRH2 of SEQ ID NO: 366, a CDRH3 of SEQ ID NO: 367, a CDRL1 ofSEQ ID NO: 368, a CDRL2 of SEQ ID NO: 369 and a CDRL3 of SEQ ID NO: 370.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 382 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 383 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 376, a CDRH2 of SEQ ID NO: 377, a CDRH3 of SEQ ID NO: 378, a CDRL1 ofSEQ ID NO: 379, a CDRL2 of SEQ ID NO: 380 and a CDRL3 of SEQ ID NO: 381.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 393 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 394 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 387, a CDRH2 of SEQ ID NO: 388, a CDRH3 of SEQ ID NO: 389, a CDRL1 ofSEQ ID NO: 390, a CDRL2 of SEQ ID NO: 391 and a CDRL3 of SEQ ID NO: 392.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 404 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 405 optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 398, a CDRH2 of SEQ ID NO: 399, a CDRH3 of SEQ ID NO: 400, a CDRL1 ofSEQ ID NO: 401, a CDRL2 of SEQ ID NO: 402 and a CDRL3 of SEQ ID NO: 403.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain havingat least 95% sequence identity to SEQ ID NO: 415 and a VL domain having at least 95% sequenceidentity to SEQ ID NO: 416 optionally wherein the anti-apex bNAb or fragment thereof comprises aCDRH1 of SEQ ID NO: 409, a CDRH2 of SEQ ID NO: 410, a CDRH3 of SEQ ID NO: 411, a CDRL1 ofSEQ ID NO: 412, a CDRL2 of SEQ ID NO: 413 and a CDRL3 of SEQ ID NO: 414.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQID NO: 250 and a VL domain of SEQ ID NO: 251. In an embodiment, the anti-apex bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO:272 and a VL domain of SEQ ID NO: 273. In an embodiment, the anti-apex bNAb or fragmentthereof, comprises a VH domain of SEQ ID NO: 283 and a VL domain of SEQ ID NO: 284. In anembodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 294and a VL domain of SEQ ID NO: 295. In an embodiment, the anti-apex bNAb or fragment thereof,comprises a VH domain of SEQ ID NO: 305 and a VL domain of SEQ ID NO: 306. In an embodiment,the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 316 and a VLdomain of SEQ ID NO: 317. In an embodiment, the anti-apex bNAb or fragment thereof, comprisesa VH domain of SEQ ID NO: 327 and a VL domain of SEQ ID NO: 328. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 338 and a VL domain of SEQID NO: 339. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain ofSEQ ID NO: 349 and a VL domain of SEQ ID NO: 350. In an embodiment, the anti-apex bNAb orfragment thereof, comprises a VH domain of SEQ ID NO: 360 and a VL domain of SEQ ID NO: 361.In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO:371 and a VL domain of SEQ ID NO: 372. In an embodiment, the anti-apex bNAb or fragmentthereof, comprises a VH domain of SEQ ID NO: 382 and a VL domain of SEQ ID NO: 383. In anembodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 393and a VL domain of SEQ ID NO: 394. In an embodiment, the anti-apex bNAb or fragment thereof,comprises a VH domain of SEQ ID NO: 404 and a VL domain of SEQ ID NO: 405. In an embodiment,the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 415 and a VLdomain of SEQ ID NO: 416. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a heavy chain (HC)having at least 95% sequence identity to SEQ ID NO: 252 or 253 and a light chain (LC) having atleast 95% sequence identity to SEQ ID NO: 254. In an embodiment, the anti-apex bNAb orfragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 263 or 264and a LC having at least 95% sequence identity to SEQ ID NO: 265. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ IDNO: 274 or 275 and a LC having at least 95% sequence identity to SEQ ID NO: 276. In anembodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95%sequence identity to SEQ ID NO: 285 or 286 and a LC having at least 95% sequence identity to SEQID NO: 287. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having atleast 95% sequence identity to SEQ ID NO: 296 or 297 and a LC having at least 95% sequenceidentity to SEQ ID NO: 298. In an embodiment, the anti-apex bNAb or fragment thereof, comprisesa HC having at least 95% sequence identity to SEQ ID NO: 307 or 308 and a LC having at least 95%sequence identity to SEQ ID NO: 309. In an embodiment, the anti-apex bNAb or fragment thereof,comprises a HC having at least 95% sequence identity to SEQ ID NO: 318 or 319 and a LC having atleast 95% sequence identity to SEQ ID NO: 320. In an embodiment, the anti-apex bNAb orfragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 329 or 330and a LC having at least 95% sequence identity to SEQ ID NO: 331. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ IDNO: 340 or 341 and a LC having at least 95% sequence identity to SEQ ID NO: 342. In anembodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95%sequence identity to SEQ ID NO: 351 or 352 and a LC having at least 95% sequence identity to SEQID NO: 353. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having atleast 95% sequence identity to SEQ ID NO: 362 or 363 and a LC having at least 95% sequenceidentity to SEQ ID NO: 364. In an embodiment, the anti-apex bNAb or fragment thereof, comprisesa HC having at least 95% sequence identity to SEQ ID NO: 373 or 374 and a LC having at least 95%sequence identity to SEQ ID NO: 375. In an embodiment, the anti-apex bNAb or fragment thereof,comprises a HC having at least 95% sequence identity to SEQ ID NO: 384 or 385 and a LC having atleast 95% sequence identity to SEQ ID NO: 386. In an embodiment, the anti-apex bNAb orfragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 395 or 396and a LC having at least 95% sequence identity to SEQ ID NO: 397. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ IDNO: 406 or 407 and a LC having at least 95% sequence identity to SEQ ID NO: 408. In anembodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95%sequence identity to SEQ ID NO: 417 or 418 and a LC having at least 95% sequence identity to SEQID NO: 419. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a heavy chain (HC)of SEQ ID NO: 252 or 253 and a light chain (LC) of SEQ ID NO: 254. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 263 or 264 and a LC of SEQ ID NO:265. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO:274 or 275 and a LC of SEQ ID NO: 276. In an embodiment, the anti-apex bNAb or fragmentthereof, comprises a HC of SEQ ID NO: 285 or 286 and a LC of SEQ ID NO: 287. In an embodiment,the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 296 or 297 and a LC of SEQID NO: 298. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ IDNO: 307 or 308 and a LC of SEQ ID NO: 309. In an embodiment, the anti-apex bNAb or fragmentthereof, comprises a HC of SEQ ID NO: 318 or 319 and a LC of SEQ ID NO: 320. In an embodiment,the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 329 or 330 and a LC of SEQID NO: 331. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ IDNO: 340 or 341 and a LC of SEQ ID NO: 342. In an embodiment, the anti-apex bNAb or fragmentthereof, comprises a HC of SEQ ID NO: 351 or 352 and a LC of SEQ ID NO: 353. In an embodiment,the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 362 or 363 and a LC of SEQID NO: 364. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ IDNO: 373 or 374 and a LC of SEQ ID NO: 375. In an embodiment, the anti-apex bNAb or fragmentthereof, comprises a HC of SEQ ID NO: 384 or 385 and a LC of SEQ ID NO: 386. In an embodiment,the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 395 or 396 and a LC of SEQID NO: 397. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ IDNO: 406 or 407 and a LC of SEQ ID NO: 408. In an embodiment, the anti-apex bNAb or fragmentthereof, comprises a HC of SEQ ID NO: 417 or 418 and a LC of SEQ ID NO: 419.Linkers Examples of suitable linkers include amino acid sequences that are from 1 amino acid to 150 amino acids in length. In particular, from 1 to 140 amino acids, from 1 to 130 amino acids, from 1 to 120 amino acids, from 1 to 110 amino acids, from 1 to 100 amino acids, from 1 to 90 amino acids, from 1 to 80 amino acids, from 1 to 70 amino acids, from 1 to 60 amino acids, from 1 to 50 amino acids, from 1 to 40 amino acids, from 1 to 30 amino acids, from 1 to 20 amino acids, from 1 to 10 aminoacids, from 5 to 30 amino acids. In an embodiment, the linker is an amino acid sequence from 5 to30 amino acids in length. In an embodiment, the linker is an amino acid sequence as set forth in any one of SEQ IDNOs: 30 to 35. In an embodiment, the linker is an amino acid sequence as set forth in SEQ IDNO:30. In an embodiment, the linker is a multimer of the amino acid sequence as set forth in SEQID NO: 30. In an embodiment, the linker is [SEQ ID NO:30]n, wherein n is an integer from 1 to 6. Inan embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:31. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:32. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:33. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:34. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:35. Any of the aforementioned linkers may be incorporated into an antigen binding protein of the invention. In particular, any of the aforementioned linkers may be used to join a domain within the antigen binding protein to another domain within the antigen binding protein. In particular, any of the aforementioned linkers may be used to join a CD4 domain within the antigen binding proteinto a broadly neutralizing antibody or fragment thereof that binds to the V1 / V2 apex of the gp120protein or the gp120-gp41 interface of a gp120 and gp41 protein of HIV. Further, any of the aforementioned linkers may be used to join a CD4 domain as disclosed herein to a bNAb as disclosed herein. In an embodiment, the linker is an amino acid sequence as set forth in any one ofSEQ ID NOs: 30 to 35. In an embodiment, the linker is an amino acid sequence as set forth in SEQID NO: 30.In an embodiment, a linker is used to join the C-terminus of a CD4 domain to the N- terminus of a bNAb heavy chain variable domain. In an embodiment, a linker is used to join the C- terminus of a CD4 domain to the N-terminus of a bNAb light chain variable domain. In an embodiment, a linker is used to join the C-terminus of a CD4 domain to the N-terminus of a bNAb heavy chain variable domain and a linker is used to join the C-terminus of a CD4 domain to the N- terminus of a bNAb light chain variable domain. In an embodiment, a linker is used to join the C- terminus of a CD4 domain to the N-terminus of a bNAb heavy chain variable domain and an identical linker is used to join the C-terminus of a CD4 domain to the N-terminus of a bNAb light chain variable domain. In an embodiment, the linker is an amino acid sequence as set forth in any one ofSEQ ID NOs: 30 to 35. In an embodiment, the linker is an amino acid sequence as set forth in SEQID NO: 30.In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C- terminus of a bNAb heavy chain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of a bNAb heavy chain variable domain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of a bNAb light chain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of a bNAb light chain variable domain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of an Fc domain. In an embodiment, the linker is an amino acid sequenceas set forth in any one of SEQ ID NOs: 30 to 35. In an embodiment, the linker is an amino acidsequence as set forth in SEQ ID NO: 30.Any of the aforementioned linkers may be used to join a VH and VL pair as disclosed herein to form a scFv. In an embodiment, the linker between the VH domain and the VL domain of the scFvis selected from one of SEQ ID NOs: 30-35. In a particular embodiment, the linker between the VHdomain and the VL domain of the scFv is SEQ ID NO: 33.Any of the aforementioned linkers may be used to join a scFv as disclosed herein to an Fc domain. In an embodiment, the scFv is fused to a human Fc via a linker selected from one of SEQID NO: 30-35. In an embodiment, the scFv is fused to a human Fc via a linker of SEQ ID NO: 31.Bispecific proteins In an embodiment, the multimeric binding protein of the invention is a bispecific bindingprotein. Examples of such bispecific binding protein are embodiments are disclosed in the belowTable 5.

