Fusogenic rhabdovirus glycoproteins and uses thereof

Abstract

The present specification provides fusogenic rhabdovirus glycoprotein and its use, the composition comprising it, and the method of using it.The present specification also provides pseudotyped virus particles comprising the rhabdovirus glycoprotein provided herein and the targeting moiety provided herein.The present specification also provides the method of producing and using the pseudotyped virus particles provided herein.

Description

[Technical Field]

[0001] CROSS-REFERENCE TO RELATED APPLICATIONS This application claims the benefit of U.S. Provisional Application No. 63 / 267,870, filed February 11, 2022, the entire contents of which are incorporated herein by reference.

[0002] Reference to an electronically submitted sequence listing This application contains a Sequence Listing that has been submitted electronically in XML format, the entire contents of which are incorporated herein by reference. The XML copy, created on February 3, 2023, is named INH_018WO_SL.xml and is 73 kilobytes in size.

[0003] Embodiments provided herein relate to certain rhabdovirus glycoproteins and compositions comprising same, as well as methods of using same. [Background technology]

[0004] Rhabdoviridae is a family of negative-strand RNA viruses that infect specific cell types. The G structural protein may play an important role in the early stages of viral infection. First, it attaches the virus to specific receptors. After binding, the virus particles enter the cell via clathrin-mediated endocytosis. In the acidic environment of the endocytic vesicle, G triggers fusion of the viral membrane with the endosomal membrane, releasing the genome into the cytoplasm for the next stage of infection.

[0005] The G proteins of various Rhabdoviridae can be used for viral pseudotyping and promote viral fusion between different cell types, for example, the VSV-G protein is widely used. However, the wild-type VSV-G protein has a broad tropism because it binds to the low-density lipoprotein receptor (LDL-R), and other members of this receptor family function as VSV receptors (Finkelshtein, D., Werman, A., Novick, D., Barak, S., and Rubinstein, M. (2013). The LDL receptor and its family members serve as cellular receptors for vesicular stomatitis virus. Proceedings of the National Academy of Sciences of the United States of America 110, 7306-7311, the entire contents of which are incorporated herein by reference). However, this broad tropism can hinder selective targeting of specific cell types. Therefore, there is a need for modified alternative fusion proteins that can be used to pseudotype viruses that will specifically fuse with desired cells. The present embodiments meet these and other needs. Summary of the Invention

[0006] In some embodiments, a viral particle is provided, in which the viral particle comprises a targeting moiety and a polypeptide comprising a viral structural protein comprising a sequence that is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the sequence of SEQ ID NO:1 or SEQ ID NO:2.

[0007] In some embodiments, a pharmaceutical composition is provided comprising a viral particle described herein.

[0008] In some embodiments, methods for preparing the viral particles described herein are provided.

[0009] In some embodiments, methods of delivering a heterologous molecule to a target cell are provided, hi some embodiments, the methods comprise contacting the cell with a viral particle provided herein.

[0010] In some embodiments, methods for delivering a heterologous molecule to a target cell in a subject are provided, in some embodiments, the methods comprise administering to the subject a viral particle provided herein, or a pharmaceutical composition comprising the same.

[0011] In some embodiments, methods of treating cancer in a subject are provided, in some embodiments, the methods include administering to the subject a viral particle provided herein, or a pharmaceutical composition comprising the same. [Brief explanation of the drawings]

[0012] [Figure 1] Figure 1 shows the ability of various rhabdovirus G proteins to transduce SupT1 and PBMC cells alone or in combination with CD7 binders. [Figure 2] A shows the ability of SVCV-G pseudotyped lentiviral particles containing a CD7 binder attached to the viral surface via the Fc domain to transduce SupT1 cells and human and non-human primate PBMCs. B shows the transduction of cells in the absence of a CD7 binder. C shows the transduction of human and non-human primate PBMCs in terms of the MOI calculated from the SupT1 titration. [Figure 3] A shows the ability of SVCV-G pseudotyped lentiviral particles containing a CD7 binder attached to the viral surface via a polypeptide stalk to transduce SupT1 cells and human and non-human primate PBMCs. B shows transduction of cells in the absence of a CD7 binder. C shows transduction of human and non-human primate PBMCs in terms of the MOI calculated from the SupT1 titration. [Figure 4](A) Off-target transduction of GFP in a panel of B cell lines compared to control SupT1 cells with SVCV-G pseudotyped lentiviral particles containing a CD7 binder attached to the viral surface via the Fc domain. (B) Off-target transduction of the CAR20-T2A-GFP construct in a panel of B cell lines compared to control SupT1 cells with SVCV-G pseudotyped lentiviral particles containing a CD7 binder attached to the viral surface via the Fc domain. [Figure 5] Figure 1A shows off-target transduction of GFP in a panel of B cell lines compared to control SupT1 cells for SVCV-G pseudotyped lentiviral particles containing a CD7 binder attached to the viral surface via a polypeptide stalk. Figure 1B shows off-target transduction of the CAR20-T2A-GFP construct in a panel of B cell lines compared to control SupT1 cells for SVCV-G pseudotyped lentiviral particles containing a CD7 binder attached to the viral surface via a polypeptide stalk. DETAILED DESCRIPTION OF THE INVENTION

[0013] The present disclosure provides viral particles containing non-human rhabdovirus glycoproteins, which can be used to pseudotype viruses such as lentiviruses. In some embodiments, the pseudotyped virus-like particles are pseudotyped using the viral glycoprotein of the spring viremia of carp virus, for example, the spring viremia of carp virus G protein. In some embodiments, the viral particles comprise the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2. In some embodiments, the viral particles comprise an amino acid sequence that is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the sequence of SEQ ID NO: 1 or SEQ ID NO: 2.

[0014] Pseudotyped viruses containing the Carp Spring Viremia Virus G protein can be used in combination with a targeting moiety to facilitate fusion of the pseudotyped virus with specific cells or tissues based on the expression of the target on the cell or tissue.

[0015] Unless otherwise defined, all technical and scientific terms have the same meaning as commonly understood by one of ordinary skill in the art to which the disclosed embodiments belong.

[0016] As used herein, the terms "a" or "an" mean "at least one" or "one or more" unless the context clearly indicates otherwise.

[0017] As used herein, the term "about" means that a numerical value is approximate and that small variations do not significantly affect the practice of the disclosed embodiments. When numerical limitations are used, unless the context indicates otherwise, "about" means that the numerical value can vary by ±10% and still remain within the scope of the disclosed embodiments. Furthermore, in the phrase "about x to y," the term "about" modifies both x and y and can be used interchangeably with the phrase "about x to about y," unless the context indicates otherwise.

[0018] As used herein, the terms "individual" or "subject" or "patient" are used interchangeably and refer to any animal, including mammals such as mice, rats, other rodents, rabbits, dogs, cats, pigs, cows, sheep, horses, or primates, such as humans.

[0019] As used herein, the terms "comprising" (and any form of "comprising," such as "comprise," "comprises," and "comprised"), "having" (and any form of "having," such as "have" and "has"), "including" (and any form of "including," such as "includes" and "include"), or "containing" (and any form of "containing," such as "contains" and "contain") are inclusive or open-ended and do not exclude additional, unrecited elements or method steps. Any step or composition using the transitional phrase "comprise" or "comprising" can also be said to describe the same thing using the transitional phrase "consisting" or "consists."

[0020] As used herein, the term "contacting" refers to bringing two elements together in an in vitro system or in vivo system. For example, "contacting" a virus or vector described herein with an individual or patient or cell includes administering the virus to an individual or patient, such as a human, as well as introducing a compound into a sample, including, for example, a cell preparation or purified preparation containing the cell.

[0021] As used herein, the terms "fused" or "linked" when used with respect to proteins having different domains or heterologous sequences means that the protein domains are part of the same peptide chain, connected to each other by peptide bonds or other covalent bonds. Domains or sections can be directly linked or fused to each other, or another domain or peptide sequence can be between the two domains or sequences, and such sequences are still considered to be fused or linked to each other. In some embodiments, the various domains or proteins provided herein are directly linked or fused to each other, or a linker sequence, such as the glycine / serine sequences described herein, links the two domains.

[0022] A "disease" is an animal's health condition in which the animal is unable to maintain homeostasis, and if the disease is not improved, the animal's health will continue to deteriorate.In contrast, an animal's "disorder" refers to a health condition in which the animal is able to maintain homeostasis, but the animal's health condition is less favorable than if the disorder were not present.If the disorder is left untreated, the disorder does not necessarily further deteriorate the animal's health condition.

[0023] "Effective amount" or "therapeutically effective amount," as used interchangeably herein, refer to an amount of a compound, formulation, substance, or composition described herein that is effective to achieve a particular biological result or to provide a therapeutic or prophylactic benefit. Such results may include, but are not limited to, an amount that, when administered to a mammal, causes a detectable level of immune cell activation compared to immune cell activation detected in the absence of the composition. The immune response may be readily assessed by a number of art-recognized methods. One of skill in the art will understand that the amount of the composition administered herein will vary and may be readily determined based on many factors, such as the disease or condition being treated, the age and health and physical condition of the mammal being treated, the severity of the disease, and the particular compound being administered.

[0024] "Encoding" refers to the inherent property of a particular sequence of nucleotides in a polynucleotide, such as a gene, cDNA, or mRNA, to serve as a template for the synthesis of other polymers and macromolecules in biological processes that have either a defined sequence of nucleotides (i.e., rRNA, tRNA, and mRNA) or a defined sequence of amino acids, and the biological properties resulting therefrom. Thus, a gene encodes a protein when transcription and translation of the mRNA corresponding to that gene produces the protein in a cell or other biological system. Both the coding strand, whose nucleotide sequence is identical to the mRNA sequence and is usually provided in a sequence listing, and the non-coding strand, which is used as a template for transcription of the gene or cDNA, can be said to encode the protein or other product of that gene or cDNA.

[0025] An "expression vector" refers to a vector containing a recombinant polynucleotide comprising an expression control sequence operably linked to a nucleotide sequence to be expressed. An expression vector contains sufficient cis-acting elements for expression; other elements for expression can be supplied by the host cell or in an in vitro expression system. Expression vectors include all expression vectors known in the art, such as cosmids, plasmids (e.g., naked or contained in liposomes), and viruses (e.g., Sendai virus, lentivirus, retrovirus, adenovirus, and adeno-associated virus) that incorporate the recombinant polynucleotide.