[0002] Table 5: Discloses bispecific proteins under the scope of the invention with reference to thesequences provided in Tables 3 and 4. For example, the cell containing an “X” in the table includes abispecific binding protein of the invention comprising a CD4 domain having a sequence of SEQ IDNO: 11 and a bNAb or fragment thereof comprising a VH domain having at least 95% sequenceidentity to SEQ ID NO: 96 and a VL domain having at least 95% sequence identity of SEQ ID NO: 97 (first row of Table 4) and CDRs according to SEQ ID NOs: 90-95 (first row of Table 3). CD4 domain comprises… (e.g. joined by a linker at the N-terminus of the heavy or light chain of the bnAb) Broad to narrow >>>>>Comprises a sequence according to SEQ ID NO: 31 4 5-21 5-15 11HC / LC according to any of pair disclosed in a row of Table 4 HC / LC having 95% sequence identity to any of pair of HC / LC disclosed in a row of Table 4 with > > > CDRs according to the equivalent row in Table wo 3 rra n HC / LC having 95% sequence identity to any of otd pair of HC / LC disclosed in a row of Table 4 a orb VH / VL according to any of pair disclosed in a row of Table 4 …se VH / VL having 95% sequence identity to any of sirp pair of VH / VL disclosed in a row of Table 4 with m X o c CDRs according to the equivalent row in Table b A 3 N b VH / VL having 95% sequence identity to any of pair of VH / VL disclosed in a row of Table 4 CDRs according to any of pair disclosed in arow of Table 3 In an embodiment, the bispecific binding protein comprises a CD4 domain and a broadly neutralizing antibody or fragment thereof comprising a pair of variable domains (a VH and a VL) as set out in any row of Table 4. In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of any one of SEQ ID NOs: 1-21 and a broadly neutralizing antibody or fragment thereofcomprising a pair of variable domains (a VH and a VL) as set out in any row of Table 4. In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and a broadly neutralizing antibody or fragment thereof comprising apair of variable domains (a VH and a VL) as set out in any row of Table 4. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 107 and a VL domain of SEQ ID NO: 108. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 118 and a VL domain of SEQ ID NO: 119. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 129 and a VL domain of SEQ ID NO: 130. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 140 and a VL domain of SEQ ID NO: 141. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 151 and a VL domain of SEQ ID NO: 152. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 162 and a VL domain of SEQ ID NO: 163. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 173 and a VL domain of SEQ ID NO: 174. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 184 and a VL domain of SEQ ID NO: 185. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 195 and a VL domain of SEQ ID NO: 196. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domainof SEQ ID NO: 206 and a VL domain of SEQ ID NO: 207.In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domainof SEQ ID NO: 217 and a VL domain of SEQ ID NO: 218.In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domainof SEQ ID NO: 228 and a VL domain of SEQ ID NO: 229.In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domainof SEQ ID NO: 239 and a VL domain of SEQ ID NO: 240.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 250 and a VL domain of SEQ ID NO: 251.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 261 and a VL domain of SEQ ID NO: 262.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 272 and a VL domain of SEQ ID NO: 273.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 283 and a VL domain of SEQ ID NO: 284.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 294 and a VL domain of SEQ ID NO: 295. In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 305 and a VL domain of SEQ ID NO: 306.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 316 and a VL domain of SEQ ID NO: 317.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 327 and a VL domain of SEQ ID NO: 328.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 338 and a VL domain of SEQ ID NO: 339.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 349 and a VL domain of SEQ ID NO: 350.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 360 and a VL domain of SEQ ID NO: 361. In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 371 and a VL domain of SEQ ID NO: 372.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 382 and a VL domain of SEQ ID NO: 383.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 393 and a VL domain of SEQ ID NO: 394.In an embodiment, the bispecific binding protein comprises a CD4 domain having asequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain ofSEQ ID NO: 404 and a VL domain of SEQ ID NO: 405. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof, comprises a VH domain ofSEQ ID NO: 415 and a VL domain of SEQ ID NO: 416. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO:60. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 60 and a sequence according to SEQ ID NO: 100.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 61. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 61 and a sequence according to SEQ ID NO: 111.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 62. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 62 and a sequence according to SEQ ID NO: 122. In an embodiment,the bispecific binding protein comprises a sequence according to SEQ IDNO: 63. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 63 and a sequence according to SEQ ID NO: 133. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 64. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 64 and a sequence according to SEQ ID NO: 144. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 65. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 65 and a sequence according to SEQ ID NO: 155. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 66. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 66 and a sequence according to SEQ ID NO: 166. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 67. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 67 and a sequence according to SEQ ID NO: 177. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 68. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 68 and a sequence according to SEQ ID NO: 188. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 69. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 69 and a sequence according to SEQ ID NO: 199. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 70. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 70 and a sequence according to SEQ ID NO: 210. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 71. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 71 and a sequence according to SEQ ID NO: 221. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 72. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 72 and a sequence according to SEQ ID NO: 232.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 73. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 73 and a sequence according to SEQ ID NO: 243.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 74. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 74 and a sequence according to SEQ ID NO: 254.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 75. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 75 and a sequence according to SEQ ID NO: 265.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 76. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 76 and a sequence according to SEQ ID NO: 276.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 77. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 77 and a sequence according to SEQ ID NO: 287.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 78. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 78 and a sequence according to SEQ ID NO: 298.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 79. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 79 and a sequence according to SEQ ID NO: 309.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 80. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 80 and a sequence according to SEQ ID NO: 320.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 81. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 81 and a sequence according to SEQ ID NO: 331. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 82. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 82 and a sequence according to SEQ ID NO: 342.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 83. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 83 and a sequence according to SEQ ID NO: 353.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 84. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 84 and a sequence according to SEQ ID NO: 364.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 85. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 85 and a sequence according to SEQ ID NO: 375.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 86. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 86 and a sequence according to SEQ ID NO: 386.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 87. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 87 and a sequence according to SEQ ID NO: 397.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 88. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 88 and a sequence according to SEQ ID NO: 408.In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 89. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO: 89 and a sequence according to SEQ ID NO: 419.Exemplary bispecific binding proteins Interface-bNAb17 e.g. supported by data in Figure 20 In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) atleast one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to theN-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizingantibody. In an embodiment, the bispecific binding protein comprises a broadly neutralizing antibodywhich has a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3 as set out in row 1 of Table 3(interface-bNAb17). In an embodiment, the bispecific binding protein comprises a broadlyneutralizing antibody or fragment thereof which has a VH and VL as set out in row 1 of Table 4 (interface-bNAb17). In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to SEQ ID NO: 90- 95 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to theN-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizingantibody. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain having at least 95% sequence identity to SEQ ID NO: 96 and a VLdomain having at least 95% sequence identity to SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which bindsto gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of one ofthe heavy chains or light chains of the broadly neutralizing antibody. Optionally wherein theantibody comprises six CDRs according SEQ ID NO: 90-95.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus orC-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4domain comprises a sequence according to SEQ ID NO: 1-21. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4domain comprises a sequence according to SEQ ID NO: 5-21. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4domain comprises a sequence according to SEQ ID NO: 5-15. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4domain comprises a sequence according to SEQ ID NO: 11. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus ofone of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 andwhich binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least oneCD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 andwhich binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least oneCD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-15 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 andwhich binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 99 and a light chain of SEQ ID NO: 100 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO:60. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO:60 and a sequence according to SEQ ID NO: 100. Apex-bNAb1 e.g. supported by data in Figure 4 In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of one of heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises a broadly neutralizing antibodywhich has a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3 as set out in row 15 of Table 3(apex-bNAb1). In an embodiment, the bispecific binding protein comprises a broadly neutralizingantibody or fragment thereof which has a VH and VL as set out in row 15 of Table 4 (apex-bNAb1). In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to SEQ ID NO: 244-249 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus orC-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain having at least 95% sequence identity to SEQ ID NO: 250 and a VL domain having at least 95% sequence identity to SEQ ID NO: 251 and which binds to the V1 / V2apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein theCD4 domain is attached by a linker to the N-terminus or C-terminus of one of the heavy chains orlight chains of the broadly neutralizing antibody. Optionally wherein the antibody comprises six CDRsaccording SEQ ID NO: 244-249. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 1-21. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 5-21. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 5-15. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 11. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises asequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises asequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain whichbinds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-15 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 253 and a light chain of SEQ ID NO: 254 and which binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO:74. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO:74 and a sequence according to SEQ ID NO: 254.Apex-bNAb2 – e.g. supported by data in Figure 5In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises a broadly neutralizing antibodythereof which has a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3 as set out in row 16 of Table 3 (apex-bNAb2). In an embodiment, the bispecific binding protein comprises a broadly neutralizing antibody or fragment thereof which has a VH and VL as set out in row 16 of Table 4 (apex-bNAb2). In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to SEQ ID NO: 255-260 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus orC-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain having at least 95% sequence identity to SEQ ID NO: 261 and a VL domain having at least 95% sequence identity to SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of one of the heavy chains orlight chains of the broadly neutralizing antibody. Optionally wherein the antibody comprises six CDRsaccording SEQ ID NO: 255-260. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus ofone of the heavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody.In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 1-21. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 5-21. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 5-15. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 11. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domaincomprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises asequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizingantibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of theheavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises asequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to the V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-15 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 264 and a light chain of SEQ ID NO: 265 andwhich binds to V1 / V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which bindsto gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO:75. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ IDNO:75 and a sequence according to SEQ ID NO: 265. Production methodsAntigen binding proteins may be prepared by any of a number of conventional techniques. Forexample, antigen binding proteins may be purified from cells that naturally express them (e.g., anantibody can be purified from a hybridoma that produces it), or produced in recombinant expression systems. Anumber of different expression systems and purification regimes can be used to generatethe antigen binding proteins of the invention. Generally, host cells are transformed with a recombinant expression vector encoding the desired antigen binding protein. The expression vector may be maintained by the host as a separate genetic element or integrated into the host chromosome depending on the expression system. A wide range of host cells can be employed,including Prokaryotes (including Gram-negative or Gram-positive bacteria, for example Escherichiacoli, Bacilli sp., Pseudomonas sp., Corynebacterium sp.), Eukaryotes including yeast (for example Saccharomyces cerevisiae, Pichia pastoris), fungi (for example Aspergilus sp.), or higher Eukaryotes including insect cells and cell lines of mammalian origin (for example, CHO, NS0, PER.C6, HEK293, HeLa). The host cell may be an isolated host cell. The host cell is usually not part of a multicellularorganism (e.g., plant or animal). The host cell may be a non-human host cell. The host cell may bea microorganism cell. Appropriate cloning and expression vectors for use with bacterial, fungal, yeast, and mammalian host cells are known in the art. The cells can be cultured under conditions that promote expression of the antigen binding protein using a variety of equipment such as shake flasks, spinner flasks, and bioreactors. The polypeptide(s) is(are) recovered by conventional protein purification procedures. Protein purification procedures typically consist of a series of unit operations comprised of various filtration and chromatographic processes developed to selectively concentrate and isolate the antigen binding protein. The purified antigen binding protein may be formulated in a pharmaceutically acceptable composition. Fc modifications Fc engineering methods can be applied to modify the functional or pharmacokinetics properties of an antigen binding protein, in particular an antibody. Effector function may be altered by making mutations in the Fc region that increase or decrease binding to C1q or Fcγ receptors and modify CDC or ADCC activity respectively. Modifications to the glycosylation pattern of an antibody can also be made to change the effector function. The interaction between the Fc region of an antigen binding protein or antibody and various Fc receptors (FcR), including FcγRI (CD64), FcγRII (CD32), FcγRIII (CD16), FcRn, C1q, and type II Fc receptors is believed to mediate the effector functions of the antigen binding protein or antibody. Significant biological effects can be a consequence of effector functionality. Usually, the ability to mediate effector function requires binding of the antigen binding protein or antibody to an antigen and not all antigen binding proteins or antibodies will mediate every effector function. Effector function can be assessed in a number of ways including, for example, evaluating ADCC effector function of antibody coated to target cells mediated by Natural Killer (NK) cells via FcγRIII, or monocytes / macrophages via FcγRI, or evaluating CDC effector function of antibody coated to target cells mediated by complement cascade via C1q. For example, an antigen binding protein of the present invention can be assessed for ADCC effector function in a Natural Killer cellassay. Examples of such assays can be found in Shields et al, 2001, The Journal of BiologicalChemistry, Vol. 276, p. 6591-6604; Chappel et al, 1993, The Journal of Biological Chemistry, Vol268, p. 25124-25131; Lazar et al, 2006, PNAS, 103; 4005-4010.Examples of assays to determine CDC function include those described in J Imm Meth, 1995, 184: 29-38. The effects of mutations on effector functions (e.g., FcRn binding, FcγRs and C1q binding,CDC, ADCML, ADCC, ADCP) can be assessed, e.g., as described in Grevys et al., J Immunol. 2015Jun 1; 194(11): 5497–5508, or Tam et al., Antibodies 2017, 6(3); Monnet et al., 2014 mAbs, 6:2,422-436. Throughout this specification, amino acid residues in Fc regions, in antibody sequences or full-length antigen binding protein sequences, are numbered according to the EU index numbering convention. The long half-life of IgG antibodies is reported to be dependent on their binding to FcRn. Therefore, substitutions that increase the binding affinity of IgG to FcRn at pH 6.0 while maintaining the pH dependence of the interaction with target, by engineering the constant region, have beenextensively studied (Ghetie et al., Nature Biotech. 15: 637-640, 1997; Hinton et al., JBC 279: 6213-6216’ 2004; Dall'Acqua et al., 10 J Immunol 117: 1129-1138, 2006). The in-vivo half-life of antigenbinding proteins of the present invention may be altered by modification of a heavy chain constant domain or an FcRn binding domain therein. In adult mammals, FcRn, plays a key role in maintaining serum antibody levels by acting as a protective receptor that binds and salvages antibodies of the IgG isotype from degradation. IgG molecules are endocytosed by endothelial cells and, if they bind to FcRn, are recycled out of the cells back into circulation. In contrast, IgG molecules that enter the cells and do not bind to FcRn and are targeted to the lysosomal pathway where they are degraded. FcRn is believed to be involved in both antibody clearance and the transcytosis acrosstissues (see Junghans R.P (1997) Immunol.Res 16. 29-57 and Ghetie et al (2000) Annu. Rev.Immunol. 18, 739-766). Human IgG1 residues determined to interact directly with human FcRn include Ile253, Ser254, Lys288, Thr307, Gln311, Asn434 and His435. Mutations at any of these positions may enable increased serum half-life and / or altered effector properties of antigen binding proteins of the invention. Antigen binding proteins of the present invention may have amino acid modifications that increase the affinity of the constant domain or fragment thereof for FcRn. Increasing the half-life(i.e., serum half-life) of therapeutic and diagnostic IgG antibodies and other bioactive molecules hasmany benefits including reducing the amount and / or frequency of dosing of these molecules. In one embodiment, an antigen binding protein of the invention comprises all or a portion (an FcRn binding portion) of an IgG constant domain having one or more of the following amino acid modifications. For example, with reference to IgG1, M252Y / S254T / T256E (commonly referred to as “YTE” mutations) and M428L / N434S (commonly referred to as “LS” mutations) increase FcRn binding atpH 6.0 (Wang et al. 2018). In an embodiment, an antigen binding protein of the inventioncomprises an Fc domain with the LS mutations. In an embodiment, an antigen binding protein of the invention comprises a bNAb in which the LS mutations are present in both of the heavy chain Fc domains. Half-life and FcRn binding can also be extended by introducing H433K and N434F mutations(commonly referred to as “HN” or “NHance” mutations) (with reference to IgG1) (WO2006 / 130834).Additionally, various publications describe methods for obtaining physiologically active molecules with modified half-lives, either by introducing an FcRn-binding polypeptide into the molecules (WO97 / 43316, US5869046, US5747035, WO96 / 32478 and WO91 / 14438) or by fusing the molecules with antibodies whose FcRn-binding affinities are preserved, but affinities for other Fc receptors have been greatly reduced (WO99 / 43713), or fusing with FcRn binding domains of antibodies (WO00 / 09560, US4703039). Post-translational modifications The skilled person will appreciate that, upon production of an antigen binding protein, such as a bispecific molecule of the invention in a host cell, post-translational modifications may occur. For example, this may include the cleavage of certain leader sequences, the addition of various sugar moieties in various glycosylation patterns, non-enzymatic glycation, deamidation, oxidation, disulfide bond scrambling and other cysteine variants such as free sulfhydryls, racemized disulfides, thioethers and trisulfide bonds, isomerisation, C-terminal lysine clipping, and N-terminal glutamine cyclisation. The present invention encompasses the use of antigen binding proteins that have been subjected to, or have undergone, one or more post-translational modifications. Thus an antigen binding protein of the invention includes an “antigen binding protein” as defined earlier that has undergone a post-translational modification such as described herein. Glycation is a post-translational non-enzymatic chemical reaction between a reducing sugar, such as glucose, and a free amine group in the protein, and is typically observed at the epsilon amine of lysine side chains or at the N-Terminus of the protein. Glycation can occur during production and storage only in the presence of reducing sugars. Deamidation can occur during production and storage, is an enzymatic reaction primarily converting asparagine (N) to iso-aspartic acid (iso-aspartate) and aspartic acid (aspartate) (D) at approximately 3:1 ratio. This deamidation reaction is therefore related to isomerization of aspartate (D) to iso-aspartate. The deamidation of asparagine and the isomerisation of aspartate, both involve the intermediate succinimide. To a much lesser degree, deamidation can occur with glutamine residues in a similar manner. Deamidation can occur in a CDR, in a Fab (non-CDR region), or in the Fc region. Oxidation can occur during production and storage (i.e., in the presence of oxidizingconditions) and results in a covalent modification of a protein, induced either directly by reactive oxygen species or indirectly by reaction with secondary by-products of oxidative stress. Oxidation happens primarily with methionine residues, but may occur at tryptophan and free cysteine residues. Oxidation can occur in a CDR, in a Fab (non-CDR) region, or in the Fc region. Disulfide bond scrambling can occur during production and basic storage conditions. Under certain circumstances, disulfide bonds can break or form incorrectly, resulting in unpaired cysteine residues (-SH). These free (unpaired) sulfhydryls (-SH) can promote shuffling. The formation of a thioether and racemization of a disulphide bond can occur under basic conditions, in production or storage, through a beta elimination of disulphide bridges back to cysteine residues via a dehydroalanine and persulfide intermediate. Subsequent crosslinking of dehydroalanine and cysteine results in the formation of a thioether bond or the free cysteineresidues can reform a disulphide bond with a mixture of D- and L-cysteine.Trisulfides result from insertion of a sulfur atom into a disulphide bond (Cys-S-S-S-Cys) and are formed due to the presence of hydrogen sulphide in production cell culture. N-terminal glutamine (Q) and glutamate (glutamic acid) (E) in the heavy chain and / or light chain is likely to form pyroglutamate (pGlu) via cyclization. Most pGlu formation happens in the production bioreactor, but it can be formed non-enzymatically, depending on pH and temperature of processing and storage conditions. Cyclization of N-terminal Q or E is commonly observed in natural human antibodies. C-terminal lysine clipping is an enzymatic reaction catalyzed by carboxypeptidases, and is commonly observed in recombinant and natural human antibodies. Variants of this process include removal of lysine from one or both heavy chains due to cellular enzymes from the recombinant host cell. Upon administration to the human subject / patient is likely to result in the removal of any remaining C-terminal lysines. Pharmaceutical compositions Antigen binding proteins as described herein may be incorporated into pharmaceutical compositions for use in the treatment or prevention of HIV infection. In one embodiment, the pharmaceutical composition comprises an antigen binding protein in combination with one or more pharmaceuticallyacceptable excipient.Such compositions comprise a pharmaceutically acceptable carrier as known and called for by acceptable pharmaceutical practice. Pharmaceutical compositions may be administered by injection or continuous infusion (examples include, but are not limited to, intravenous, intraperitoneal, intradermal, subcutaneous, intramuscular, intraocular, and intraportal). In one embodiment, the composition is suitable for intravenous administration. In one embodiment, the composition is suitable for subcutaneous administration. Pharmaceutical compositions may be suitable for topical administration (which includes, but is not limited to, epicutaneous, inhaled, intranasal or ocular administration) or enteral administration (which includes, but is not limited to, oral, vaginal, or rectal administration). The pharmaceutical composition may be included in a kit containing the antigen binding protein together with other medicaments, for example dolutegravir or cabotegravir, and / or withinstructions for use. For convenience, the kit may comprise the reagents in predetermined amountswith instructions for use. The kit may also include devices used for administration of the pharmaceutical composition. The terms “individual”, “subject” and “patient” are used herein interchangeably. In one embodiment the subject is a human. Treatment The antigen binding proteins described herein may be used in methods of treatment or prevention of HIV infection and AIDs. The antigen binding proteins described herein may be used in the manufacture of medicaments for the treatment or prevention of HIV infection and AIDs. The antigen binding proteins described may be used in an effective amount for therapeutic, prophylactic or preventative treatment. A therapeutically effective amount of the antigen binding protein described herein is an amount effective to ameliorate or reduce one or more symptoms of HIV infection. A prophylactically effective amount of the antigen binding protein described herein is an amount effective to prevent one or more symptoms of HIV infection. Combinations Antigen binding proteins of the present invention may be employed alone or in combination with other therapeutic agents, or a prodrug thereof. Combination therapies according to the present invention thus comprise the administration of an antigen binding protein and the administration of at least one other agent which may be useful in the treatment or prevention of HIV infection and / or AIDS. An antigen binding protein of the present invention and the other therapeutic agent may be formulated and administered together in a single pharmaceutical composition or may be formulated and administered separately. When formulated and administered separately, administration may occur simultaneously or sequentially in any order. Antigen binding proteins as described herein may be combined with, for example, one or more of an antiretroviral agent, an anti-infective agent, an immunomodulator, and other HIV entry inhibitors. Antiretroviral agents include Nucleoside Reverse Transcriptase Inhibitors (NRTIs), Non- Nucleoside Reverse Transcriptase Inhibitors (NNRTIs), Nucleoside Reverse TranscriptaseTranslocation Inhibitors (NRTTIs), Protease Inhibitors (PIs), Entry Inhibitors (EI), Integrase StrandTransfer Inhibitors (INSTI), Maturation Inhibitors (MIs), and Capsid Inhibitors (CIs).NRTIs may include, but are not limited to: abacavir, adefovir, adefovir dipivoxil, alovudine, amdoxovir, apricitabine, calanolide A, censavudine, didanosine, elvucitabine, emtricitabine, fozivudine, lamivudine, racivir, stampidine, stavudine, tenofovir disoproxil fumerate, tenofovir alafenamide, todoxil, zalcitabine, and zidovudine. NNRTIs may include, but are not limited to, HBY 097 (Hoechst / Bayer), capravirine,delaviridine, doravirine, efavirenz, etravirine, immunocal, lersivirine, loviride, nevirapine, oltipraz, andrilpivirine. NRTTIs include, but are not limited to, islatravir. PIs may include, but are not limited to, amprenavir, atazanavir, brecanavir, cobicistat,darunavir, fosamprenavir, indinavir, lasinavir, lopinavir, palinavir, nelfinavir, ritonavir, saquinavir, andtipranavir. EIs are discussed in DRUGS OF THE FUTURE 1999, 24(12), 1355-1362; CELL, Vol. 9, 243- 246, Oct. 29, 1999; and DRUG DISCOVERY TODAY, Vol. 5, No. 5, May 2000, pp. 183-194; andMeanwell et al., Current Opinion in Drug Discovery & Development (2003), 6(4), 451-461. Inparticular, the antigen binding proteins of the invention can be utilized in combination with attachment inhibitors, fusion inhibitors, and chemokine receptor antagonists aimed at either the CCR5 or CXCR4 coreceptor. HIV attachment inhibitors are also set forth in US 7,354,924 and uS7,745,625. EIs may include, but are not limited to, cenicriviroc, enfuvirtide, fostemsavir, ibalizumab,leronlimab, maraviroc, vicriviroc and VIR-576. INSTIs may include, but are not limited to, bictegravir, cabotegravir, dolutegravir, elvitegravir, and raltegravir, . In an embodiment, the INSTI is dolutegravir or cabotegravir. In an embodiment, the INSTI is cabotegravir. Maturation inhibitors may include, but are not limited to, bevirimat, BMS-955176, GSK3640254, GSK3739937, PA-344 and PA-457. It will be understood that GSK3640254 is a compound as described in Dicker I, Jeffrey JL, Protack T, et al., Antimicrob Agents Chemother. 