[0026] As used herein, the phrase "ex vivo" with respect to cells that have been transduced, transfected or transformed ex vivo refers to cells that have been transduced, transfected or transformed outside of a subject, i.e., cells that are removed from a subject before being so transduced, transfected or transformed.

[0027] As used herein, "identity" refers to the identity of the subunit sequences between two polymer molecules, such as between two nucleic acid molecules or amino acid molecules, for example, between two polynucleotide molecules or polypeptide molecules. If two amino acid sequences have the same residue at the same position, for example, if each position in two polypeptide molecules is occupied by arginine, they are identical at that position. The identity or degree to which two amino acid sequences or two nucleic acid sequences have the same residue at the same position in an alignment is often expressed as a percentage. The identity between two amino acid sequences or two nucleic acid sequences directly depends on the number of matching or identical positions; for example, if half of the positions in the two sequences are identical, the two sequences are 50% identical; if 90% (e.g., 9 out of 10) of the positions are identical or matched, the two amino acid sequences are 90% identical.

[0028] "Substantially identical" means that a polypeptide or nucleic acid molecule exhibits at least 50% identity to a reference amino acid sequence (e.g., any one of the amino acid sequences described herein) or nucleic acid sequence (e.g., any one of the nucleic acid sequences described herein). In some embodiments, such a sequence is at least 60%, 80%, or 85%, or 90%, 95%, or even 99% identical at the amino acid or nucleic acid level to the sequence used for comparison. Other identity percentages for specific sequences are described herein.

[0029] Sequence identity can be measured / determined using sequence analysis software (e.g., Sequence Analysis Software Package of the Genetics Computer Group, University of Wisconsin Biotechnology Center, 1710 University Avenue, Madison, Wis. 53705, BLAST, BESTFIT, GAP, or PILEUP / PRETTYBOX programs). Such software matches identical or similar sequences by assigning degrees of homology to various substitutions, deletions, and / or other modifications. Conservative substitutions typically include substitutions within the following groups: glycine, alanine, valine, isoleucine, leucine, aspartic acid, glutamic acid, asparagine, glutamine, serine, threonine, lysine, arginine, and phenylalanine, tyrosine. An exemplary method for measuring the degree of identity can use the BLAST program, where a probability score of e3 to e100 indicates closely related sequences. In some embodiments, sequence identity is determined using BLAST with default settings.

[0030] To the extent that embodiments provided herein include compositions comprising various proteins, these proteins may, in some cases, comprise amino acid sequences that share sequence identity with the amino acid sequences disclosed herein. Thus, in certain embodiments, depending on the particular sequence, the degree of sequence identity is greater than 50% (e.g., 60%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more) to the SEQ ID NOs disclosed herein. In addition to these percentages, other identity percentages are also provided herein. Identity between polypeptides may be determined by the Smith-Waterman homology search algorithm as implemented in the MPSRCH program (Oxford Molecular) using an affine gap search with parameters of a gap opening penalty of -12 and a gap extension penalty of 1.

[0031] These proteins may contain one or more (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, etc.) conservative amino acid substitutions, i.e., substitution of one amino acid for another amino acid with a related side chain, compared to the disclosed proteins. Genetically encoded amino acids are generally classified into four families: (1) acidic, i.e., aspartic acid, glutamic acid; (2) basic, i.e., lysine, arginine, histidine; (3) nonpolar, i.e., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan; and (4) uncharged polar, i.e., glycine, asparagine, glutamine, cysteine, serine, threonine, tyrosine. Phenylalanine, tryptophan, and tyrosine are sometimes collectively classified as aromatic amino acids. Typically, substitution of a single amino acid within these families does not significantly affect biological activity. The proteins can have one or more (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, etc.) single amino acid deletions relative to the disclosed protein sequences. The proteins can also include one or more (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, etc.) insertions (e.g., of 1, 2, 3, 4, or 5 amino acids each) relative to the disclosed protein sequences.

[0032] As used herein, the term "in vivo" with respect to cells that have been transduced, transfected or transformed in vivo refers to cells that have been transduced, transfected or transformed in a subject where the cells have not been removed from the subject before the cells have been so transduced, transfected or transformed.

[0033] "Isolated" means altered or removed from the natural state. For example, a nucleic acid or peptide naturally present in a living animal is not "isolated," but the same nucleic acid or peptide would be "isolated" if it was partially or completely separated from the coexisting materials of its natural state. An isolated nucleic acid or protein can exist in a substantially purified form or can exist in a non-native environment, such as a host cell.

[0034] As used herein, "lentivirus" refers to a genus of the Retroviridae family that can infect non-dividing cells. Non-limiting examples of lentiviruses are HIV, SIV, and FIV. Lentivirus-derived vectors or virus-like particles can be used to transduce cells to deliver genes or other molecules and express them in cells in vitro (ex vivo) or in vivo.

[0035] As used herein, the term "modified" refers to an altered state or structure of a molecule or cell provided herein. Molecules can be modified in a variety of ways, including chemically, structurally, and functionally, such as by mutation, substitution, insertion, or deletion (e.g., internal deletion, truncation). Cells can be modified through the introduction of a nucleic acid or the expression of a heterologous protein.

[0036] As used herein, the term "modulation" means mediating an increase or decrease in the level of a subject's response compared to the level of the subject's response in the absence of the treatment or compound and / or compared to the level of the response in an otherwise identical subject not receiving the treatment. The term encompasses disrupting and / or affecting the natural signal or response, thereby mediating a beneficial therapeutic response in a subject, such as a human.

[0037] Unless otherwise specified, a "nucleotide sequence encoding an amino acid sequence" includes all nucleotide sequences that are degenerate versions of each other and that encode the same amino acid sequence. The phrase nucleotide sequence encoding a protein or RNA can include introns, to the extent that a nucleotide sequence that encodes a protein may, in some versions, contain intron(s).

[0038] The term "oligonucleotide" generally refers to a short polynucleotide. When a nucleotide sequence is represented by a DNA sequence (i.e., A, T, C, G), it is understood that this also provides the corresponding RNA sequence (i.e., A, U, C, G) in which "T" is replaced by "U".

[0039] "Parenteral" administration of the compositions includes, for example, subcutaneous (sc), intravenous (iv), intramuscular (im), or intrasternal injection or infusion techniques.

[0040] The term "polynucleotide," as used herein, is defined as a chain of nucleotides. Furthermore, a nucleic acid is a polymer of nucleotides. Therefore, the terms "nucleic acid" and "polynucleotide," as used herein, are interchangeable. As used herein, polynucleotide includes, but is not limited to, all nucleic acid sequences obtained by any method available in the art, including, but not limited to, recombinant methods, i.e., cloning and synthetic means of nucleic acid sequences from recombinant libraries or cell genomes using cloning techniques and PCR, etc.

[0041] As used herein, the terms "peptide," "polypeptide," and "protein" are used interchangeably and refer to compounds composed of multiple amino acid residues covalently linked by peptide bonds. As used herein, the term refers to both short chains, e.g., also commonly referred to in the art as peptides, oligopeptides, and oligomers, and longer chains, of which there are many varieties, commonly referred to in the art as proteins. "Polypeptide" includes, for example, biologically active fragments, substantially homologous polypeptides, oligopeptides, homodimers, heterodimers, polypeptide variants, modified polypeptides, derivatives, analogs, fusion proteins, and the like, among others. Polypeptides include natural peptides, recombinant peptides, synthetic peptides, or combinations thereof.

[0042] As used herein, the term "pseudotyped" or "pseudotyped virus particle" refers to a viral particle that contains glycoproteins derived from other enveloped viruses or a viral vector that encodes envelope glycoproteins from a virus different from the parent virus. Thus, the host range of the vector particle can be expanded or altered depending on the type of cell surface receptor used by the glycoprotein. For example, as described herein, a virus can be pseudotyped using the carp spring viremia virus G protein.

[0043] The term "specifically binds" as used herein with respect to antibodies refers to an antibody that recognizes a specific antigen but does not substantially recognize or bind other molecules in a sample. For example, an antibody that specifically binds to an antigen from one species may also bind that antigen from one or more other species. However, such cross-species reactivity does not, in itself, alter the antibody's classification as specific. In another example, an antibody that specifically binds to an antigen may also bind to different allelic forms of the antigen. However, such cross-reactivity does not, in itself, alter the antibody's classification as specific. In some cases, the terms "specific binding" or "specifically binds" are used in reference to the interaction of an antibody, protein, or peptide with a second chemical species to mean that the interaction is dependent on the presence of a specific structure (e.g., an antigenic determinant or epitope) on the chemical species; for example, an antibody recognizes and binds to a specific protein structure rather than proteins in general. If an antibody is specific for epitope "A," the presence of a molecule containing epitope A (or unlabeled, free A) in a reaction containing labeled "A" and the antibody will reduce the amount of labeled A that binds to the antibody. In some embodiments, the targeting moieties described herein that can be used to target a viral particle comprising the Carp Spring Viremia Virus G protein are capable of specifically binding to that target.

[0044] The term "subject" includes living organisms (e.g., mammals), including those in which an immune response can be elicited. As used herein, "subject" or "patient" refers to a human or non-human mammal. Non-human mammals include, for example, livestock and pets, such as ovine, bovine, porcine, canine, non-human primates, feline and murine mammals. In some embodiments, the subject is a human.

[0045] The term "therapeutic" as used herein means treatment and / or prophylaxis. A therapeutic effect is achieved by suppression, amelioration, or eradication of a disease condition.

[0046] As used herein, the terms "transfected" or "transformed" or "transduced" refer to the process by which exogenous nucleic acid is transferred or introduced into a cell. A "transfected" or "transformed" or "transduced" cell is one that has been transfected, transformed, or transduced with exogenous nucleic acid. This cell includes the primary subject cell and its progeny. In some embodiments, transfection, transformation, or transduction is performed or occurs in vivo.

[0047] "Treating" a disease, as that term is used herein, means reducing the frequency or severity of at least one sign or symptom of the disease or disorder experienced by a subject.

[0048] A "vector" is a composition of matter comprising an isolated nucleic acid encoding a protein or peptide. Numerous vectors are known in the art, including, but not limited to, linear polynucleotides, plasmids, DNA, and RNA. Examples of viral vectors include, but are not limited to, Sendai virus vectors, adenovirus vectors, adeno-associated virus vectors, retrovirus vectors, lentivirus vectors, and the like.

[0049] "Carriers" or "delivery vehicles" include viral particles, viruses, polylysine compounds, and liposomes, which facilitate the transfer of nucleic acids into cells. Carriers or delivery vehicles can also be used to deliver proteins or peptides to cells.