2022;66(1). GSK3739937, also known as VH3739937, is the compound of clinical trial NCT04493684. Capsid inhibitors may include, but are not limited to, GSK4004280, GSK4011499, and lencapavir. Anti-infective agents include, but are not limited to, clindamycin with primaquine,daunorubicin, fluconazole, intraconazole, nystatin pastille, ornidyl eflornithine, megestrol acetate,pentamidine isethionate, piritrexim, trimethoprim, trimetrexate, recombinant human erythropoietin, recombinant human growth hormone, spiramycin, testosterone and total enteral nutrition, Immunomodulators include, but are not limited to, acemannan, alpha-2-interferon, AS-101, bropirimine, CL246,738, FP-21399, gamma interferon, granulocyte macrophage colony stimulating factor, HIV core particle immunostimulant, interleukin-2, immune globulin, IMREG-1, IMREG-2,imuthiol diethyl dithio carbamate, methionine enkephalin, MTP-PE muramyl tripeptide, remune,recombinant soluble human CD4, rCD4-IgG hybrids, SK&F106528, thymopentin, and tumour necrosis factor (TNF). The antigen binding proteins of the present invention may also be used in combination with agents that induce HIV expression, such as latency reversing agents. Several latency reversing agents include, but are not limited to, the following: histone deacetylase inhibitors (e.g66anobinostatt, panobinostat, romidepin), histone crotonyl transferase inhibitors (sodiumcorotonate), protein kinase C agonists (e.g., bryostatin, ingenol B), disulfiram, TLR7 agonists (e.g.,GS-9620), and bromodomain inhibitors (e.g., JQ1, iBET151).The antigen binding proteins of the present invention may also be used in combination with other agents that induce HIV expression, such as agents for clearance therapy. Several examples of agents for clearance therapy, or of immunological combinations for clearance, include, but are not limited to, the following: bNAbs, CD4-Ig, eCD4-Ig, and dual-affinity re-targeting (DART) proteins. Antigen binding proteins of the invention may be used in combination with broadlyneutralizing HIV-1 antibodies, including 1NC9, 1B2530, 2F5, 2G12, 3NBC60, 3BNC117, 4E10,8ANC131, 8ANC134, 10-1074, 10-1074LS, 10E8, 12A12, 12A21, b12, CAP206-CH12, CH01-04,CH103-106, elipovimab (formerly known as GS-9722), HJ16, M66.6, N6LS (also known as VRC- HIVMAB091-00-AB and the compound of clinical trial NCT03538626), NIH45–46, PG9, PG16, PGT121-123, PGT125-131, PCT135-137, PGT141-145, PGT121.414.LS, PGT1512G12, QA013.2, VRC01-03, VRC-PG04, VRC-PG04b, VRC-CH30–34. Other agents that may be combined with antigen binding proteins of the invention include BIT225, GSK4000422 / VH4000422, and S-648414 (the compound of clinical trial NCT04147715). The scope of combinations of compounds of this invention with HIV agents is not limited to those mentioned above, but includes in principle any combination with any pharmaceutical composition useful for the treatment and / or prevention of HIV infection and / or AIDS. Nucleic acid In some embodiments, a subject is administered DNA or RNA encoding an multimeric antigenbinding protein of the invention to provide in vivo antibody production, for example using the cellularmachinery of the subject. Administration of nucleic acid constructs is known in the art and taught. for example, in U.S. Patent No. 5,643,578, U.S. Patent. No. 5,593,972 and U.S. Patent No. 5,817,637. U.S. Patent. No. 5,880,103 describes several methods of delivery of nucleic acids encoding proteins to an organism. One approach to administration of nucleic acids is direct administration with plasmid DNA. such as with a mammalian expression plasmid. The nucleotide sequence encoding the disclosed antigenbinding protein can be placed under the control of a promoter to increase expression. The methodsinclude liposomal delivery of the nucleic acids. Such methods can be applied to the production of anantigen binding protein of the invention. In some embodiments, a multimeric antigen binding protein ofthe invention is expressed in a subject using the pVRC8400 vector (described in Barouch er u / ., J.Virol., 79(14), 8828-8834, 2005). In some embodiments, a subject (such as a human subject at risk of HIV infection) can beadministered an effective amount of an adeno-associated virus (AAV) viral vector that includes one ormore nucleic acid molecules encoding an multimeric antigen binding protein of the invention. The AAVviral vector is designed for expression of the nucleic acid molecules encoding a disclosed antigenbinding protein, and administration of an effective amount of the AAV viral vector to the subject leadsto expression of an effective amount of the antigen binding protein in the subject. Non-limitingexamples of AAV viral vectors that can be used to express a disclosed antigen binding protein in asubject include those provided in Johnson et al., Nut. Med., 15(8):901-906, 2009 and Gardner et al.,Nature, 519(7541):87-91, 2015. The invention is illustrated by the following clauses: 1. A multimeric anti-HIV envelope spike complex-binding protein comprising:i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at leastone heavy chain or light chain, wherein the antibody binds to the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein; andii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.2. The binding protein of clause 1, wherein the broadly neutralizing antibody binds to theV1 / V2 loop of a gp120 protein.3. The binding protein of clause 1, wherein the broadly neutralizing antibody binds to thegp120-gp41 interface of a gp120 protein and a gp41 protein.4. The binding protein of clause 1, wherein the broadly neutralizing antibody binds to at leastone complex N-glycan at the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein.5. A multimeric anti-HIV envelope spike complex-binding protein comprising:i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at leastone heavy chain or light chain, wherein the antibody or fragment binds to at least one complex N-glycan on a gp120 or gp41 protein; andii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.6. The binding protein of clause 5, wherein the broadly neutralizing antibody binds to at leastone complex N-glycan at the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 protein and a gp41 protein.7. The binding protein of any preceding clause, wherein the CD4 domain is attached via alinker to the N-terminus or C-terminus of at least one heavy or light chain of the broadly neutralizing antibody.8. The binding protein of any preceding clause, wherein the CD4 domain is attached via alinker to the N-terminus at least one heavy chain or light chain of the broadly neutralizing antibody.The binding protein of any preceding clause, wherein the CD4 domain is attached via alinker to the N-terminus at least one heavy chain of the broadly neutralizing antibody.The binding protein of any preceding clause, wherein the binding protein comprises at leastfour CD4 domains.The binding protein of clause 10, wherein the broadly neutralizing antibody has two heavychains and two light chains; and the C-terminus of a first CD4 domain is attached by a linker to the N-terminus of a first heavy chain, a second CD4 domain is attached by a linker to the N-terminus of a second heavy chain, a third CD4 domain is attached by a linker to the N- terminus of a first light chain, an a fourth CD4 domain is attached by a linker to the N- terminus of a second light chain.A multimeric anti-HIV envelope spike complex-binding protein comprising:i. A broadly neutralizing anti-HIV envelope spike complex antibody or an antigen-binding Fab’ or F(ab’)2 fragment thereof comprising at least one heavy chain variableregion or light chain variable region, wherein siad antibody fragment binds to the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein; and ii. at least one CD4 domain, wherein the C-terminus of the CD4 domain is attacheddirectly or by a linker to the N-terminus of the heavy chain variable region or light chain variable region.The binding protein of clause 12, wherein the fragment is an antigen-binding Fab’ fragment,and wherein the CD4 domain is attached via a linker to the heavy chain variable region of the Fab’ fragment.The binding protein of clause 12, wherein the fragment is an antigen-binding Fab’ fragment,and wherein the CD4 domain is attached via a linker to the light chain variable region of the Fab’ fragment.The binding protein of clause 12, comprising at least two CD4 domains, wherein thefragment is an antigen-binding Fab’ fragment, wherein the first CD4 domain is attached via alinker to the heavy chain variable region of the Fab’ fragment and the second CD4 domain isattached via a linker to the light chain variable region of the Fab’ fragment.16. The binding protein of clause 12, comprising at least two CD4 domains, wherein thefragment is an antigen-binding F(ab’)2 fragment, and wherein each of the CD4 domains isattached via a linker to each of the heavy chain variable regions of the F(ab’)2 fragment.17. The binding protein of clause 12, comprising at least two CD4 domains, wherein thefragment is an antigen-binding F(ab’)2 fragment, and wherein each of the CD4 domains isattached via a linker to each of the light chain variable regions of the F(ab’)2 fragment.18. The binding protein of clause 12, comprising at least four CD4 domains, wherein thefragment is an antigen-binding F(ab’)2 fragment, and wherein each of the CD4 domains isattached via a linker to each of the heavy chain variable regions and each of the light chain variable regions of the F(ab’)2 fragment.19. The binding protein of clauses 12 to 18, wherein the C-terminus of the CD4 domains areeach attached via a linker to the N-terminus of the heavy chain variable region or light chain variable region of the Fab or F(ab’)2 fragment.20. A multimeric anti-HIV envelope spike complex-binding protein comprising:i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at leastone heavy chain or light chain, wherein the antibody comprises a VH domain and VLdomain pair according to SEQ ID NOs: 96 and 97, 250 and 251, or 261 and 262; andii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.21. The binding protein of any preceding clause, wherein the binding protein is a bispecificbinding protein.22. The binding protein of any preceding clause, wherein the linker is a peptide linker.23. The binding protein of any preceding clause, wherein the peptide linker is between 5 and 30amino acids in length.24. The binding protein of any preceding clause, wherein the linker is a multimer of the aminoacid sequence as set forth in SEQ ID NO: 30.25. The binding protein of any preceding clause, wherein the linker is selected from one of SEQID NOs: 30 to 35.26. The binding protein of any preceding clause, wherein the CD4 domain is a human CD4 D1domain or CD4 D1D2 domain.27. The binding protein of any preceding clause, wherein the CD4 domain comprises at least onestabilizing mutation compared to a wild type CD4 domain.28. The binding protein of any preceding clause, wherein the CD4 domain comprises at least onemutation selected from: L5Y, S23N, A55V, I79P, L96V and / or F98V.29. The binding protein of any preceding clause, wherein the CD4 domain comprises L5Y, S23N,A55V, I79P, L96V and F98V mutations; and at least one further mutation selected from:E91Q, E91H, E87G, N52W, K8V, K8I, K8C, G99C, T11C, K72C, E13C, I70C, H27C, G38C, K21C, G65C, Q25E, H27D, R58V, R58N, R58Y, and / or L61M.30. The binding protein of any preceding clause, wherein the CD4 domain comprises or consistsof any one of SEQ ID NO: 4 – 21.31. The binding protein of any preceding clause, wherein the CD4 domain comprises or consistsof any one of SEQ ID NO: 5 – 21.32. The binding protein of any preceding clause, wherein the CD4 domain comprises or consistsof any one of SEQ ID NO: 5 – 15.33. The binding protein of any preceding clause, wherein the CD4 domain comprises or consistsof SEQ ID NO: 11.34. The binding protein of any preceding clause, wherein the CD4 domain has a Tm above about70℃.35. The binding protein of any preceding clause, wherein the CD4 domain has a Tm betweenabout 70℃ and 95℃.36. The binding protein of any preceding clause, wherein the CD4 domain has a Tm of about90℃.37. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a mutation that increases the half-life of the binding protein compared to the same binding protein without said mutation.38. The binding protein of clause 37, wherein the binding protein comprises an Fc domain andthe half-life increasing mutation is a mutation in said Fc domain.39. The binding protein of clause 38, wherein the Fc domain comprises at least one of thefollowing sets of mutations (EU numbering): M428L and N434S (LS); L309D, Q311H and N434S (DHS); M252Y, S254T and T256E (YTE); and H433K and N434F (HN).40. The binding protein of clause 38, wherein the Fc domain comprises M428L and N434S (LS)mutations (EU numbering).41. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 as set out in any one row of Table 3.42. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to:i. SEQ ID NOs: 90 – 95, orii. SEQ ID NOs: 244 - 249, oriii. SEQ ID NOs: 255 - 260.43. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain variable domain and a light chain variable domain pair that is at least 95% identical to any of the variable domain pairs set out in any one row of Table 4.44. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain variable domain and a light chain variable domain pair that is atleast 95% identical to:i. SEQ ID NOs: 96 and 97, orii. SEQ ID NOs: 250 and 251, oriii. SEQ ID NOs: 261 and 261.45. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain variable domain and a light chain variable domain pair that is at least 95% identical to any of the variable domain pairs set out in any one row of Table 4, and a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to the equivalent row in Table 3.46. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises: i. a heavy chain variable domain and a light chain variable domain pair that is at least95% identical to SEQ ID NOs: 96 and 97 and a CDRH1, CDRH2, CDRH3, CDRL1,CDRL2, CDRL3 according to SEQ IS NOs: 90-95, orii. a heavy chain variable domain and a light chain variable domain pair that is at least95% identical to SEQ ID NOs: 250 and 251 and a CDRH1, CDRH2, CDRH3, CDRL1,CDRL2, CDRL3 according to SEQ IS NOs: 244-249, oriii. a heavy chain variable domain and a light chain variable domain pair that is at least95% identical to SEQ ID NOs: 261 and 261 and a CDRH1, CDRH2, CDRH3, CDRL1,CDRL2, CDRL3 according to SEQ IS NOs: 255-260.47. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain variable domain and a light chain variable domain pair according to any of the variable domain pairs set out in any one row of Table 4.48. The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain variable domain and a light chain variable domain pair accordingto: i. SEQ ID NOs: 96 and 97, orii. SEQ ID NOs: 250 and 251, oriii. SEQ ID NOs: 261 and 261.The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain and a light chain pair that is at least 95% identical to any of the chain pairs set out in any one row of Table 4.The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain and a light chain pair that is at least 95% identical to:i. SEQ ID NOs: 98 or 99, and 100, orii. SEQ ID NOs: 252 or 253, and 254, oriii. SEQ ID NOs: 263 or 264, and 265.The binding protein of any preceding clause, wherein the broadly neutralizing antibodycomprises a heavy chain and a light chain pair that is at least 95% identical to any of thechain pairs set out in any one row of Table 4, and a CDRH1, CDRH2, CDRH3, CDRL1,CDRL2, CDRL3 according to the equivalent row in Table 3.The binding protein of any preceding clause, wherein the broadly neutralizing antibody:i. a heavy chain and a light chain pair that is at least 95% identical to SEQ ID NOs: 98or 99, and 100 and; a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according toSEQ IS NOs: 90-95, or ii. a heavy chain and a light chain pair that is at least 95% identical to SEQ ID NOs:252 or 253, and 254; and a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3according to SEQ IS NOs: 244-249, or iii. a heavy chain and a light chain pair that is at least 95% identical to SEQ ID NOs:263 or 264, and 265; and a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3according to SEQ IS NOs: 255-260.The binding protein of any preceding clause, wherein the binding protein comprises orconsists of a sequence at least 95% identical to SEQ ID NO: 60 - 89.The binding protein of any preceding clause wherein binding protein comprises or consists ofa sequence according to SEQ ID NO: 60-89.55. The binding protein of any preceding clause, wherein the binding protein can reduce theIC50 of at least one HIV envelope in a PSV assay compared to the IC50 reduction caused bythe broadly neutralizing antibody and CD4 domain alone or in combination.56. The binding protein of any preceding clause, wherein the binding protein is linked to aneffector molecule or detectable marker, optionally wherein the detectable marker is a fluorescent, enzymatic or radioactive marker.57. A method of detecting an HIV infection in a human subject comprising contacting abiological sample from the human subject with the binding protein according to any one of clauses 1 to 56 under conditions sufficient to form an immune complex; and detecting thepresence of the immune complex in the sample, wherein the presence of the immune complex in the sample indicates that the subject has a HIV infection.58. A pharmaceutical composition comprising the binding protein as defined in any one of thepreceding clauses and a pharmaceutically acceptable excipient.59. A method of treating or preventing an HIV infection in a human comprising administering tothe human an anti-HIV binding protein according to any one of clauses 1 to 56, or a pharmaceutical composition according to clause 58.60. The method of clause 59, whereby viral load in the human is decreased.61. An anti-HIV binding protein according to any one of clauses 1 to 56, or a pharmaceuticalcomposition according to clause 58, for use in treating or preventing an HIV infection in a human.62. Use of an anti-HIV binding protein according to any one of clauses 1 to 56, or apharmaceutical composition according to clause 58, in the manufacture of a medicament for treating or preventing an HIV infection in a human.63. A kit comprising in separate containers: an anti-HIV binding protein according to any one ofclauses 1 to 56 and at least one anti-viral drug that inhibits cellular entry, replication, ortranscription of HIV in a human.64. The kit of clause 63, wherein the antiviral drug is selected from: Nucleoside ReverseTranscriptase Inhibitors (NRTIs), Non-Nucleoside Reverse Transcriptase Inhibitors (NNRTIs), Protease Inhibitors (PIs), Entry Inhibitors, Integrase Strand Transfer Inhibitors (INSTI),Maturation Inhibitors (MIs), Capsid Inhibitors (CIs) and / or Nucleoside Reverse TranscriptaseTranslocation Inhibitors (NRTTIs). 65. The kit of clause 64, wherein the antiviral drug is an INSTI.66. The kit of clause 65, wherein the INSTI is dolutegravir or cabotegravir.67. A nucleic acid sequence that encodes an anti-HIV binding protein according to any one ofclauses 1 to 56. 68. An expression vector that comprises the nucleic acid sequence of clause 67.69. A recombinant host cell that comprises the nucleic acid sequence of clause 67 or theexpression vector of clause 68. 70. A method of producing an anti-HIV binding protein, comprising culturing the host cell asdefined in clause 69 under conditions suitable for expression of said nucleic acid sequence orvector, whereby an anti-HIV binding protein is produced. 71. The anti-HIV binding protein produced by the method of clause 70.EXAMPLES Example 1 – Antigen Binding Protein ProductionPlasmids encoding the antigen binding proteins of the invention were expressed in EXPI293 or FREESTYLE 293-F cells using the manufacturer’s standard protocol (ThermoFisher Scientific, Waltham, MA). The expressed medium was harvested by centrifugation (4000 rpm for 10 min) and the antigen binding proteins were purified by filtration through a 0.22 µm filter (Millipore Sigma, Burlington, MA) and fast protein liquid chromatography (FPLC) (ÄKTATM Pure, Cytiva, Marlborough MA). The medium was then passed through a Mabselect SuRe column (Cytiva, Marlborough MA) to capture the antigen binding proteins and the column was washed sequentially with phosphate- buffered saline (PBS) before elution. The antigen binding proteins were then exchanged into a final buffer by using dialysis, a desalting column and preparative size exclusion column (SEC). The purity of the antigen binding proteins was evaluated by using sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS- PAGE) and on a size exclusion column on a high-performance liquid chromatography system (SEC- HPLC). Antigen binding protein concentrations were determined by measuring absorbance at 280nm wavelength (A280) on a NanoDrop machine (ThermoFisher Scientific, Waltham, MA), and theirmolecular mass was measured by using liquid –hromatography - mass spectrometry (LC-MS) toconfirm their identity. The endotoxin level in the final purified products was measured on an ENDOSAFE system (Charles River Labs, Wilmington MA) to make sure it was sufficiently low (usually < 1 EU (Endotoxin Unit) / mg of protein) for downstream anti-viral studies. Example 2 – Anti-Viral Activity Using Pseudotyped Virus AssayThe anti-viral activity of the antigen binding proteins was measured in a pseudotyped virus (PSV) assay. Pseudotyped HIV-1 virus (PSV) contains deletions in the genome that make it unable to produce infectious virions, but it can be used to measure the activity of cell entry inhibitors (i.e., molecules that prevent the binding of HIV-1 virions to the target cell membrane and / or prevent entry of HIV-1 into target cells), which include the antigen binding proteins of the invention. PSV was produced in HEK-293T cells (ATCC, Manassas VA) by co-transfecting expression plasmids encoding the HIV-1 gp160 envelope gene and an HIV-1 backbone plasmid using TRANSIT- 2020 transfection reagent (Mirus Bio, Madison WI). A panel of HIV-1 PSVs expressing different gp160 envelope trimers was generated to evaluate the effectiveness of the antigen binding proteins of the invention against a wide spectrum of HIV-1 strains. Meanwhile, to facilitate mechanistic studies of the antigen binding proteins, the complex N- glycans on selected HIV-1 envelopes were removed by adding Kifunensine during PSV production. Kifunensine inhibits mannosidase I, prevents processing of high mannose N-glycans into complex N- glycans in the cells and consequently produces high mannose glycoproteins. In brief, after 6 hours of transfection, Kifunensine was added to a final concentration of 100 µM, the cells were incubated for another 48 hours, and the supernatant which contains the PSV was harvested and aliquoted. i. ACTOne cellsThe genome of PSV used in this assay contains a luciferase gene that is expressed once the virus enters cells. Accordingly, the luminescence signal (after adding a substrate of luciferase) can be used to determine the level of viral infection. The 50% tissue culture infectious dose (TCID) of a single thawed aliquot of each batch of PSV was determined in ACTOne cells. The ACTOne cell-line used in this assay was derived in-house from a genetically engineered 293T cell clone that expresses CD4, CXCR4, and CCR5. Cells were maintained in growth medium composed of Dulbecco’s modified Eagle’s medium (DMEM, Life Technologies) at 37 ⁰C in a humidified 5% CO2–95% air environment. Cell monolayers were split by treatment with Trypsin-EDTA (0.05%). To run the anti-viral assay, ACTOne cells were detached by treating the cell culture flask with trypsin (trypsinization) and resuspended in growth medium containing 2% of DMSO to a density of 2.5 x 10⁵ cells / ml. One hundred µl of such cells was added to 10 µl of antigen binding protein pre-loaded in a 96-well plate. Ninety µl of PSV was then added to each well. The assay plates were incubated at 37°C in a humidified incubator at 5% CO₂ level. Plates were developed after 72 hours of incubation by adding 50 µl of BRIGHTGLO luciferase reagent (Promega, Madison WI) to each well, and transferring the plates to an ENVISION multilabel plate reader (PerkinElmer, Waltham MA) to measure the luminescence and determine the level of virus that had infected the cells. The higher the luminescence signal, the higher the level of infection. Raw data were analyzed using an in-house template in an IDBS system to calculate half- maximal inhibitory concentration (IC50) values which reflects the activity of the antigen binding proteins of the invention at inhibiting viral entry (the smaller the number is, the more active themolecule is). Maximal percent inhibition values were calculated as MPI = 100 – (mean signals at the2 highest concentrations of compound / mean signal of 2 no-drug control wells) × 100 (PMID: 34780263). ii. TMZ.bl cellsAlternatively, the PSV assay was carried out using a luciferase-based assay in a TZM.bl cell line. The TZM-bl cell line is derived from a HeLa cell clone that was engineered to express CD4, CCR5 and CXCR4 and to contain integrated reporter genes for firefly luciferase and E. coli β-galactosidase under the control of an HIV-1 long terminal repeat (Wei et al., Antimicrobial agents and chemotherapy 46:1896–905(2002)) permitting sensitive and accurate measurements of infection. The detailed materials and methodology have been described elsewhere (Mentefiori, Curr. Protoc. Immunol., 2005, Chapter 12; Seaman et al., Journal of Virology, Feb. 2010, 84(3), p. 1439- 1452). In brief, the assay measures the reduction in luciferase reporter gene expression in TZM.bl cells following a single round of virus infection. Five-fold serial dilutions of the antigen binding proteins of the invention, from 50 µg / ml to 3.2 ng / ml, were performed in duplicate in 10% DMEM growth medium (100 µ / well). An amount of 200 TCID50 (50% tissue culture infectious dose) of virus was added to each well in a volume of µl, and the plates were incubated for 1 h at 37°C. TZM.bl cells were then added (1x104 / well in a 100-µl volume) in 10% D-MEM growth medium containing DEAE-dextran (Sigma, St. Louis, MO) at a final concentration of 11 µg / ml. Assay controls included TZM.bl cells alone (cell control) and TZM.bl cells with virus (virus control). Following a 48-hour incubation at 37°C, 150 µl of assay medium was removed from each well and 100 µl of BRIGHTGLO luciferase reagent (Promega, Madison, WI) was added. The cells were allowed to lyse for 2 min, and then 150 µl of the cell lysate was transferred to a 96-well black solid plate, and luminescence was measured using a Victor 3 luminometer (Perkin Elmer). The 50% and 80% inhibitory concentration (IC50 and IC80) values were calculated as the serum dilution that caused a 50% and 80% reduction respectively, in relative luminescence units (RLU) compared to the level in the virus control wells after subtraction of cell control RLU. All data were analyzed with 5-parameter curve fitting using neutralizing antibody analysis software providedby the CAVD Vaccine Immunology Statistical Center. Maximal percent inhibition values werecalculated as MPI = 100 – (mean signals at the 2 highest concentrations of compound / mean signalof 2 no-drug control wells) × 100 (PMID: 34780263). Example 3 – Anti-Viral Activity Using Pseudotyped Virus AssayThe anti-viral activity of the antigen binding proteins was also measured in a replicating virus assay against NL4-3 strain and its variants in MT2 cells. The proviral clone of NL4-3 (obtained from NIH) was used to make the replicating reporter virus NLRepRluc, in which a section of the nef gene from the proviral clone of NL4˗3 was replaced with the Renilla luciferase gene (Techniques in HIV Research. Tech HIV Res. Published online 1990. doi:10.1007 / 978-1-349-11888-5). Virus was produced through transfection of HEK293T cells usingLipofectamine Plus (Invitrogen, Carlsbad CA), according to the manufacturer's instructions. Thereplication-competent virus was harvested 3 days after transfection of HEK 293T cells with the modified pNLRepRluc proviral clone and titrated in MT-2 cells using luciferase activity as a biomarker. The 10E8-insensitive strains are engineered based on this proviral clone NL4-3 by introducing point mutations into its envelope gene, including W680R / K683Q and W672L / F673L. MT-2 cells were obtained from the American Type Culture Collection (ATCC) and were propagated in RPMI 1640 medium supplemented with 10% heat-inactivated fetal bovine serum (FBS), 100 units / ml of penicillin G, 100 μg / ml of streptomycin, 10 mM HEPES buffer pH 7.55 and 2-mM L-glutamine. HEK293T cells were obtained from the ATCC and propagated in DMEM media supplemented with 10% heat-inactivated FBS. The NLRepRluc was used to infect MT-2 cells at a multiplicity of 0.01 for 1 hour before adding the proteins to the 96-well plates. The antigen binding proteins were serially diluted four-foldand 11 concentrations were plated in triplicate. After 4 days of incubation, cells were processed andquantitated for virus growth by the amount of expressed luciferase. Luciferase was quantitated using the ENDUREN substrate from Promega (Madison, WI) according to the manufacturer’s instructions. Luciferase activity was measured immediately on an ENVISION multilabel plate reader (PerkinElmer, Waltham MA). EC50 values were calculated by comparing the amount of luciferase produced in the presence of antigen binding protein compared to wells where no antigen binding protein (DMSO control) was added. A 5-parameter sigmoidal equation was used to fit the resulting signal vs. concentration curves, and the concentration of each antigen binding protein that produced 50% maximal inhibition(EC50) was determined. Maximal percent inhibition values were calculated as MPI = 100 – (meansignals at the 2 highest concentrations of compound / mean signal of 2 no-drug control wells) × 100 (PMID: 34780263). Those in the field will know that half maximal inhibitory concentration (IC50) is a measure ofthe potency of a substance in inhibiting a specific biological or biochemical function (in this case,viral replication). IC50 is a quantitative measure that indicates how much of a substance (e.g. drug)is needed to inhibit, in vitro, a given biological process or biological component by 50%. Similarly,IC80 or IC90 are the amount of the particular inhibitory substance needed to inhibit, in vitro, a givenbiological process or biological component by 80% or 90% respectively.Example 4 – Stability of soluble CD4 domainsAll soluble human CD4 domains tested contain a set of “base” mutations in human CD4 domain 1 (D1) over the wild-type sequence (SEQ ID NO:3) that enable the folding of human CD4 D1 on its own. Soluble CD4 D1 with this set of mutations is known as mD1.22 (Chen et al., J Virol. 2014 Jan;88(2):1125-39) and the mutations therein consist of: L5Y, S23N, A55V, I76P, L96V, and F98V (SEQ ID NO:4, also referred to as D1m herein). To achieve better developability and pharmacokinetics, further mutations were introduced into mD1.22 (SEQ ID NO:4) to enhance its thermal stability. The additional stabilizing mutations were designed based on several methodologies: 1) computational simulation by using Free Energy Perturbation (FEP+, Schrodinger, New York, NY USA); 2) computational simulation by using disulfide-bond scan in Molecular Operating Environment program (MOE, Chemical Computing Group, Montreal Canada); and 3) panning a library of human CD4 D1 with each residue mutated, one by one, to the other 19 types of amino acids (site saturation mutagenesis, TWIST BioScience, San Francisco, CA USA) using phage display under thermally challenging conditions (i.e., incubating the phage at room temperature, 70 °C, and 80 °C, then selecting the CD4 domain variants that can still bind to recombinant HIV-1 gp120 (CN54 strain, Acro Biosystems, Beijing China)). The best performing variants (SEQ ID NOs: 5-21) were fused with 6xHis tag at their C- termini, expressed and purified from mammalian cells using methods as described in Example 1, except that purification was via a Ni-NTA resin (Cytiva, Marlborough MA) instead of Mabselect SuRe column, with standard protocol from the vendor. These purified CD4 D1 variants (with C-terminal 6xHis tag) were then evaluated to determine their melting temperature (Tm, using Prometheus System, NanoTemper, München Germany), which indicates thermal stability, as well as their anti-viral activity against HIV-1 pseudotyped virus (see Example 2 above for methods using ACTOne cells). As shown in Table 6 below and in Figure 2, several CD4 D1 variants (SEQ ID NO:5-15)showed dramatically improved thermal stability over the “baseline” or “control” CD4 D1 (D1m, SEQ 5 ID NO:4), while maintaining similar anti-viral activity.Table 6 – Melting temperature of soluble CD4 domainsCD4 Domain SEQ ID NO: Tm (℃)D1m 4 68.2D1m-E91Q 6 72.4D1m-E91H 7 72.6D1m-E87G 8 71.9D1m-N52W 9 72D1m-K8V 5 77.1D1m-K8I 10 75.9D1m-K8C-G99C 11 88.8D1m-T11C-K72C 12 79.9D1m-E13C-I70C 13 78.8D1m-H27C-G38C 14 90.1D1m-K21C-G65C 15 80.1Example 5 – Antigen Binding Protein Format and Linker LengthThe fusion position of the CD4 domain in the broadly neutralizing mAbs (e.g., whether to fuse theCD4 domain to the light chain or heavy chain or both, whether to fuse the CD4 domain to the N- terminus or C-terminus of these chains, or whether to fuse the CD4 domain in the middle of the heavy chain (in between CH1 and CH2 domains)) was tested in some examples V3-bNAbs (another class of bNAbs that bind to a distinct target called the V3 loop). We observed that the most potent bispecific molecule resulted from fusing CD4 D1 to the N-terminus of the heavy chain of V3-bNAb1 (molecule 1 in Table 7, which neutralized 6 envelopes withIC50 < 160 pM and 1 envelope with IC50 about 3 nM in PSV assay). In this bispecific format, thelinker length between the CD4 domain and V3-bNAb1 heavy chain N-terminus does not particularlyaffect anti-viral activity (Figure 3A) but changes the pharmacokinetics (PK) of the resultant bispecificmolecules dramatically (Figure 3B). As shown in Figure 3B, the shorter-linker bispecific (D1m_1xG4S_bNAb1, SEQ ID NOs: 36and 23) showed much better PK (longer half-life and lower clearance rate) than the longer-linkerbispecific (D1m_4xG4S_bNAb1, SEQ ID NOs: 37 and 23)) in a humanized mouse model (Tg32strain where human neonatal Fc receptor (hFcRn) replaced the corresponding mouse gene (mFcRn), The Jackson Laboratory, Bar Harbor, Maine USA).