[0050] Regarding ranges, various aspects of the embodiments can be expressed in range format throughout this disclosure. It should be understood that the description in range format is merely for convenience and brevity and should not be construed as an inflexible limitation. Thus, the description of a range should be considered to have specifically disclosed all possible subranges and individual numerical values ​​within that range. For example, a description of a range such as 1 to 6 should be considered to have specifically disclosed subranges such as 1 to 3, 1 to 4, 1 to 5, 2 to 4, 2 to 6, 3 to 6, etc., and individual numerical values ​​within that range, for example, 1, 2, 2.7, 3, 4, 5, 5.3, and 6. This applies regardless of the breadth of the range. Unless expressly stated to the contrary, the disclosed ranges include the endpoints of the range.

[0051] Without being bound by any particular theory, it is found that the embodiments provided herein demonstrate that the Spring Viremia of Carp virus G protein can be used to pseudotype a virus and transduce cells when the virus contains a targeting moiety. The provided Spring Viremia of Carp virus G protein can, in some embodiments, be used to transduce target cells and deliver heterologous molecules to the target cells.

[0052] In some embodiments, a carp spring viremia virus G protein is provided comprising SEQ ID NO: 1. SEQ ID NO: 1 is the full-length protein, and SEQ ID NO: 2 is the extracellular domain of the carp spring viremia virus G protein with the N-terminal signal peptide removed. Thus, in some embodiments, the protein comprises the amino acid sequence of SEQ ID NO: 2.

[0053] The Carp Spring Viremia Virus G protein can be used to pseudotype viruses, such as, but not limited to, lentiviruses. Thus, in some embodiments, a viral particle is provided comprising the Carp Spring Viremia Virus G protein described herein. In some embodiments, the viral particle comprises a Carp Spring Viremia Virus G protein comprising SEQ ID NO:1 or SEQ ID NO:2, or a sequence that is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO:1 or SEQ ID NO:2. In some embodiments, the viral particle comprises a Carp Spring Viremia Virus G protein comprising an amino acid sequence that is at least 80% identical to SEQ ID NO:1 or SEQ ID NO:2. In some embodiments, the viral particle comprises a Carp Spring Viremia Virus G protein comprising an amino acid sequence having at least 85% identity to SEQ ID NO:1 or SEQ ID NO:2. In some embodiments, the viral particle comprises a Carp Spring Viremia Virus G protein comprising an amino acid sequence having at least 90% identity to SEQ ID NO:1 or SEQ ID NO:2. In some embodiments, the viral particle comprises a Carp Spring Viremia Virus G protein comprising an amino acid sequence having at least 95% identity to SEQ ID NO:1 or SEQ ID NO:2. In some embodiments, the viral particle comprises a Carp Spring Viremia Virus G protein comprising an amino acid sequence having at least 98% identity to SEQ ID NO:1 or SEQ ID NO:2. In some embodiments, the viral particle comprises a Carp Spring Viremia Virus G protein comprising the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2.

[0054] In some embodiments, the viral particle comprises a targeting moiety. The targeting moiety can be used to target viral particles comprising the Carp Spring Viremia Virus G protein to cells expressing a target to which the targeting moiety binds. In some embodiments, the targeting moiety is an antibody, an scFv antibody, an antigen-binding domain, ankyrin repeats (e.g., DARPIN), a VHH domain antibody, a nanobody, a single-domain antibody, an FN3 domain, or any combination thereof. The targeting moiety can bind to the viral surface via any suitable polypeptide sequence. In some embodiments, the targeting moiety is attached to the viral surface via a polypeptide stalk. In some embodiments, the polypeptide stalk comprises a transmembrane domain. In some embodiments, the transmembrane domain comprises a CD8 and / or CD28 transmembrane domain. In some embodiments, the targeting moiety binds to the viral surface via an IgG Fc stalk. In some embodiments, the IgG Fc stalk comprises a transmembrane domain. In some embodiments, the transmembrane domain comprises a CD8 and / or CD28 transmembrane domain. In some embodiments, the targeting moiety is attached (fused or linked) to the envelope glycoprotein G or H of a Paramyxoviridae virus, such as a Morbillivirus, such as measles virus, or a Henipavirus, such as Nipah virus, Cedar virus, or Hendra virus. In some embodiments, the targeting moiety may be conjugated (fused or linked) to a glycoprotein of a Rhabdoviridae virus, such as New Jersey vesicular stomatitis virus, vesicular stomatitis Indiana virus, vesicular stomatitis Alagoas virus, vesicular stomatitis Maraba virus, vesicular stomatitis Carajas virus, parainfluenza virus, Fall armyworm rhabdovirus isolate Sf G, Drosophila obscurus sigma virus 10A, Wuhan insect virus 7, Perch virus, or Spring viremia of carp virus. In some embodiments, the Spring viremia of carp virus protein is Spring viremia of carp virus G protein, as provided herein.In some embodiments, the targeting moiety is conjugated to a glycoprotein of a Filoviridae virus, such as Ebola virus, or a glycoprotein of an Arenaviridae virus, such as Machupo virus.

[0055] In some embodiments, the targeting moiety is selected from the group including, but not limited to, an scFv, an antigen-binding domain, a VHH, a DARPin, an adnectin, an affibody, an affilin, an affimer, an affitin, an alphabody, an anticalin, an aptamer, an armadillo repeat protein-based scaffold, an atrimer, an avimer, a fynomer, a knottin, a Kunitz domain peptide, a monobody, a nanophytin, or any combination thereof. In some embodiments, the target cell is an scFv. In some embodiments, the targeting moiety is a single-domain antibody. In some embodiments, the targeting moiety is a VHH.

[0056] In some embodiments, the targeting moiety is selected from the group consisting of moieties that bind to stem cell factor protein (SCF, KIT ligand, KL, or steel factor), or cKit (CD117), CD4, CD8, CD3, CD5, CD6, CD7, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, CXCR3, CD39, CD73, CTLA-4, GITR, LAG-3, LRRC32, Neurophili-1, and CX3CR1.

[0057] In some embodiments, the targeting moiety is selected from the group consisting of CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed on acute leukemia or lymphoma but not on hematopoietic progenitor cells, a glycosylated CD43 epitope expressed on non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin l8.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also known as CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), mutant elongation factor 2 (ELF2M), ephrin B2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSH) R), Fos-related antigen 1, fucosyl-GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(ll)Cer), ganglioside GM3 (aNeu5Ac(2-3)bDClalp(l-4)bDGlcp(ll)Cer), GD3, GFR alpha 4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide moiety of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV-1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer-testis antigen 1 (MAD-CT-1), melanoma cancer-testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface-associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin-4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), and O-acetylglucosaminyltransferase V (O-acetylglucosaminyltransferase V). Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta-specific 1 (PLAC1), platelet-derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin-binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate-specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, kidney ubiquitous 1 (RU1), kidney ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF-beta R2, antigen recognized by TNT antibodies, thyroid-stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn In some embodiments, the targeting moiety binds to CD7, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B-cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7-related (TEM7R), tumor protein p53 (p53), tumor-associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase-related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1). In some embodiments, the targeting moiety binds to CD7. In some embodiments, the targeting moiety binds to CD8.

[0058] In some embodiments, the targeting moiety binds to a target present on a cell, such as an immune cell. In some embodiments, the cell is a T cell, a B cell, a NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell, or an immune cell, such as, but not limited to, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD20+ cancer cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, an NKG2D+ natural killer cell, a SLC1A3+ astrocyte, or a SLC7A10+ adipocyte. In some embodiments, the cell is a T cell. In some embodiments, the cell is a B cell. In some embodiments, the cells are CD7+ T cells and / or CD8+ T cells.

[0059] In some embodiments, the targeting moiety (polypeptide) is capable of binding to CD7.

[0060] In some embodiments, the polypeptide binds to CD7. In some embodiments, the polypeptide that binds to CD7 is an antibody that binds to non-human primate CD7. In some embodiments, the polypeptide that binds to CD7 is an antibody that binds to human CD7. The sequence of human CD7 (UniProtKB P09564) is as follows (SEQ ID NO: 8): MAGPPRLLLLPLLLALARGLPGALAAQEVQQSPHCTTVPVGASVNITCSTSGGLRGIYLRQLGPQPQDIIYYEDGVVPTTDRRFRGRIDFSGSQDNLTITMHRLQLSDTGTYTCQAITEVNVYGSGTLVLVTEEQSQGWHRCSDAPPRASALPAPPTGSALPDPQTASALPDPPAASALPAALAVISFLLGLGLGVACVLARTQIKKLCSWRDKNSAACVVYEDMSHSRCNTLSSPNQYQ (SEQ ID NO: 8)

[0061] In some embodiments, the CD7 antibody comprises an Fc region. The Fc region can bind to the heavy or light chain of the antibody. The Fc region can be directly fused to the heavy or light chain of the antibody, or indirectly fused to the heavy or light chain of the antibody via, for example, a peptide linker provided herein. In some embodiments, the Fc region is an IgG Fc. In some embodiments, the IgG is selected from IgG1, IgG2, IgG3, or IgG4. In some embodiments, the IgG Fc is an IgG1 Fc. In some embodiments, the antibody comprises the Fc constant region of SEQ ID NO: 9, as set forth below. ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK (SEQ ID NO: 9)

[0062] In some embodiments, the IgG fc is an IgG2 Fc. In some embodiments, the antibody comprises the Fc constant region of SEQ ID NO: 10, as set forth below. STKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYTCNVDHKPSNTKVDKTVERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK (SEQ ID NO: 10)

[0063] In some embodiments, the IgG fc is an IgG4 Fc. In some embodiments, the antibody comprises the Fc constant region of SEQ ID NO: 11, as set forth below. STKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK (SEQ ID NO: 11)

[0064] In some embodiments, the IgG Fc comprises an amino acid sequence having at least 80% identity to SEQ ID NO:9, SEQ ID NO:10, or SEQ ID NO:11. In some embodiments, the IgG Fc comprises an amino acid sequence having at least 85% identity to SEQ ID NO:9, SEQ ID NO:10, or SEQ ID NO:11. In some embodiments, the IgG Fc comprises an amino acid sequence having at least 90% identity to SEQ ID NO:9, SEQ ID NO:10, or SEQ ID NO:11. In some embodiments, the IgG Fc comprises an amino acid sequence having at least 95% identity to SEQ ID NO:9, SEQ ID NO:10, or SEQ ID NO:11. In some embodiments, the IgG Fc comprises an amino acid sequence having at least 98% identity to SEQ ID NO:9, SEQ ID NO:10, or SEQ ID NO:11. In some embodiments, the IgG Fc comprises the amino acid sequence of SEQ ID NO:9, SEQ ID NO:10, or SEQ ID NO:11.