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This resulted in the production of bispecific moleculescomprising sequences according to SEQ ID NOs: 74-89 and associated light chains (see descriptionof Figures 4 to 19 above). These bispecifics were tested against a panel of HIV-1 envelopes in PSVassay, along with control molecules including CD4 domain 1 alone, bNAbs alone, and their mixtures (combo). Several such bispecifics showed much higher anti-viral activity than the control molecules, indicating strong anti-viral synergy between the CD4 domain and the fused bNAb. This is particularly surprising since the binding of these V1 / V2 apex bNAbs relies on a closed conformation of the gp160trimer (Gorman et al., Cell Rep. 2020 Apr 7;31(1):107488.) while CD4 induces the opening of thegp160 trimer / envelope spike complex (Dam et al., Nature. 2024 Feb;626(7998):E7.). Furthermore, ithas been shown that soluble CD4 abolishes the anti-viral activity of V1 / V2 apex bNAbs when mixed together (Ivan et al., PLoS Biol. 2019 Jan 16;17(1):e3000114.). In contrary, our experiments demonstrated that the covalent fusion of CD4 domain to one of a range of V1 / V2 apex bNAbs canboost their anti-viral potency and spectrum (Figures 4 to 19). Most strikingly, the resultingbispecifics potently neutralized the HIV-1 envelopes that are insensitive to the parental bNAb, CD4 domain or their mixture, indicating a strong functional synergy between the CD4 domain and the bNAb it is attached to (Table 10). Table 10: Anti-viral activity of bNAb1-derived bispecifics and control molecules against “double- insensitive” HIV-1 envelopes in PSV assay (ACTOne cells)Envelope Bispecific1-1 Bispecific1-2 bNAb1 CD4 Combo3637_V5_C3 IC50 1.2 3.8 >500 >500 >5003468_V1_C12nM0.16 4.4 >500 >500 >5003637_V5_C3 IC90 44.9 33 >500 >500 >5003468_V1_C12nM24.3 135 >500 >500 >5003637_V5_C3 MPI 99 100 18 32 433468_V1_C12(%)99 99 19 43 53Without being bound by theory, we believe this synergy might be a combined outcome from 1) the CD4 domain and the linked bNAb bind to a same gp160 envelope trimer; 2) CD4-induced conformational change of the HIV envelope spike protein complex, which exposes new epitopes for the bNAb, which overcomes the low susceptibility of insensitive envelopes; 3) the bNAb is sequestered at a high local concentration near the CD4 domain, providing advantage of binding kinetics, and 4) the combination of N-glycan binding coupled with CD4 domain anchoring to such N-glycans . Indeed, we observed in the case of CD4-bNAb1 and CD4-bNAb2 fusions, the synergy isparticularly obvious when the CD4 domain is attached to the N-terminus of the bNAb1 heavy or lightchain (“bispecific 1-1” comprising a heavy chain (including a linked CD4 domain) of SEQ ID NO: 74and a light chain of SEQ ID NO: 254 and “bispecific 1-2” comprising a heavy chain of SEQ ID NO:253 and a light chain (including a linked CD4 domain) of SEQ ID NO: 420; Figure 4), or the N- terminus of the bNAb2 heavy chain (“bispecific 2-1” comprising a heavy chain of SEQ ID NO: 75 (including a linked CD4 domain) and a light chain of SEQ ID NO: 265; Figure 5). Based on structural modeling, these N-terminal fusions can accommodate the co-binding of the CD4 domain and the linked bNAb to a same gp160 trimer / envelope spike complex. We also tested one such bispecific (Apex bispecific1, (also known as “bispecific 1-1” – SEQID NO: 74 (HC) and 254 (LC))) and its parental bNAb (Apex bNAb1 – SEQ ID NO: 253 (HC) and 254(LC)) against pseudotyped viruses treated with Kifunensine, which removes complex glycans on theenvelopes and shall reduce their susceptibility to Apex-bNAb1. The result demonstrated that theanti-viral synergy of the bispecific can be driven by the presence of complex glycans.As shown in Table 11, if an envelope is sensitive to Apex-bNAb1, treatment with Kifunensine greatly decreases its susceptibility to Apex-bNAb1 as well as the bispecific. If an envelope is resistant to Apex-bNAb1 (IC50 >500 nM) and shows synergy against the bispecific (lower IC50 against the bispecific than against CD4 and combo of CD4 with bNAb17), Kifunensine treatment destroys the synergy and gives an IC50 similar to that of the CD4 (treatment with Kifunensine can also alter the susceptibility to CD4 probably through changing the glycosylation pattern near theCD4 binding site (Liang et al., J Virol. 2016 Sep 29;90(20):9224-36.)). This proves that binding tocomplex glycans is important for the synergy observed within the bispecific.Table 11: Anti-viral activity of Apex- bNAb1-derived bispecific and control molecules againstKifunensine-treated HIV-1 envelopes in PSV assay (ACTOne cells)EnvelopeUntreated Kifunensine treatedIC50 nM IC90 nM IC50 nM IC90 nMBispecific1 0.008 0.1 0.1 2.13326V4C3Apex-bNAb1 <0.002 0.0 0.02 1.1CD4 1000.3 5333.9 977.6 4872.7Combo 0.0 0.1 0.0 1.1Bispecific1 12.6 149.5 214.3 >500Apex-bNAb1 >500 >500 >500 >5003637-V5-C3CD4 521.7 2245.6 940.5 5374.0Combo >500 >500 >500 >500Example 7 – Bispecifics based on interface bindersTo generate “CD4-interface” bispecifics, CD4 domain 1 was fused to broadly neutralizing antibodies(bNAbs) that target the gp41-gp120 interface region of the HIV-1 envelope proteins gp120 andgp41 (part of the gp160 trimer / envelope spike complex). This resulted in the production of bispecificmolecules comprising sequences according to SEQ ID NOs: 60-73 and associated light chains (seedescription of Figures 20 to 33 above). These bispecifics were tested against a panel of HIV-1envelopes in PSV assay, along with control molecules including CD4 domain 1 alone, bNAbs alone, and their mixtures (combo). Several such bispecifics showed much higher anti-viral activity than the control molecules, indicating strong anti-viral synergy between the CD4 domain and the fusedbNAbs (Figures 20 to 33).These “synergistic” bispecifics contain a lineage of bNAbs that binds to complex tri- andtetra-antennary glycans in a conserved epitope on gp41 and distinguish cleaved from uncleaved envelope trimers (Falkowska et al., Immunity. 2014 May 15;40(5):657-68.). Therefore, we alsotested one such bispecific (bispecific17 – comprising a heavy chain (including a linked CD4 domain)according to SEQ ID NO: 60 and a light chain according to SEQ ID NO: 100) and its parental bNAb(bNAb17, comrpising CDRs: 90-95, VH / VL: SEQ ID NOs: 97 and 97, HC / LC: 99 and 100) againstpseudotyped viruses treated with Kifunensine, which removes complex glycans on the envelopes and shall reduce their susceptibility to bNAb17. The result demonstrated that the anti-viral synergy of the bispecific relies on the presence of complex glycans. As shown in Table 12, if an envelope is sensitive to bNAb17, treatment with Kifunensine greatly decreases its susceptibility to bNAb17 as well as the bispecific. If an envelope is resistant to bNAb17 (IC50 >500 nM) and shows synergy against the bispecific (lower IC50 against the bispecific than against CD4 and combo of CD4 with bNAb17), Kifunensine treatment destroys the synergy and gives an IC50 similar to that of the CD4 (treatment with Kifunensine can also alter the susceptibilityto CD4 probably through changing the glycosylation pattern near the CD4 binding site (Liang et al.,J Virol. 2016 Sep 29;90(20):9224-36.)). This proves that binding to complex glycans is necessary forthe synergy observed within the bispecific. Without being bound by theory, we believe this synergy might be a combined outcome from 1) the CD4 domain and the linked bNAb bind to a same gp160 envelope trimer; 2) CD4-induced conformational change of the HIV envelope spike protein complex, which exposes new epitopes for the bNAb, which overcomes the low susceptibility of insensitive envelopes; 3) the bNAb is sequestered at a high local concentration near the CD4 domain, providing advantage of binding kinetics, and 4) the combination of N-glycan binding coupled with CD4 domain anchoring to such N- glycansTable 12: Anti-viral activity of bNAb17-derived bispecific and control molecules against Kifunensine-treated HIV-1 envelopes in PSV assay (ACTOne cells) Untreated Kifunensine treatedEnvelopeIC50 nM IC90 nM IC50 nM IC90 nMBispecific17 0.04 0.5 6.3 268.1bNAb17 0.03 0.6 82.2 >500MP11.38CD4 19.5 377.2 8.5 428.3Combo 0.02 0.3 3 459.4Bispecific17 0.03 0.6 5.8 >500398F1bNAb17 0.1 1.4 >500 >500CD4 6.2 >500 29.2 >500Combo 0 0.5 17 >500Bispecific17 2.5 70.3 8.5 194.2bNAb17 25.5 >500 >500 >50093UG065CD4 82.3 >500 6.2 >428Combo 5.6 >500 29.7 >500Bispecific17 0.5 34.8 187.8 >5000260.v5.c36bNAb17 >500 >500 >500 >500CD4 328.8 >500 332.5 >500Combo 28.5 >500 404.8 >500Bispecific17 0.7 45.2 195.1 >500MP35.2bNAb17 >500 >500 >500 >500CD4 50.1 276 423 >500Combo 93.7 >500 439 >500Bispecific17 1.6 19.2 85.1 >500TRO11bNAb17 >500 >500 >500 >500CD4 196.1 >500 98.6 >500Combo >500 >500 56.9 >500Bispecific17 1.7 313.6 29.1 >500bNAb17 >500 >500 >500 >500CNE8CD4 65.7 >500 90.1 >500Combo >500 >500 104.1 >500SEQUENCE LISTING SEQName / Identifier DescriptionID NO 1D1D2 Human CD4 D1D2 (wild type)2 D1mD2 Human CD4 mD1.22-D2 (D1 mutations S23N, A55V, andL96V) 3D1 Human CD4 D1 (wild type)4 D1m Human CD4 mD1.22 (NCBI accession code:QHY83614.1; D1 mutations L5Y, S23N, A55V, I76P, L96V and F98V) 5D1m-K8V Human CD4 mD1.22 + K8V6 D1m-E91Q Human CD4 mD1.22 + E91Q7 D1m-E91H Human CD4 mD1.22 + E91H8 D1m-E87G Human CD4 mD1.22 + E87G9 D1m-N52W Human CD4 mD1.22 + N52W10 D1m-K8I Human CD4 mD1.22 + K8I11 D1m-K8C-G99C Human CD4 mD1.22 + K8C, G99C12 D1m-T11C-K72C Human CD4 mD1.22 + T11C, K72C13 D1m-E13C-I70C Human CD4 mD1.22 + E13C, I70C14 D1m-H27C-G38C Human CD4 mD1.22 + H27C, G38C15 D1m-K21C-G65C Human CD4 mD1.22 + K21C, G65C16 D1m-Q25E Human CD4 mD1.22 + Q25E17 D1m-H27D Human CD4 mD1.22 + H27D18 D1m-R58V Human CD4 mD1.22 + R58V19 D1m-R58N Human CD4 mD1.22 + R58N20 D1m-R58T Human CD4 mD1.22 + R58T21 D1m-L61M Human CD4 mD1.22 + L61M22 V3-bNAb1 HC+LS Full heavy chain of model V3-bNAb1 with M428L / N434Smutations 23 V3-bNAb1 LC Full light chain of model V3-bNAb124 V3-bNAb2 HC+LS Full heavy chain of model V3-bNAb2 with M428L / N434Smutations 25 V3-bNAb2 LC Full light chain of model V3-bNAb226 V3-bNAb3 HC+LS Full heavy chain of model V3-bNAb3 with M428L / N434Smutations 27 V3-bNAb3 LC Full light chain of model V3-bNAb3V3-bNAb4 HC+LS Full heavy chain of model V3-bNAb4 with M428L / N434SmutationsV3-bNAb4 LC Full light chain of model V3-bNAb41xG4S Linker2xG4S Linker3xG4S Linker4xG4S Linker5xG4S Linker6xG4S LinkerD1m_1xG4S_bNAb1-HC Human CD4 mD1.22 fused to the N-terminus of modelV3-bNAb1 heavy chain with 1xG4S linker, Fc includesM428L / N434SD1m_4xG4S_bNAb1-HC Human CD4 mD1.22 fused to the N-terminus of modelV3-bNAb1 heavy chain with 4xG4S linker, Fc includesM428L / N434SD1m_1xG4S_bNAb1-LC Human CD4 mD1.22 fused to the N-terminus of modelV3-bNAb1 light chain with 1xG4S linkerbNAb1-HC-mid_1xG4S_D1m-Human CD4 mD1.22 + K8C + G99C fused in between K8C-G99Cthe CH1 domain and hinge of model V3-bNAb1 heavychain with 1xG4S linker, Fc includes M428L / N434SbNAb1-HC_1xG4S_ D1m-K8C-Human CD4 mD1.22 + K8C + G99C fused to the C- G99Cterminus of model V3-bNAb1 heavy chain with 1xG4Slinker, Fc includes M428L / N434SbNAb1-LC_1xG4S_D1m-K8C-Human CD4 mD1.22 + K8C + G99C fused to the C- G99Cterminus of model V3-bNAb1 light chain with 1xG4SlinkerD1m-K8I_1xG4S_bNAb1-HC Human CD4 mD1.22 + K8I fused to the N-terminus ofmodel V3-bNAb1 heavy chain with 1xG4S linker, Fcincludes M428L / N434SD1m-K8V_1xG4S_bNAb1-HC Human CD4 mD1.22 + K8V fused to the N-terminus ofmodel V3-bNAb1 heavy chain with 1xG4S linker, Fcincludes M428L / N434SD1m-K8C-G99C_1xG4S_bNAb1-Human CD4 mD1.22 + K8C + G99C fused to the N- HCterminus of model V3-bNAb1 heavy chain with 1xG4Slinker, Fc includes M428L / N434SD1m-T11C-Human CD4 mD1.22 + T11C + K72C fused to the N- K72C_1xG4S_bNAb1-HCterminus of model V3-bNAb1 heavy chain with 1xG4Slinker, Fc includes M428L / N434SD1m-K8C-G99C_2xG4S_bNAb2-Human CD4 mD1.22 + K8C + G99C fused to the N- HCterminus of model V3-bNAb2 heavy chain with 2xG4Slinker, Fc includes M428L / N434SD1m-K8C-G99C_3xG4S_bNAb2-Human CD4 mD1.22 + K8C + G99C fused to the N- HCterminus of model V3-bNAb2 heavy chain with 3xG4Slinker, Fc includes M428L / N434SD1m-K8C-G99C_4xG4S_bNAb2-Human CD4 mD1.22 + K8C + G99C fused to the N- HCterminus of model V3-bNAb2 heavy chain with 4xG4Slinker, Fc includes M428L / N434SbNAb2-LC_1xG4S_D1m-K8C-Human CD4 mD1.22 + K8C + G99C fused to the C- G99Cterminus of model V3-bNAb2 light chain with 1xG4SlinkerD1m-K8C-G99C_1xG4S_bNAb3-Human CD4 mD1.22 + K8C + G99C fused to the N- HCterminus of model V3-bNAb3 heavy chain with 1xG4Slinker, Fc includes M428L / N434SD1m-K8C-G99C_4xG4S_bNAb3-Human CD4 mD1.22 + K8C + G99C fused to the N- HCterminus of model V3-bNAb3 heavy chain with 4xG4Slinker, Fc includes M428L / N434SD1m-K8C-G99C_4xG4S_bNAb4-Human CD4 mD1.22 + K8C + G99C fused to the N- HCterminus of model V3-bNAb4 heavy chain with 4xG4Slinker, Fc includes M428L / N434SD1m-K8C-G99C_Fc Human CD4 mD1.22 + K8C, G99C with C-terminal Fctag including M428L / N434SV3 loop V3 loop consensus sequenceExemplary gp160 Exemplary gp160 sequenceExemplary gp120 Exemplary gp120 sequenceExemplary gp41 Exemplary gp41 sequenceV1 / V2 loop Apex V1 / V2 apex consensus sequenceInterface Gp120-gp41 interface consensus non-continuoussequenceInterface bispecific (based onHuman CD4 mD1.22 + K8C + G99C fused to the N- Interface-bNAb17) terminus of interface-bNAb17 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecific (based onHuman CD4 mD1.22 + K8C + G99C fused to the N- interface-bNAb18) terminus of interface-bNAb18 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb19)terminus of interface-bNAb19 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on interface-bNAb20) terminus of interface-bNAb20 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb21)terminus of interface-bNAb21 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb22)terminus of interface-bNAb22 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb23)terminus of interface-bNAb23 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb24)terminus of interface-bNAb24 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on interface-bNAb25) terminus of interface-bNAb25 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb26)terminus of interface-bNAb26 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb27)terminus of interface-bNAb27 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb29)terminus of interface-bNAb29 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb30)terminus of interface-bNAb30 heavy chain with 1xG4S linker, Fc includes M428L / N434SInterface bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on interface-bNAb31)terminus of interface-bNAb31 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N-(based on Apex-bNAb1)terminus of apex-bNAb1 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb2) terminus of apex-bNAb2 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb3) terminus of apex-bNAb3 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb4) terminus of apex-bNAb4 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb5) terminus of apex-bNAb5 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb6) terminus of apex-bNAb7 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb7) terminus of apex-bNAb8 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecific (based onHuman CD4 mD1.22 + K8C + G99C fused to the N- Apex-bNAb8) terminus of apex-bNAb9 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb9) terminus of apex-bNAb10 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb10) terminus of apex-bNAb11 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb11) terminus of apex-bNAb12 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb12) terminus of apex-bNAb13 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb13) terminus of apex-bNAb14 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb14) terminus of apex-bNAb15 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb15) terminus of apex-bNAb16 heavy chain with 1xG4S linker, Fc includes M428L / N434SV1 / V2 apex bispecificHuman CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb16) terminus of apex-bNAb7 heavy chain with 1xG4S linker, Fc includes M428L / N434S(Interface-bNAb17) CDRH1 CDRH1 of interface-bNAb17(Interface-bNAb17) CDRH2 CDRH2 of interface-bNAb17(Interface-bNAb17) CDRH3 CDRH3 of interface-bNAb17(Interface-bNAb17) CDRL1 CDRL1 of interface-bNAb17(Interface-bNAb17) CDRL2 CDRL2 of interface-bNAb17(Interface-bNAb17) CDRL3 CDRL3 of interface-bNAb17(Interface-bNAb17) VH VH domain of interface-bNAb17(Interface-bNAb17) VL VL domain of interface-bNAb17(Interface-bNAb17) HC (no LS) Heavy chain of interface-bNAb17(Interface-bNAb17) HC (LS) Heavy chain of interface-bNAb17, Fc includesM428L / N434S(Interface-bNAb17) LC Light chain of interface-bNAb17(Interface-bNAb18) CDRH1 CDRH1 of interface-bNAb18(Interface-bNAb18) CDRH2 CDRH2 of interface-bNAb18(Interface-bNAb18) CDRH3 CDRH3 of interface-bNAb18(Interface-bNAb18) CDRL1 CDRL1 of interface-bNAb18(Interface-bNAb18) CDRL2 CDRL2 of interface-bNAb18(Interface-bNAb18) CDRL3 CDRL3 of interface-bNAb18(Interface-bNAb18) VH VH domain of interface-bNAb18(Interface-bNAb18) VL VL domain of interface-bNAb18(Interface-bNAb18) HC (no LS) Heavy chain of interface-bNAb18(Interface-bNAb18) HC (LS) Heavy chain of interface-bNAb18, Fc includesM428L / N434S(Interface-bNAb18) LC Light chain of interface-bNAb18(Interface-bNAb19) CDRH1 CDRH1 of interface-bNAb19(Interface-bNAb19) CDRH2 CDRH2 of interface-bNAb19(Interface-bNAb19) CDRH3 CDRH3 of interface-bNAb19(Interface-bNAb19) CDRL1 CDRL1 of interface-bNAb19(Interface-bNAb19) CDRL2 CDRL2 of interface-bNAb19(Interface-bNAb19) CDRL3 CDRL3 of interface-bNAb19(Interface-bNAb19) VH VH domain of interface-bNAb19(Interface-bNAb19) VL VL domain of interface-bNAb19(Interface-bNAb19) HC (no LS) Heavy chain of interface-bNAb19(Interface-bNAb19) HC (LS) Heavy chain of interface-bNAb19, Fc includesM428L / N434S(Interface-bNAb19) LC Light chain of interface-bNAb19(Interface-bNAb20) CDRH1 CDRH1 of interface-bNAb20(Interface-bNAb20) CDRH2 CDRH2 of interface-bNAb20(Interface-bNAb20) CDRH3 CDRH3 of interface-bNAb20(Interface-bNAb20) CDRL1 CDRL1 of interface-bNAb20(Interface-bNAb20) CDRL2 CDRL2 of interface-bNAb20(Interface-bNAb20) CDRL3 CDRL3 of interface-bNAb20(Interface-bNAb20) VH VH domain of interface-bNAb20(Interface-bNAb20) VL VL domain of interface-bNAb20(Interface-bNAb20) HC (no LS) Heavy chain of interface-bNAb20(Interface-bNAb20) HC (LS) Heavy chain of interface-bNAb20, Fc includesM428L / N434S(Interface-bNAb20) LC Light chain of interface-bNAb20(Interface-bNAb21) CDRH1 CDRH1 of interface-bNAb21(Interface-bNAb21) CDRH2 CDRH2 of interface-bNAb21(Interface-bNAb21) CDRH3 CDRH3 of interface-bNAb21(Interface-bNAb21) CDRL1 CDRL1 of interface-bNAb21(Interface-bNAb21) CDRL2 CDRL2 of interface-bNAb21(Interface-bNAb21) CDRL3 CDRL3 of interface-bNAb21(Interface-bNAb21) VH VH domain of interface-bNAb21(Interface-bNAb21) VL VL domain of interface-bNAb21(Interface-bNAb21) HC (no LS) Heavy chain of interface-bNAb21(Interface-bNAb21) HC (LS) Heavy chain of interface-bNAb21, Fc includesM428L / N434S(Interface-bNAb21) LC Light chain of interface-bNAb21(Interface-bNAb22) CDRH1 CDRH1 of interface-bNAb22(Interface-bNAb22) CDRH2 CDRH2 of interface-bNAb22(Interface-bNAb22) CDRH3 CDRH3 of interface-bNAb22(Interface-bNAb22) CDRL1 CDRL1 of interface-bNAb22(Interface-bNAb22) CDRL2 CDRL2 of interface-bNAb22(Interface-bNAb22) CDRL3 CDRL3 of interface-bNAb22(Interface-bNAb22) VH VH domain of interface-bNAb22(Interface-bNAb22) VL VL domain of interface-bNAb22(Interface-bNAb22) HC (no LS) Heavy chain of interface-bNAb22(Interface-bNAb22) HC (LS) Heavy chain of interface-bNAb22, Fc includesM428L / N434S(Interface-bNAb22) LC Light chain of interface-bNAb22(Interface-bNAb23) CDRH1 CDRH1 of interface-bNAb23(Interface-bNAb23) CDRH2 CDRH2 of interface-bNAb23(Interface-bNAb23) CDRH3 CDRH3 of interface-bNAb23(Interface-bNAb23) CDRL1 CDRL1 of interface-bNAb23(Interface-bNAb23) CDRL2 CDRL2 of interface-bNAb23(Interface-bNAb23) CDRL3 CDRL3 of interface-bNAb23(Interface-bNAb23) VH VH domain of interface-bNAb23(Interface-bNAb23) VL VL domain of interface-bNAb23(Interface-bNAb23) HC (no LS) Heavy chain of interface-bNAb23(Interface-bNAb23) HC (LS) Heavy chain of interface-bNAb23, Fc includesM428L / N434S(Interface-bNAb23) LC Light chain of interface-bNAb23(Interface-bNAb24) CDRH1 CDRH1 of interface-bNAb24(Interface-bNAb24) CDRH2 CDRH2 of interface-bNAb24(Interface-bNAb24) CDRH3 CDRH3 of interface-bNAb24(Interface-bNAb24) CDRL1 CDRL1 of interface-bNAb24(Interface-bNAb24) CDRL2 CDRL2 of interface-bNAb24(Interface-bNAb24) CDRL3 CDRL3 of interface-bNAb24(Interface-bNAb24) VH VH domain of interface-bNAb24(Interface-bNAb24) VL VL domain of interface-bNAb24(Interface-bNAb24) HC (no LS) Heavy chain of interface-bNAb24(Interface-bNAb24) HC (LS) Heavy chain of interface-bNAb24, Fc includesM428L / N434S(Interface-bNAb24) LC Light chain of interface-bNAb24(Interface-bNAb25) CDRH1 CDRH1 of interface-bNAb25(Interface-bNAb25) CDRH2 CDRH2 of interface-bNAb25(Interface-bNAb25) CDRH3 CDRH3 of interface-bNAb25(Interface-bNAb25) CDRL1 CDRL1 of interface-bNAb25(Interface-bNAb25) CDRL2 CDRL2 of interface-bNAb25(Interface-bNAb25) CDRL3 CDRL3 of interface-bNAb25(Interface-bNAb25) VH VH domain of interface-bNAb25(Interface-bNAb25) VL VL domain of interface-bNAb25(Interface-bNAb25) HC (no LS) Heavy chain of interface-bNAb25(Interface-bNAb25) HC (LS) Heavy chain of interface-bNAb25, Fc includesM428L / N434S(Interface-bNAb25) LC Light chain of interface-bNAb25(Interface-bNAb26) CDRH1 CDRH1 of interface-bNAb26(Interface-bNAb26) CDRH2 CDRH2 of interface-bNAb26(Interface-bNAb26) CDRH3 CDRH3 of interface-bNAb26(Interface-bNAb26) CDRL1 CDRL1 of interface-bNAb26(Interface-bNAb26) CDRL2 CDRL2 of interface-bNAb26(Interface-bNAb26) CDRL3 CDRL3 of interface-bNAb26(Interface-bNAb26) VH VH domain of interface-bNAb26(Interface-bNAb26) VL VL domain of interface-bNAb26(Interface-bNAb26) HC (no LS) Heavy chain of interface-bNAb26(Interface-bNAb26) HC (LS) Heavy chain of interface-bNAb26, Fc includesM428L / N434S(Interface-bNAb26) LC Light chain of interface-bNAb26(Interface-bNAb27) CDRH1 CDRH1 of interface-bNAb27(Interface-bNAb27) CDRH2 CDRH2 of interface-bNAb27(Interface-bNAb27) CDRH3 CDRH3 of interface-bNAb27(Interface-bNAb27) CDRL1 CDRL1 of interface-bNAb27(Interface-bNAb27) CDRL2 CDRL2 of interface-bNAb27(Interface-bNAb27) CDRL3 CDRL3 of interface-bNAb27(Interface-bNAb27) VH VH domain of interface-bNAb27(Interface-bNAb27) VL VL domain of interface-bNAb27(Interface-bNAb27) HC (no LS) Heavy chain of interface-bNAb27(Interface-bNAb27) HC (LS) Heavy chain of interface-bNAb27, Fc includesM428L / N434S(Interface-bNAb27) LC Light chain of interface-bNAb27(Interface-bNAb29) CDRH1 CDRH1 of interface-bNAb29(Interface-bNAb29) CDRH2 CDRH2 of interface-bNAb29(Interface-bNAb29) CDRH3 CDRH3 of interface-bNAb29(Interface-bNAb29) CDRL1 CDRL1 of interface-bNAb29(Interface-bNAb29) CDRL2 CDRL2 of interface-bNAb29(Interface-bNAb29) CDRL3 CDRL3 of interface-bNAb29(Interface-bNAb29) VH VH domain of interface-bNAb29(Interface-bNAb29) VL VL domain of interface-bNAb29(Interface-bNAb29) HC (no LS) Heavy chain of interface-bNAb29(Interface-bNAb29) HC (LS) Heavy chain of interface-bNAb29, Fc includesM428L / N434S(Interface-bNAb29) LC Light chain of interface-bNAb29(Interface-bNAb30) CDRH1 CDRH1 of interface-bNAb30(Interface-bNAb30) CDRH2 CDRH2 of interface-bNAb30(Interface-bNAb30) CDRH3 CDRH3 of interface-bNAb30(Interface-bNAb30) CDRL1 CDRL1 of interface-bNAb30(Interface-bNAb30) CDRL2 CDRL2 of interface-bNAb30(Interface-bNAb30) CDRL3 CDRL3 of interface-bNAb30(Interface-bNAb30) VH VH domain of interface-bNAb30(Interface-bNAb30) VL VL domain of interface-bNAb30(Interface-bNAb30) HC (no LS) Heavy chain of interface-bNAb30(Interface-bNAb30) HC (LS) Heavy chain of interface-bNAb30, Fc includesM428L / N434S(Interface-bNAb30) LC Light chain of interface-bNAb30(Interface-bNAb31) CDRH1 CDRH1 of interface-bNAb31(Interface-bNAb31) CDRH2 CDRH2 of interface-bNAb31(Interface-bNAb31) CDRH3 CDRH3 of interface-bNAb31(Interface-bNAb31) CDRL1 CDRL1 of interface-bNAb31(Interface-bNAb31) CDRL2 CDRL2 of interface-bNAb31(Interface-bNAb31) CDRL3 CDRL3 of interface-bNAb31(Interface-bNAb31) VH VH domain of interface-bNAb31(Interface-bNAb31) VL VL domain of interface-bNAb31(Interface-bNAb31) HC (no LS) Heavy chain of interface-bNAb31(Interface-bNAb30) HC (LS) Heavy chain of interface-bNAb31, Fc includesM428L / N434S(Interface-bNAb30) LC Light chain of interface-bNAb31(Apex-bNAb1) CDRH1 CDRH1 of apex-bNAb1(Apex-bNAb1) CDRH2 CDRH2 of apex-bNAb1(Apex-bNAb1) CDRH3 CDRH3 of apex-bNAb1(Apex-bNAb1) CDRL1 CDRL1 of apex-bNAb1(Apex-bNAb1) CDRL2 CDRL2 of apex-bNAb1(Apex-bNAb1) CDRL3 CDRL3 of apex-bNAb1(Apex-bNAb1) VH VH domain of apex-bNAb1(Apex-bNAb1) VL VL domain of apex-bNAb1(Apex-bNAb1) HC (no LS) Heavy chain of apex-bNAb1(Apex-bNAb1) HC (LS) Heavy chain of apex-bNAb1, Fc includes M428L / N434S(Apex-bNAb1) LC Light chain of apex-bNAb1(Apex-bNAb2) CDRH1 CDRH1 of apex-bNAb2(Apex-bNAb2) CDRH2 CDRH2 of apex-bNAb2(Apex-bNAb2) CDRH3 CDRH3 of apex-bNAb2(Apex-bNAb2) CDRL1 CDRL1 of apex-bNAb2(Apex-bNAb2) CDRL2 CDRL2 of apex-bNAb2(Apex-bNAb2) CDRL3 CDRL3 of apex-bNAb2(Apex-bNAb2) VH VH domain of apex-bNAb2(Apex-bNAb2) VL VL domain of apex-bNAb2(Apex-bNAb2) HC (no LS) Heavy chain of apex-bNAb2(Apex-bNAb2) HC (LS) Heavy chain of apex-bNAb2, Fc includes M428L / N434S(Apex-bNAb2) LC Light chain of apex-bNAb2(Apex-bNAb3) CDRH1 CDRH1 of apex-bNAb3(Apex-bNAb3) CDRH2 CDRH2 of apex-bNAb3(Apex-bNAb3) CDRH3 CDRH3 of apex-bNAb3(Apex-bNAb3) CDRL1 CDRL1 of apex-bNAb3(Apex-bNAb3) CDRL2 CDRL2 of apex-bNAb3(Apex-bNAb3) CDRL3 CDRL3 of apex-bNAb3(Apex-bNAb3) VH VH domain of apex-bNAb3(Apex-bNAb3) VL VL domain of apex-bNAb3(Apex-bNAb3) HC (no LS) Heavy chain of apex-bNAb3(Apex-bNAb3) HC (LS) Heavy chain of apex-bNAb3, Fc includes M428L / N434S(Apex-bNAb3) LC Light chain of apex-bNAb3(Apex-bNAb4) CDRH1 CDRH1 of apex-bNAb4(Apex-bNAb4) CDRH2 CDRH2 of apex-bNAb4(Apex-bNAb4) CDRH3 CDRH3 of apex-bNAb4(Apex-bNAb4) CDRL1 CDRL1 of apex-bNAb4(Apex-bNAb4) CDRL2 CDRL2 of apex-bNAb4(Apex-bNAb4) CDRL3 CDRL3 of apex-bNAb4(Apex-bNAb4) VH VH domain of apex-bNAb4(Apex-bNAb4) VL VL domain of apex-bNAb4(Apex-bNAb4) HC (no LS) Heavy chain of apex-bNAb4(Apex-bNAb4) HC (LS) Heavy chain of apex-bNAb4, Fc includes M428L / N434S(Apex-bNAb4) LC Light chain of apex-bNAb4(Apex-bNAb5) CDRH1 CDRH1 of apex-bNAb5(Apex-bNAb5) CDRH2 CDRH2 of apex-bNAb5(Apex-bNAb5) CDRH3 CDRH3 of apex-bNAb5(Apex-bNAb5) CDRL1 CDRL1 of apex-bNAb5(Apex-bNAb5) CDRL2 CDRL2 of apex-bNAb5(Apex-bNAb5) CDRL3 CDRL3 of apex-bNAb5(Apex-bNAb5) VH VH domain of apex-bNAb5(Apex-bNAb5) VL VL domain of apex-bNAb5(Apex-bNAb5) HC (no LS) Heavy chain of apex-bNAb5(Apex-bNAb5) HC (LS) Heavy chain of apex-bNAb5, Fc includes M428L / N434S(Apex-bNAb5) LC Light chain of apex-bNAb5(Apex-bNAb6) CDRH1 CDRH1 of apex-bNAb6(Apex-bNAb6) CDRH2 CDRH2 of apex-bNAb6(Apex-bNAb6) CDRH3 CDRH3 of apex-bNAb6(Apex-bNAb6) CDRL1 CDRL1 of apex-bNAb6(Apex-bNAb6) CDRL2 CDRL2 of apex-bNAb6(Apex-bNAb6) CDRL3 CDRL3 of apex-bNAb6(Apex-bNAb6) VH VH domain of apex-bNAb6(Apex-bNAb6) VL VL domain of apex-bNAb6(Apex-bNAb6) HC (no LS) Heavy chain of apex-bNAb6(Apex-bNAb6) HC (LS) Heavy chain of apex-bNAb6, Fc includes M428L / N434S(Apex-bNAb6) LC Light chain of apex-bNAb6(Apex-bNAb7) CDRH1 CDRH1 of apex-bNAb7(Apex-bNAb7) CDRH2 CDRH2 of apex-bNAb7(Apex-bNAb7) CDRH3 CDRH3 of apex-bNAb7(Apex-bNAb7) CDRL1 CDRL1 of apex-bNAb7(Apex-bNAb7) CDRL2 CDRL2 of apex-bNAb7(Apex-bNAb7) CDRL3 CDRL3 of apex-bNAb7(Apex-bNAb7) VH VH domain of apex-bNAb7(Apex-bNAb7) VL VL domain of apex-bNAb7(Apex-bNAb7) HC (no LS) Heavy chain of apex-bNAb7(Apex-bNAb7) HC (LS) Heavy chain of apex-bNAb7, Fc includes M428L / N434S(Apex-bNAb7) LC Light chain of apex-bNAb7(Apex-bNAb8) CDRH1 CDRH1 of apex-bNAb8(Apex-bNAb8) CDRH2 CDRH2 of apex-bNAb8(Apex-bNAb8) CDRH3 CDRH3 of apex-bNAb8(Apex-bNAb8) CDRL1 CDRL1 of apex-bNAb8(Apex-bNAb8) CDRL2 CDRL2 of apex-bNAb8(Apex-bNAb8) CDRL3 CDRL3 of apex-bNAb8(Apex-bNAb8) VH VH domain of apex-bNAb8(Apex-bNAb8) VL VL domain of apex-bNAb8(Apex-bNAb8) HC (no LS) Heavy chain of apex-bNAb8(Apex-bNAb8) HC (LS) Heavy chain of apex-bNAb8, Fc includes M428L / N434S(Apex-bNAb8) LC Light chain of apex-bNAb8(Apex-bNAb9) CDRH1 CDRH1 of apex-bNAb9(Apex-bNAb9) CDRH2 CDRH2 of apex-bNAb9(Apex-bNAb9) CDRH3 CDRH3 of apex-bNAb9(Apex-bNAb9) CDRL1 CDRL1 of apex-bNAb9(Apex-bNAb9) CDRL2 CDRL2 of apex-bNAb9(Apex-bNAb9) CDRL3 CDRL3 of apex-bNAb9(Apex-bNAb9) VH VH domain of apex-bNAb9(Apex-bNAb9) VL VL domain of apex-bNAb9(Apex-bNAb9) HC (no LS) Heavy chain of apex-bNAb9(Apex-bNAb9) HC (LS) Heavy chain of apex-bNAb9, Fc includes M428L / N434S(Apex-bNAb9) LC Light chain of apex-bNAb9(Apex-bNAb10) CDRH1 CDRH1 of apex-bNAb10(Apex-bNAb10) CDRH2 CDRH2 of apex-bNAb10(Apex-bNAb10) CDRH3 CDRH3 of apex-bNAb10(Apex-bNAb10) CDRL1 CDRL1 of apex-bNAb10(Apex-bNAb10) CDRL2 CDRL2 of apex-bNAb10(Apex-bNAb10) CDRL3 CDRL3 of apex-bNAb10(Apex-bNAb10) VH VH domain of apex-bNAb10(Apex-bNAb10) VL VL domain of apex-bNAb10(Apex-bNAb10) HC (no LS) Heavy chain of apex-bNAb10(Apex-bNAb10) HC (LS) Heavy chain of apex-bNAb10, Fc includes M428L / N434S(Apex-bNAb10) LC Light chain of apex-bNAb10(Apex-bNAb11) CDRH1 CDRH1 of apex-bNAb11(Apex-bNAb11) CDRH2 CDRH2 of apex-bNAb11(Apex-bNAb11) CDRH3 CDRH3 of apex-bNAb11(Apex-bNAb11) CDRL1 CDRL1 of apex-bNAb11(Apex-bNAb11) CDRL2 CDRL2 of apex-bNAb11(Apex-bNAb11) CDRL3 CDRL3 of apex-bNAb11(Apex-bNAb11) VH VH domain of apex-bNAb11(Apex-bNAb11) VL VL domain of apex-bNAb11(Apex-bNAb11) HC (no LS) Heavy chain of apex-bNAb11(Apex-bNAb11) HC (LS) Heavy chain of apex-bNAb11, Fc includes M428L / N434S(Apex-bNAb11) LC Light chain of apex-bNAb11(Apex-bNAb12) CDRH1 CDRH1 of apex-bNAb12(Apex-bNAb12) CDRH2 CDRH2 of apex-bNAb12(Apex-bNAb12) CDRH3 CDRH3 of apex-bNAb12(Apex-bNAb12) CDRL1 CDRL1 of apex-bNAb12(Apex-bNAb12) CDRL2 CDRL2 of apex-bNAb12(Apex-bNAb12) CDRL3 CDRL3 of apex-bNAb12(Apex-bNAb12) VH VH domain of apex-bNAb12(Apex-bNAb12) VL VL domain of apex-bNAb12(Apex-bNAb12) HC (no LS) Heavy chain of apex-bNAb12(Apex-bNAb12) HC (LS) Heavy chain of apex-bNAb12, Fc includes M428L / N434S(Apex-bNAb12) LC Light chain of apex-bNAb12(Apex-bNAb13) CDRH1 CDRH1 of apex-bNAb13(Apex-bNAb13) CDRH2 CDRH2 of apex-bNAb13(Apex-bNAb13) CDRH3 CDRH3 of apex-bNAb13(Apex-bNAb13) CDRL1 CDRL1 of apex-bNAb13(Apex-bNAb13) CDRL2 CDRL2 of apex-bNAb13(Apex-bNAb13) CDRL3 CDRL3 of apex-bNAb13(Apex-bNAb13) VH VH domain of apex-bNAb13(Apex-bNAb13) VL VL domain of apex-bNAb13(Apex-bNAb13) HC (no LS) Heavy chain of apex-bNAb13(Apex-bNAb13) HC (LS) Heavy chain of apex-bNAb13, Fc includes M428L / N434S(Apex-bNAb13) LC Light chain of apex-bNAb13(Apex-bNAb14) CDRH1 CDRH1 of apex-bNAb14(Apex-bNAb14) CDRH2 CDRH2 of apex-bNAb14(Apex-bNAb14) CDRH3 CDRH3 of apex-bNAb14(Apex-bNAb14) CDRL1 CDRL1 of apex-bNAb14(Apex-bNAb14) CDRL2 CDRL2 of apex-bNAb14(Apex-bNAb14) CDRL3 CDRL3 of apex-bNAb14(Apex-bNAb14) VH VH domain of apex-bNAb14(Apex-bNAb14) VL VL domain of apex-bNAb14(Apex-bNAb14) HC (no LS) Heavy chain of apex-bNAb14(Apex-bNAb14) HC (LS) Heavy chain of apex-bNAb14, Fc includes M428L / N434S(Apex-bNAb14) LC Light chain of apex-bNAb14398 (Apex-bNAb15) CDRH1 CDRH1 of apex-bNAb15399 (Apex-bNAb15) CDRH2 CDRH2 of apex-bNAb15400 (Apex-bNAb15) CDRH3 CDRH3 of apex-bNAb15401 (Apex-bNAb15) CDRL1 CDRL1 of apex-bNAb15402 (Apex-bNAb15) CDRL2 CDRL2 of apex-bNAb15403 (Apex-bNAb15) CDRL3 CDRL3 of apex-bNAb15404 (Apex-bNAb15) VH VH domain of apex-bNAb15405 (Apex-bNAb15) VL VL domain of apex-bNAb15406 (Apex-bNAb15) HC (no LS) Heavy chain of apex-bNAb15407 (Apex-bNAb15) HC (LS) Heavy chain of apex-bNAb15, Fc includes M428L / N434S408 (Apex-bNAb15) LC Light chain of apex-bNAb15409 (Apex-bNAb16) CDRH1 CDRH1 of apex-bNAb16410 (Apex-bNAb16) CDRH2 CDRH2 of apex-bNAb16411 (Apex-bNAb16) CDRH3 CDRH3 of apex-bNAb16412 (Apex-bNAb16) CDRL1 CDRL1 of apex-bNAb16413 (Apex-bNAb16) CDRL2 CDRL2 of apex-bNAb16414 (Apex-bNAb16) CDRL3 CDRL3 of apex-bNAb16415 (Apex-bNAb16) VH VH domain of apex-bNAb16416 (Apex-bNAb16) VL VL domain of apex-bNAb16417 (Apex-bNAb16) HC (no LS) Heavy chain of apex-bNAb16418 (Apex-bNAb16) HC (LS) Heavy chain of apex-bNAb16, Fc includes M428L / N434S419 Apex-bNAb16 LC Light chain of apex-bNAb16420 V1 / V2 apex bispecific 2Human CD4 mD1.22 + K8C + G99C fused to the N- (bispecific1-2, based on Apex- terminus of apex-bNAb1 light chain with 1xG4S linker, bNAb1) Fc includes M428L / N434S 421 V1 / V2 apex bispecific 3Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific1-3, based on Apex- terminus of apex-bNAb1 heavy chain with 1xG4S linker, bNAb1) Fc includes M428L / N434S 422 V1 / V2 apex bispecific 4Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific1-4, based on Apex- terminus of apex-bNAb1 light chain with 1xG4S linker, bNAb1) Fc includes M428L / N434S 423 V1 / V2 apex bispecific 2Human CD4 mD1.22 + K8C + G99C fused to the N- (bispecific2-2, based on Apex- terminus of apex-bNAb2 light chain with 1xG4S linker, bNAb2) Fc includes M428L / N434S 424 V1 / V2 apex bispecific 3Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific2-3, based on Apex- terminus of apex-bNAb2 heavy chain with 1xG4S linker, bNAb2) Fc includes M428L / N434S 425 V1 / V2 apex bispecific 4Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific2-4, based on Apex- terminus of apex-bNAb2 light chain with 1xG4S linker, bNAb2) Fc includes M428L / N434S 426 D1m-K8C-G99C_1xG4S_bNAb1- Human CD4 mD1.22 + K8C + G99C fused to the N-LCterminus of model V3-bNAb1 light chain with 1xG4Slinker SEQ ID NO: 1 (D1D2) KKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLK IEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLEL QDSGTWTCTVLQNQKKVEFKIDIVVLA SEQ ID NO:2 (D1mD2) KKVVLGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KIEDSDTYICEVEDQKEEVQLVVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLE LQDSGTWTCTVLQNQKKVEFKIDIVVLAF SEQ ID NO:3 (D1) KKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLK IEDSDTYICEVEDQKEEVQLLVFG SEQ ID NO:4 (D1m) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:5 (D1m-K8V) KKVVYGKVGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:6 (D1m-E91Q) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKQEVQLVVVG SEQ ID NO:7 (D1m-E91H) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKHEVQLVVVG SEQ ID NO:8 (D1m-E87G) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVGDQKEEVQLVVVG SEQ ID NO:9 (D1m-N52W) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLWDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:10 (D1m-K8I) KKVVYGKIGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLK PEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:11 (D1m-K8C-G99C) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVC SEQ ID NO:12 (D1m-T11C-K72C) KKVVYGKKGDCVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIICNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:13 (D1m-E13C-I70C) KKVVYGKKGDTVCLTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLCIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:14 (D1m-H27C-G38C) KKVVYGKKGDTVELTCTASQKKNIQFCWKNSNQIKILCNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:15 (D1m-K21C-G65C) KKVVYGKKGDTVELTCTASQCKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQCNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:16 (D1m-Q25E) KKVVYGKKGDTVELTCTASQKKNIEFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGSEQ ID NO:17 (D1m-H27D)KKVVYGKKGDTVELTCTASQKKNIQFDWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGSEQ ID NO:18 (D1m-R58V)KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSVRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:19 (D1m-R58N) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSNRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGSEQ ID NO:20 (D1m-R58T)KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSTRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:21 (D1m-L61M) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSMWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:22 (V3-bNAb1 HC+LS) QPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLK SRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGK SEQ ID NO:23 (V3-bNAb1 LC) QSALTQPPSASGSPGQSITISCTGTSNNFVSWYQQHAGKAPKLVIYDVNKRPSGVPDRFSGSKSGNTASLTVSG LQTDDEAVYYCGSLVGNWDVIFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKA DSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS SEQ ID NO:24 (V3-bNAb2 HC+LS) QMQLQESGPGLVKPSETLSLTCSVSGASISDSYWSWIRRSPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTS KNQVSLSLVAATAADSGKYYCARTLHGRRIYGIVAFNEWFTYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSK STSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSN TKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVE VHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDEL TKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEAL HSHYTQKSLSLSPGK SEQ ID NO:25 (V3-bNAb2 LC) SDISVAPGETARISCGEKSLGSRAVQWYQHRAGQAPSLIIYNNQDRPSGIPERFSGSPDSPFGTTATLTITSVEAG DEADYYCHIWDSRVPTKWVFGGGTTLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKAD SSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS SEQ ID NO:26 (V3-bNAb3 HC+LS) QVQLRESGPGLVKPSETLSLSCTVSNDSRPSDHSWTWVRQSPGKALEWIGDIHYNGATTYNPSLRSRVRIELDQ SIPRFSLKMTSMTAADTGMYYCARNAIRIYGVVALGEWFHYGMDVWGQGTAVTVSSASTKGPSVFPLAPSSKST SGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTK VDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTK NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHS HYTQKSLSLSPGK SEQ ID NO:27 (V3-bNAb3 LC) SSELTQPPSVSVSPGQTARITCSGAPLTSRFTYWYRQKPGQAPVLIISRSSQRSSGWSGRFSASWSGTTVTLTIR GVQADDEADYYCQSSDTSDSYKMFGGGTKLTVLGQPAAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTEC SEQ ID NO:28 (V3-bNAb4 HC+LS) QVQLQESGPGLVKPSETLSVTCSVSGDSMNNYYWTWIRQSPGKGLEWIGYISDRESATYNPSLNSRVVISRDTS KNQLSLKLNSVTPADTAVYYCATARRGQRIYGVVSFGEFFYYYSMDVWGKGTTVTVSSASTKGPSVFPLAPSSKS TSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNT KVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALH SHYTQKSLSLSPGK SEQ ID NO:29 (V3-bNAb4 LC) SYVRPLSVALGETARISCGRQALGSRAVQWYQHRPGQAPILLIYNNQDRPSGIPERFSGTPDINFGTRATLTISG VEAGDEADYYCHMWDSRSGFSWSFGGATRLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS SEQ ID NO:30 (1XG4S) GGGGS SEQ ID NO: 31 (2XG4S) GGGGSGGGGS SEQ ID NO: 32 (3XG4S) GGGGSGGGGSGGGGS SEQ ID NO: 33 (4XG4S) GGGGSGGGGSGGGGSGGGGS SEQ ID NO: 34 (5XG4S) GGGGSGGGGSGGGGSGGGGSGGGGS SEQ ID NO: 35 (6XG4S) GGGGSGGGGSGGGGSGGGGSGGGGSGGGGS SEQ ID NO: 36 (D1m_1xG4S_bNAb1-HC) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 37 (D1m_4xG4S_bNAb2-HC) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSGGGGSGGGGSGGGGSQPQLQESGPTLVEASETLSLTCAVSGDS TAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTAT YYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTV SWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPA PELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVL TVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEW ESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 38 (D1m_1xG4S_bNAb1-LC) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQSALTQPPSASGSPGQSITISCTGTSNNFVSWYQQHAGKAPKLV IYDVNKRPSGVPDRFSGSKSGNTASLTVSGLQTDDEAVYYCGSLVGNWDVIFGGGTKLTVLGQPKAAPSVTLFP PSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQ VTHEGSTVEKTVAPTECS SEQ ID NO: 39 (bNAb1-HC-mid_1xG4S_D1m-K8C-G99C) QPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLK SRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCGGGGSKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLN DRVDSRRSLWDQGNFPLIIKNLKPEDSDTYICEVEDQKEEVQLVVVCGGGGSDKTHTCPPCPAPELLGGPSVFLF PPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNG KEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY KTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 40 (bNAb1-HC_1xG4S_ D1m-K8C-G99C) QPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLK SRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGGGGGSKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSK LNDRVDSRRSLWDQGNFPLIIKNLKPEDSDTYICEVEDQKEEVQLVVVC SEQ ID NO: 41 (bNAb1-LC_1xG4S_D1m-K8C-G99C) QSALTQPPSASGSPGQSITISCTGTSNNFVSWYQQHAGKAPKLVIYDVNKRPSGVPDRFSGSKSGNTASLTVSG LQTDDEAVYYCGSLVGNWDVIFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKA DSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECSGGGGSKKVVYGK CGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLKPEDSDT YICEVEDQKEEVQLVVVC SEQ ID NO: 42 (D1m-K8I_1xG4S_bNAb1-HC) KKVVYGKIGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLK PEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPG KGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWP KPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 43 (D1m-K8V_1xG4S_bNAb1-HC) KKVVYGKVGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 44 (D1m-K8C-G99C_1xG4S_bNAb1-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 45 (D1m-T11C-K72C_1xG4S_bNAb1-HC) KKVVYGKKGDCVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIICNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 46 (D1m-K8C-G99C_2xG4S_bNAb2-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSQMQLQESGPGLVKPSETLSLTCSVSGASISDSYWSWIRR SPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTSKNQVSLSLVAATAADSGKYYCARTLHGRRIYGIVAFNEWF TYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 47 (D1m-K8C-G99C_3xG4S_bNAb2-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSQMQLQESGPGLVKPSETLSLTCSVSGASISDSY WSWIRRSPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTSKNQVSLSLVAATAADSGKYYCARTLHGRRIYGI VAFNEWFTYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVF LFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 48 (D1m-K8C-G99C_4xG4S_bNAb2-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSQMQLQESGPGLVKPSETLSLTCSVSGAS ISDSYWSWIRRSPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTSKNQVSLSLVAATAADSGKYYCARTLHGR RIYGIVAFNEWFTYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSG ALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQ DWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQ PENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 49 (bNAb2-LC_1xG4S_D1m-K8C-G99C) SDISVAPGETARISCGEKSLGSRAVQWYQHRAGQAPSLIIYNNQDRPSGIPERFSGSPDSPFGTTATLTITSVEAG DEADYYCHIWDSRVPTKWVFGGGTTLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKAD SSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECSGGGGSKKVVYGKC GDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLKPEDSDTYI CEVEDQKEEVQLVVVC SEQ ID NO: 50 (D1m-K8C-G99C_1xG4S_bNAb3-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLRESGPGLVKPSETLSLSCTVSNDSRPSDHSWTWVRQSPG KALEWIGDIHYNGATTYNPSLRSRVRIELDQSIPRFSLKMTSMTAADTGMYYCARNAIRIYGVVALGEWFHYGM DVWGQGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMIS RTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKA LPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDG SFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 51 (D1m-K8C-G99C_4xG4S_bNAb3-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSQVQLRESGPGLVKPSETLSLSCTVSNDS RPSDHSWTWVRQSPGKALEWIGDIHYNGATTYNPSLRSRVRIELDQSIPRFSLKMTSMTAADTGMYYCARNAI RIYGVVALGEWFHYGMDVWGQGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSG ALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQ DWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQ PENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 52 (D1m-K8C-G99C_4xG4S_bNAb4-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSQVQLQESGPGLVKPSETLSVTCSVSGDS MNNYYWTWIRQSPGKGLEWIGYISDRESATYNPSLNSRVVISRDTSKNQLSLKLNSVTPADTAVYYCATARRGQ RIYGVVSFGEFFYYYSMDVWGKGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGA LTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGP SVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQD WLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQP ENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 53 (D1m-K8C-G99C_Fc) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 54 (V3 loop) CTRPNNNTRKSIHIGPGRAFYTTGEIIGDIRQAHC SEQ ID NO: 55 (Exemplary gp160) MKVMGTKKNYQHLWRWGIMLLGMLMMSSAAEQLWVTVYYGVPVWREANTTLFCASDAKAYDTEVHNVWAT HACVPTDPNPQEVVMGNVTEDFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTA NVTMREEMKNCSFNTTTVIRDKIQKEYALFYKLDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPA GFAILKCNNKTFNGKGPCRNVSTVQCTHGIKPVVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCTR PGNNTRRSINIGPGRAFYATGAIIGDIRKAHCNISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDPEVVMHT FNCGGEFFYCNSTQLFNSTWFNNGTSTWNSTADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCSSNITGLI LTRDGGSNSSQNETFRPGGGNMKDNWRSELYKYKVVKIEPLGIAPTRAKRRVVQREKRAVTLGAVFLGFLGAAG STMGAASLTLTVQARLLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQARVLAIERYLKDQQLLGIWGCSGK LICTTTVPWNTSWSNKSYDYIWNNMTWMQWEREIDNYTGFIYTLIEESQNQQEKNELELLELDKWASLWNWF NITNWLWYIKLFIMIIGGLVGLRIVCAVLSIVNRVRQGYSPLSFQTRLPNPRGPDRPEETEGEGGERDRDRSARLV NGFLAIIWDDLRSLCLFSYHRLRDLLLIVARVVEILGRRGWEILKYWWNLLKYWSQELKNSAVSLLNVTAIAVAE GTDRVIEIVQRAVRAILHIPTRIRQGFERALL SEQ ID NO: 56 (Exemplary AEQLWVIVYYGVPVWREANTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVMGNVTEDFNMWKNNMV EQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTANVTMREEMKNCSFNTTTVIRDKIQKEYALFYK LDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGKGPCRNVSTVQCTHGIKP VVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCTRPGNNTRRSINIGPGRAFYATGAIIGDIRKAHC NISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDPEVVMHTFNCGGEFFYCNSTQLFNSTWFNNGTSTWNS TADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCSSNITGLILTRDGGSNSSQNETFRPGGGNMKDNWRSE LYKYKVVKIEPLGIAPTRAKRRVVQREKR SEQ ID NO: 57 (Exemplary AVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVER YLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNE QELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEG IEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQEL KNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL SEQ ID NO: 58 Apex CTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCSEQ ID NO: 59 InterfaceSDAKAYDTVPTDPNPQTKAKRRVVNASWSNKSLEQIWNSEQ ID NO: 60 PGT151 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSRVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGK GLEWVAAISGDAWHVVYSNSVQGRFLVSRDNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNY YYYSGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 61 PGT152 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSRVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGK GLEWVAAISADAWHVVYSGSVQGRFLVSRDNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNY YYYSGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 62 PGT153 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVESGGGVVQPGKSLRLSCVVSNFLFNKRHMHWVRQAPGK GLEWIAVISSDAIHVDYASSVRGRSLISRDNSKNSLYLDMNNLKIEDTATYYCARDRDGYGPPQIQTWSGRYLHL YSGIDAWGLGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTL MISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDS DGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 63 PGT154 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGK GLEWVAAISADAWHVDYAASVKDRFLISRDNSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYY HYFGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 64 PGT155 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVHLVESGGGVVQPGKSLRLSCETSGFIFNEYPMYWIRQAPGKG PEWVAAISADAWHVDYAGSVRGRFTVSRDNSKNSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLY HYTGFDVWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 65 PGT156 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGK GPEWVAAISADAWHVDYPGSVRGRFTVSRDNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNL YHYTGFDVWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 66 PGT157 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKG LEWVAAISADAWHVDYAGSVRGRFTVSRDNSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLY HYTGVDIWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKV SNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 67 PGT158 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVRLMESGGGVVQPGKSLRLSCVTSGFIFKKYPMYWIRQAPGKG LEWVAAISADAWHVDYPGSVRGRFTVSRDNSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLY HYTGVDVWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 68 8ANC195 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQIHLVQSGTEVKKPGSSVTVSCKAYGVNTFGLYAVNWVRQAPG QSLEYIGQIWRWKSSASHHFRGRVLISAVDLTGSSPPISSLEIKNLTSDDTAVYFCTTTSTYDKWSGLHHDGVM AFSSWGQGTLISVSAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMI SRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNK ALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSD GSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 69 35O22 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQGQLVQSGAELKKPGASVKISCKTSGYRFNFYHINWIRQTAGRG PEWMGWISPYSGDKNLAPAFQDRVIMTTDTEVPVTSFTSTGAAYMEIRNLKFDDTGTYFCAKGLLRDGSSTWL PYLWGQGTLLTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMIS RTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKA LPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDG SFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 70 ACS202 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGGVVQPGGSLRLSCAASGFAFKDFGMHWVRQAPGK GLEWVAVIGGGHGQHQSYSESVKGRFAITRDNEKNKLYLHMDRLRTEDTAVYYCAKDRLGRPWNIGGRLVYYY YGMDVWGQGTTATVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTL MISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDS DGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 71 LN02 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQAPLPESGPGVVRPTGTLSLTCTAAYGSISRHFWGWVRQSPQG TLEWIAHMHHLGVKYVNPSLKNRVSISMDTSKNQMSLTLKTVTATDAAKYHCVRMGARMSDIAFFSFGDWGPG SLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVV TVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCV VVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTI SKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLT VDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 72 CAP248-2B interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLQQSGPGLVKPSQTLSLTCNVYGVAISNEDYYWTWIRQHP GKGLEWIGDIYYNSGTTHYNPSLKSRASVSVDLSRNQFTLKVTSVTTADAAVYYCAREASTKITDDGGAFDFWG RGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLS SVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEV TCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPI EKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLY SKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 73 3BC315 interface bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGAEMKDPGASVKVSCRASGYKFTDYYMHWVRQAPG QGLEWVGWVNTNGGFTKYGAKFQGRVTVTRDTSTNTVFLELSRLTFGDTAMYFCARPMRPVSHGIDYSGLFVF QFWGRGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMIS RTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKA LPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDG SFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 74 CAP256V2LS V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVESGGGVVQPGTSLRLSCAASQFRFDGYGMHWVRQAPG KGLEWVASISHDGIKKYHAEKVWGRFTISRDNSKNTLYLQMNSLRPEDTALYYCAKDLREDECEEWWSDYYDF GAQLPCAKSRGGLVGIADNWGQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSG ALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQ DWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQ PENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 75 PGDM1400 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQAQLVQSGPEVRKPGTSVKVSCKAPGNTLKTYDLHWVRSVPGQ GLQWMGWISHEGDKKVIVERFKAKVTIDWDRSTNTAYLQLSGLTSGDTAVYYCAKGSKHRLRDYALYDDDGAL NWAVDVDYLSNLEFWGQGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 76 PG9 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQRLVESGGGVVQPGSSLRLSCAASGFDFSRQGMHWVRQAPGQ GLEWVAFIKYDGSEKYHADSVWGRLSISRDNSKDTLYLQMNSLRVEDTATYFCVREAGGPDYRNGYYYYDFYD GYYNYHYMDVWGKGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPK PKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEY KCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTT PPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 77 PG16 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQEQLVESGGGVVQPGGSLRLSCLASGFTFHKYGMHWVRQAPGK GLEWVALISDDGMRKYHSDSMWGRVTISRDNSKNTLYLQFSSLKVEDTAMFFCAREAGGPIWHDDVKYYDFN DGYYNYHYMDVWGKGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFP PKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGK EYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK TTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 78 PG20 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVRLVQSGPEVKKPGSSVTVSCQASGGTFSSYAFTWVRQAPGQ GLEWLGMVTPIFGEAKYSQRFEGRVTITADESTSTTSIELRGLTSEDTAIYYCARDRRAVPIATDNWLDPWGQG TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVV TVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCV VVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTI SKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLT VDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 79 PGG14 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVLLVQSGTEVKKPGSSVKVSCQASGGAFSSYAFSWVRQAPGQ GLEWMGMITPVFGETKYAPRFQGRLTLTAEESLSTTYMELRSLTSDDTAFYYCTRDRRVVPMATDNWLDPWGQ GTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV VTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTC VVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEK TISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSK LTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 80 PGC14 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSDGHLVQSGVEVKKTGATVKISCKVSGYSFIDYYLHWVQRAPGKG LEWVGLIDPENGEARYAEKFQGRVTIIADTSIDTGYMEMRSLKSEDTAVYFCAAGAVGADSGSWFDPWGQGTL VTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTV PSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVV DVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISK AKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVD KSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 81 CH01 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGANVVRPGGSLRLSCKASGFIFENFGFSWVRQAPGKG LQWVAGLNWNGGDTRYADSVKGRFRMSRDNSRNFVYLDMDKVGVDDTAFYYCARGTDYTIDDAGIHYQGSG TFWYFDLWGRGTLVSVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKV SNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 82 CH02 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGSVVRPGGSLRLSCRASGFIFENYGLTWVRQVPGKG LHWVSGMNWNGGDTRYADSVRGRFSMSRDNSNNIAYLQMNNLRVEDTALYYCARGTDYTIDDQGRFYQGSG TFWYFDFWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 83 CH03 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGGVVRPGGSLRLSCAASGFIFENYGLTWVRQVPGKG LHWVSGMNWNGGDTRYADSVRGRFSMSRDNSNNIAYLQMKNLRVDDTALYYCARGTDYTIDDQGIFYKGSGT FWYFDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKV SNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 84 CH04 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGGLIRPGGSLRLSCKGSGFIFENFGFGWVRQGPGKG LEWVSGTNWNGGDSRYGDSVKGRFTISRDNSNNFVYLQMNSLRPEDTAIYYCARGTDYTIDDQGIRYQGSGTF WYFDVWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTL MISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDS DGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 85 PGT141 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQ GLEWVGWMSHEGDKTESAQRFKGRVTFTRDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLI NYQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 86 PGT142 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQ GLEWVGWISHERDKTESAQRFKGRVTFTRDTSATTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLIN YQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLF PPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNG KEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY KTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 87 PGT143 V1 / V2 apex bispecific KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLEQSGAEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQ GLEWVGWMSHEGDKTESAQRFKGRVTFTRDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLI NYQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 88 PGT144 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGAEVKKPGSSVKVSCKASGNTFRKYDVHWVRQATGQ GLEWVGWMSHEGDKTESAQRFKGRVSFTRDNSASTAYIELRGLTSDDTAIYYCTGGSKHRLRDYVLYDDYGLI NQQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVF LFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 89 PGT145 V1 / V2 apex bispecificKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGAEVKKPGSSVKVSCKASGNSFSNHDVHWVRQATG QGLEWMGWMSHEGDKTGLAQKFQGRVTITRDSGASTVYMELRGLTADDTAIYYCLTGSKHRLRDYFLYNEYGP NYEEWGDYLATLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGKSEQ ID NO: 90 PGT151 (Interface-bNAb17) CDRH1KYPMYSEQ ID NO: 91 PGT151 (Interface-bNAb17) CDRH2AISGDAWHVVYSNSVQGSEQ ID NO: 92 PGT151 (Interface-bNAb17) CDRH3MFQESGPPRLDRWSGRNYYYYSGMDVSEQ ID NO: 93 PGT151 (Interface-bNAb17) CDRL1KSSESLRQSNGKTSLYSEQ ID NO: 94 PGT151 (Interface-bNAb17) CDRL2EVSNRFSSEQ ID NO: 95 PGT151 (Interface-bNAb17) CDRL3MQSKDFPLTSEQ ID NO: 96 PGT151 (Interface-bNAb17) VHRVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISGDAWHVVYSNSVQGRFLVSR DNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNYYYYSGMDVWGQGTTVTVSSSEQ ID NO: 97 PGT151 (Interface-bNAb17) VLDIVMTQTPLSLSVTPGQPASISCKSSESLRQSNGKTSLYWYRQKPGQSPQLLVFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLKSEQ ID NO: 98 PGT151 (Interface-bNAb17) HC (no LS)RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISGDAWHVVYSNSVQGRFLVSR DNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV MHEALHNHYTQKSLSLSPGKSEQ ID NO: 99 PGT151 (Interface-bNAb17) HC RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISGDAWHVVYSNSVQGRFLVSR DNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGKSEQ ID NO: 100 PGT151 (Interface-bNAb17) LCDIVMTQTPLSLSVTPGQPASISCKSSESLRQSNGKTSLYWYRQKPGQSPQLLVFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECSEQ ID NO: 101 PGT152 (Interface-bNAb18) CDRH1KYPMYSEQ ID NO: 102 PGT152 (Interface-bNAb18) CDRH2AISADAWHVVYSGSVQGSEQ ID NO: 103 PGT152 (Interface-bNAb18) CDRH3MFQESGPPRFDSWSGRNYYYYSGMDVSEQ ID NO: 104 PGT152 (Interface-bNAb18) CDRL1KSSQSLRQSNGKTSLYSEQ ID NO: 105 PGT152 (Interface-bNAb18) CDRL2EVSNRFSSEQ ID NO: 106 PGT152 (Interface-bNAb18) CDRL3MQSKDFPLTSEQ ID NO: 107 PGT152 (Interface-bNAb18) VHRVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISADAWHVVYSGSVQGRFLVSR DNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNYYYYSGMDVWGQGTTVTVSSSEQ ID NO: 108 PGT152 (Interface-bNAb18) VL DIVMTQTPLSLSVDPGQPASISCKSSQSLRQSNGKTSLYWYQQKPGQSPQLLIFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLNSEQ ID NO: 109 PGT152 (Interface-bNAb18) HC (no LS)RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISADAWHVVYSGSVQGRFLVSR DNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV MHEALHNHYTQKSLSLSPGKSEQ ID NO: 110 PGT152 (Interface- RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISADAWHVVYSGSVQGRFLVSR DNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGKSEQ ID NO: 111 PGT152 (Interface-bNAb18) LCDIVMTQTPLSLSVDPGQPASISCKSSQSLRQSNGKTSLYWYQQKPGQSPQLLIFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLNRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECSEQ ID NO: 112 PGT153 (Interface-bNAb19) CDRH1KRHMHSEQ ID NO: 113 PGT153 (Interface-bNAb19) CDRH2VISSDAIHVDYASSVRGSEQ ID NO: 114 PGT153 (Interface-bNAb19) CDRH3DRDGYGPPQIQTWSGRYLHLYSGIDASEQ ID NO: 115 PGT153 (Interface-bNAb19) CDRL1KSSQSLRQSNGKTYLY DIVLTQSPLFLSVSPGQPASISCKSSQSLRQSNGKTYLYWYVQKSGQSPQPLIQEVSIRFSGVPGRFAGSGSGTD FTLKISRVEAEDVGVYFCMQSKDFPLTFGGGTKVDLNSEQ ID NO: 120 PGT153 (Interface-bNAb19) HC (no LS)QVQLVESGGGVVQPGKSLRLSCVVSNFLFNKRHMHWVRQAPGKGLEWIAVISSDAIHVDYASSVRGRSLISRDN SKNSLYLDMNNLKIEDTATYYCARDRDGYGPPQIQTWSGRYLHLYSGIDAWGLGTTVTVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGKSEQ ID NO: 121 PGT153 (Interface-bNAb19) HC QVQLVESGGGVVQPGKSLRLSCVVSNFLFNKRHMHWVRQAPGKGLEWIAVISSDAIHVDYASSVRGRSLISRDN SKNSLYLDMNNLKIEDTATYYCARDRDGYGPPQIQTWSGRYLHLYSGIDAWGLGTTVTVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLH EALHSHYTQKSLSLSPGKSEQ ID NO: 122 PGT153 (Interface-bNAb19) LCDIVLTQSPLFLSVSPGQPASISCKSSQSLRQSNGKTYLYWYVQKSGQSPQPLIQEVSIRFSGVPGRFAGSGSGTD FTLKISRVEAEDVGVYFCMQSKDFPLTFGGGTKVDLNRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKV QWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECSEQ ID NO: 123 PGT154 (Interface-bNAb20) CDRH1KYPMYSEQ ID NO: 124 PGT154 (Interface-bNAb20) CDRH2AISADAWHVDYAASVKDSEQ ID NO: 125 PGT154 (Interface-bNAb20) CDRH3NIEEFSVPQFDSWSGRSYYHYFGMDVSEQ ID NO: 126 PGT154 (Interface-bNAb20) CDRL1SSSESLGRGDGRTYLHSEQ ID NO: 127 PGT154 (Interface-bNAb20) CDRL2EVSTRFSSEQ ID NO: 128 PGT154 (Interface-bNAb20) CDRL3MQSRDFPITSEQ ID NO: 129 PGT154 (Interface-bNAb20) VHQVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGKGLEWVAAISADAWHVDYAASVKDRFLISRD NSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYYHYFGMDVWGQGTTVTVSSSEQ ID NO: 130 PGT154 (Interface-bNAb20) VLDIVMTQTPVSLSVSLGQAASISCSSSESLGRGDGRTYLHWYRQKPGQTPQLLMYEVSTRFSGVSDRFAGSGSRT QFTLKISRVEAEDVGVYYCMQSRDFPITFGGGTRVDLKSEQ ID NO: 131 PGT154 (Interface-bNAb20) HC (no LS)QVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGKGLEWVAAISADAWHVDYAASVKDRFLISRD NSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYYHYFGMDVWGQGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGKSEQ ID NO: 132 PGT154 (Interface-bNAb20) HC (LS)QVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGKGLEWVAAISADAWHVDYAASVKDRFLISRD NSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYYHYFGMDVWGQGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGKSEQ ID NO: 133 PGT154 (Interface-bNAb20) LCDIVMTQTPVSLSVSLGQAASISCSSSESLGRGDGRTYLHWYRQKPGQTPQLLMYEVSTRFSGVSDRFAGSGSRT QFTLKISRVEAEDVGVYYCMQSRDFPITFGGGTRVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECSEQ ID NO: 134 PGT155 (Interface-bNAb21) CDRH1EYPMYSEQ ID NO: 135 PGT155 (Interface-bNAb21) CDRH2AISADAWHVDYAGSVRGSEQ ID NO: 136 PGT155 (Interface-bNAb21) CDRH3DGEEHKVPQLHSWSGRNLYHYTGFDVSEQ ID NO: 137 PGT155 (Interface-bNAb21) CDRL1KSSQSVRQSDGKTFLY QVHLVESGGGVVQPGKSLRLSCETSGFIFNEYPMYWIRQAPGKGPEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK QVHLVESGGGVVQPGKSLRLSCETSGFIFNEYPMYWIRQAPGKGPEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGK DIVMTQSPVSLSVTLGQPASMSCKSSQSVRQSDGKTFLYWYRQKPGQSPQLLIYEGSSRFSGVSDRISGSGSGT DFTLRISRVEAEDAGVYFCLQTKDFPLTFGGGTRVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECSEQ ID NO: 145 PGT156 (Interface-bNAb22) CDRH1QYPMYSEQ ID NO: 146 PGT156 (Interface-bNAb22) CDRH2AISADAWHVDYPGSVRGSEQ ID NO: 147 PGT156 (Interface-bNAb22) CDRH3DGEEHKVPQLHSWSGRNLYHYTGFDVSEQ ID NO: 148 PGT156 (Interface-bNAb22) CDRL1KSSQTVRQSDGKTFLYSEQ ID NO: 149 PGT156 (Interface-bNAb22) CDRL2EGSNRFSSEQ ID NO: 150 PGT156 (Interface-bNAb22) CDRL3LQTKDFPLTSEQ ID NO: 151 PGT156 (Interface-bNAb22) VHQVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGKGPEWVAAISADAWHVDYPGSVRGRFTVSR DNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSSEQ ID NO: 152 PGT156 (Interface-bNAb22) VLDIVMTQSPVSLSVTLGQPASMSCKSSQTVRQSDGKTFLYWYRQKAGQSPQLLIYEGSNRFSGVSDRISGSGSGT DFTLRISRVEAEDVGVYFCLQTKDFPLTFGGGTRVDIKSEQ ID NO: 153 PGT156 (Interface-bNAb22) HC (no LS)QVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGKGPEWVAAISADAWHVDYPGSVRGRFTVSR DNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV MHEALHNHYTQKSLSLSPGKSEQ ID NO: 154 PGT156 (Interface-bNAb22) HC QVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGKGPEWVAAISADAWHVDYPGSVRGRFTVSR DNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGKSEQ ID NO: 155 PGT156 (Interface-bNAb22) LCDIVMTQSPVSLSVTLGQPASMSCKSSQTVRQSDGKTFLYWYRQKAGQSPQLLIYEGSNRFSGVSDRISGSGSGT DFTLRISRVEAEDVGVYFCLQTKDFPLTFGGGTRVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECSEQ ID NO: 156 PGT157 (Interface-bNAb23) CDRH1QYPMYSEQ ID NO: 157 PGT157 (Interface-bNAb23) CDRH2AISADAWHVDYAGSVRGSEQ ID NO: 158 PGT157 (Interface-bNAb23) CDRH3DGEEHEVPQLHSWSGRNLYHYTGVDISEQ ID NO: 159 PGT157 (Interface-bNAb23) CDRL1KSSQSLRQSDGKTFLYSEQ ID NO: 160 PGT157 (Interface-bNAb23) CDRL2EASNRFSSEQ ID NO: 161 PGT157 (Interface-bNAb23) CDRL3MQTKDFPLTSEQ ID NO: 162 PGT157 (Interface-bNAb23) VHEVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKGLEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDIWGPGTTVTVSSSEQ ID NO: 163 PGT157 (Interface-bNAb23) VLDIVMTQTPVSLSVTLGQPASMSCKSSQSLRQSDGKTFLYWYRQKAGQSPQLLISEASNRFSGVSDRFSGSGSGT DFTLKISRVEAEDVGIYFCMQTKDFPLTFGGGTKVDLKSEQ ID NO: 164 PGT157 (Interface-bNAb23) HC (no LS)EVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKGLEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDIWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGKSEQ ID NO: 165 PGT157 (Interface-bNAb23) HC (LS)EVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKGLEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDIWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSN...