[0065] In some embodiments, provided herein are polypeptides (e.g., CD7-binding polypeptides). In some embodiments, provided herein are antibodies (e.g., anti-CD7 antibodies). In some embodiments, the antibody is a recombinant antibody that binds to CD7. In some embodiments, the CD7 protein is a human CD7 protein. In some embodiments, the CD7 protein is a non-human CD7 protein (e.g., mouse, rat, pig, dog, non-human primate). As used herein, the term "recombinant antibody" refers to a non-naturally occurring antibody. In some embodiments, the term "recombinant antibody" refers to an antibody that is not isolated from a human subject.

[0066] In some embodiments, the CD7 antibody does not comprise an Fc region. In some embodiments, the CD7 antibody comprises a polypeptide stalk as described herein. In some embodiments, the CD7 antibody comprises a polypeptide stalk comprising a transmembrane domain as described herein.

[0067] In some embodiments, an antibody or antigen-binding fragment thereof is provided, wherein the antibody or antibody fragment comprises a peptide selected from the table below showing the CDRs according to Chothia numbering. [Table 1]

[0068] In some embodiments, an antibody or antigen-binding fragment thereof is provided, wherein the antibody or antibody fragment comprises a peptide selected from the table below showing the CDRs based on Kabat numbering. [Table 2]

[0069] In some embodiments, an antibody or antigen-binding fragment thereof is provided, wherein the antibody or antibody fragment comprises a peptide selected from the table below showing the CDRs according to IMGT numbering. [Table 3]

[0070] In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy or light chain CDR provided in the table above. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy or light chain CDR provided in the table above and binds to non-human primate CD7. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy or light chain CDR provided in the table above and binds to human CD7. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having a sequence selected from SEQ ID NOs: 15-17. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having the sequence of SEQ ID NO: 15. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having the sequence of SEQ ID NO: 16. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having the sequence of SEQ ID NO: 17. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having a sequence selected from SEQ ID NOs: 12-14. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having the sequence of SEQ ID NO: 12. In some embodiments, the polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having the sequence of SEQ ID NO: 13. In some embodiments, the polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having the sequence of SEQ ID NO: 14. The CDRs referenced in embodiments throughout this specification are interchangeable with CDRs characterized in different formats, such as Kabat and IMGT.

[0071] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a light chain variable region having LCDR1, LCDR2 and LCDR3, wherein LCDR1 has the sequence of SEQ ID NO: 15, LCDR2 has the sequence of SEQ ID NO: 16 and LCDR3 has the sequence of SEQ ID NO: 17.

[0072] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a light chain variable region having LCDR1, LCDR2 and LCDR3, wherein LCDR1 has the sequence of SEQ ID NO: 23, LCDR2 has the sequence of YA, and LCDR3 has the sequence of SEQ ID NO: 17.

[0073] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a heavy chain variable region having HCDR1, HCDR2 and HCDR3, wherein HCDR1 has the sequence of SEQ ID NO: 12, HCDR2 has the sequence of SEQ ID NO: 13 and HCDR3 has the sequence of SEQ ID NO: 14.

[0074] In some embodiments, the polypeptide, antibody or antigen-binding fragment thereof comprises a heavy chain variable region having HCDR1, HCDR2 and HCDR3, wherein HCDR1 has the sequence of SEQ ID NO: 18, HCDR2 has the sequence of SEQ ID NO: 19 and HCDR3 has the sequence of SEQ ID NO: 14.

[0075] In some embodiments, the polypeptide, antibody or antigen-binding fragment thereof comprises a heavy chain variable region having HCDR1, HCDR2 and HCDR3, wherein HCDR1 has the sequence of SEQ ID NO: 20, HCDR2 has the sequence of SEQ ID NO: 21 and HCDR3 has the sequence of SEQ ID NO: 22.

[0076] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises (i) a light chain having any one of the above combinations of LCDR1, LCDR2 and LCDR3 sequences, and (ii) a heavy chain having any one of the above combinations of HCDR1, HCDR2 and HCDR3 sequences.

[0077] Different CDR motifs can be combined in any combination, including those not shown in the table above. For example, the following embodiments are provided as non-limiting examples of such combinations.

[0078] In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises: (i) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 15, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 16, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 17; and (ii) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 12, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 13, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 14, or a variant of any of the foregoing.

[0079] In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises: (i) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 15, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 16, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 17; and (ii) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 18, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 19, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 14, or any variant thereof.

[0080] In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises: (i) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 23, the light chain CDR2 has the amino acid sequence of YA, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 17; and (ii) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 20, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 21, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 22, or any variant of the foregoing.

[0081] In some embodiments, the light chain variable region CDR1 is replaced with any of other light chain CDR1 sequences. In some embodiments, the light chain variable region CDR2 is replaced with any of other light chain CDR2 sequences. In some embodiments, the light chain variable region CDR3 is replaced with any of other light chain CDR3 sequences. In some embodiments, the heavy chain variable region CDR1 is replaced with any of other heavy chain CDR1 sequences. In some embodiments, the heavy chain variable region CDR2 is replaced with any of other heavy chain CDR2 sequences. In some embodiments, the heavy chain variable region CDR3 is replaced with any of other heavy chain CDR3 sequences.