Claims

CLAIMS 1. A multimeric anti-HIV envelope spike complex-binding protein comprising:i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at leastone heavy chain or light chain, wherein the antibody binds to the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface region of a gp120 and a gp41 protein;and ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of at least one of the heavychains or light chains of the broadly neutralizing antibody.

2. The binding protein of claim 1, wherein the broadly neutralizing antibody binds to at leastone complex N-glycan at the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein.

3. A multimeric anti-HIV envelope spike complex-binding protein comprising:i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at leastone heavy chain or light chain, wherein the antibody binds to at least one complex N-glycan on a gp120 protein or a gp41 protein; andii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attacheddirectly or by a linker to the N-terminus or C-terminus of at least one of the heavy chains or light chains of the broadly neutralizing antibody.

4. The binding protein of claim 3, wherein the broadly neutralizing antibody binds to at leastone complex N-glycan at the V1 / V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein.

5. The binding protein of any preceding claim, wherein the binding protein is a bispecificbinding protein.

6. The binding protein of any preceding claim, wherein the CD4 domain is attached via a linkerto the N-terminus or C-terminus of at least one heavy chain or light chain of the broadlyneutralizing antibody.

7. The binding protein of any preceding claim, wherein the binding protein comprises at leastfour CD4 domains.

8. The binding protein of claim 7, wherein the C-terminus of each of the four CD4 domains isattached by a linker to the N-terminus of the two heavy chains and two light chains of the broadly neutralizing antibody.

9. The binding protein of any preceding claim, wherein the CD4 domain is attached via a linkerand said linker is selected from one of SEQ ID NOs: 30 to 35.

10. The binding protein of any preceding claim, wherein the CD4 domain comprises at least onemutation selected from: L5Y, S23N, A55V, I79P, L96V and / or F98V mutations.

11. The binding protein of any preceding claim, wherein the CD4 domain comprises or consistsof any one of SEQ ID NO: 4 – 21.

12. The binding protein of any preceding claim, wherein the broadly neutralizing antibodycomprises CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDLR3 as set out in any one row ofTable 3.

13. The binding protein of any preceding claim, wherein the broadly neutralizing antibodycomprises a heavy chain variable domain and a light chain variable domain pair that is at least 95% identical to any of the variable domain pairs set out in any one row of Table 4.

14. The binding protein of any preceding claim, wherein the broadly neutralizing antibodycomprises a heavy chain and a light chain pair that is at least 95% identical to any of the chain pairs set out in any one row of Table 4.

15. The binding protein of any preceding claim, wherein the binding protein comprises orconsists of a sequence at least 95% identical to any one of SEQ ID NO: 60-73 or 74-89.

16. A pharmaceutical composition comprising the binding protein as defined in any one of thepreceding claims and a pharmaceutically acceptable excipient.

17. A method of treating or preventing an HIV infection in a human comprising administering tothe human an anti-HIV binding protein according to any one of claims 1 to 15, or a pharmaceutical composition according to claim 16.

18. An anti-HIV binding protein according to any one of claims 1 to 15, or a pharmaceuticalcomposition according to claim 16, for use in treating or preventing an HIV infection in a human.

19. Use of an anti-HIV binding protein according to any one of claims 1 to 15, or apharmaceutical composition according to claim 16, in the manufacture of a medicament for treating or preventing an HIV infection in a human.

20. The method according to claim 17, protein or composition for use according to claim 18, oruse according to claim 19, wherein HIV viral load in the human is decreased.

21. A kit comprising in separate containers: an anti-HIV binding protein according to any one ofclaims 1 to 15 or a pharmaceutical composition according to claim 16, and at least one anti-viral drug that inhibits cellular entry, replication, or transcription of HIV in a human.

22. The kit as claimed in claim 21, wherein the antiviral drug is selected from: NucleosideReverse Transcriptase Inhibitors (NRTIs), Non-Nucleoside Reverse Transcriptase Inhibitors (NNRTIs), Protease Inhibitors (PIs), Entry Inhibitors, Integrase Strand Transfer Inhibitors (INSTI), Maturation Inhibitors (MIs), Capsid Inhibitors (CIs) and Nucleoside Reverse Transcriptase Translocation Inhibitors (NRTTIs).

23. A nucleic acid sequence that encodes an anti-HIV binding protein according to any one ofclaims 1 to 15.

24. An expression vector that comprises the nucleic acid sequence of claim 23.

25. A recombinant host cell that comprises the nucleic acid sequence of claim 23 or theexpression vector of claim 24.

26. A method of producing an anti-HIV binding protein, comprising culturing the host cell asdefined in claim 25 under conditions suitable for expression of said nucleic acid sequence orvector, whereby an anti-HIV binding protein is produced.

27. The anti-HIV binding protein produced by the method of claim 26.

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