[0082] In some embodiments, the polypeptide comprises a heavy chain variable region peptide having one of the following sequences, or a variant thereof: [Table 4]

[0083] In some embodiments, the polypeptide comprises a light chain variable region peptide having one of the following sequences, or a variant thereof: [Table 5]

[0084] In some embodiments, the polypeptide, antibody or antigen-binding fragment thereof comprises V of SEQ ID NO:24. H In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises a peptide selected from the group consisting of V of SEQ ID NO: 25. L In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises a V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 24 or a variant thereof, LThe peptide comprises the sequence of SEQ ID NO: 25 or a variant thereof. In some embodiments, the polypeptide, antibody or antigen-binding fragment thereof comprises V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 24 or a variant thereof, L The peptide comprises the sequence of SEQ ID NO: 25 or a variant thereof, and the polypeptide, antibody, or antigen-binding fragment thereof binds to non-human primate CD7. In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof binds to V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 24 or a variant thereof, L The peptide comprises the sequence of SEQ ID NO: 25 or a variant thereof, and the polypeptide, antibody, or antigen-binding fragment thereof binds to human CD7. H The peptide comprises the sequence of SEQ ID NO: 24, L The peptide comprises the sequence of SEQ ID NO:25.

[0085] The VH and VL sequences can be in any format, including, but not limited to, an scFv format in which the VH and VL regions are linked by a peptide linker. An example of a peptide linker that can be used to link the various peptides provided herein is (GGGGS) n (SEQ ID NO:26) (each n is independently 1 to 5). In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. In some embodiments, the variable regions are not linked by a peptide linker. In some examples, the polypeptide comprises SEQ ID NO:24 and SEQ ID NO:25.

[0086] In some examples, the VH and VL polypeptides are linked to an Fc region. In some embodiments, the Fc region is as provided herein. In some embodiments, the Fc region comprises the amino acid sequence of SEQ ID NO:9, SEQ ID NO:10, or SEQ ID NO:11 as described herein. As provided herein, the heavy chain can be linked to an Fc region. Non-limiting mutations in the Fc region are provided herein. In some embodiments, the Fc region further comprises a transmembrane domain. Examples of transmembrane domains include, but are not limited to, a CD8 or CD28 ("CD8 / CD28") transmembrane domain. In some embodiments, the Fc region further comprises a CD8 transmembrane domain. In some embodiments, the Fc region further comprises a CD28 transmembrane domain. In some embodiments, an Fc region comprising a transmembrane domain further comprises an Env integration motif. In some embodiments, an Fc region comprising a CD8 / CD28 transmembrane domain further comprises an Env integration motif. In some embodiments, the VH and VL polypeptides provided herein are linked to an Fc region comprising a transmembrane domain. In some embodiments, the VH and VL polypeptides provided herein are linked to an Fc region comprising a CD8 / CD28 transmembrane domain. In some embodiments, the VH and VL polypeptides provided herein are linked to an Fc region comprising a CD8 / CD28 transmembrane domain and an Env integration motif. In some embodiments, the VH and VL polypeptides provided herein linked to an Fc region comprising a CD8 / CD28 transmembrane domain are anchored to the plasma membrane on the surface of a cell. In some embodiments, the cell is an immune cell such as those provided herein. In some embodiments, a VH having the sequence set forth in SEQ ID NO: 24 and a VL having the sequence set forth in SEQ ID NO: 25 are linked to an Fc region comprising a transmembrane domain. In some embodiments, a VH having the sequence set forth in SEQ ID NO: 24 and a VL having the sequence set forth in SEQ ID NO: 25 are linked to an Fc region comprising a CD8 / CD28 transmembrane domain.In some embodiments, a VH having the sequence set forth in SEQ ID NO: 24 and a VL having the sequence set forth in SEQ ID NO: 25 are linked to an Fc region comprising a CD8 / CD28 transmembrane domain and an Env integration motif. In some embodiments, a VH having the sequence set forth in SEQ ID NO: 24 and a VL having the sequence set forth in SEQ ID NO: 25 linked to an Fc region comprising a CD8 / CD28 transmembrane domain are anchored to the plasma membrane on the surface of a cell. In some embodiments, the cell is an immune cell, such as those provided herein.

[0087] In some embodiments, a V comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO:24. H peptides, and V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25. L In some embodiments, the peptide is linked to an Fc region that includes a transmembrane domain. In some embodiments, the peptide is linked to a Vc region that includes a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO:24. H peptides, and V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25. L In some embodiments, the peptide is linked to an Fc region comprising a CD8 / CD28 transmembrane domain. In some embodiments, the peptide comprises a V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO:24. H peptides, and V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25. LThe peptide is linked to an Fc region comprising a CD8 / CD28 transmembrane domain and an Env integration motif. In some embodiments, a V peptide comprising a sequence at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 24 linked to an Fc region comprising a CD8 / CD28 transmembrane domain. H peptides, and V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25. L The peptide is anchored to the plasma membrane on the cell surface. In some embodiments, the cell is an immune cell, such as those provided herein.

[0088] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO:25.

[0089] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that VH Peptides and V L The peptide comprises a light chain CDR having the sequence of SEQ ID NO: 15-17 and / or a heavy chain CDR having the sequence of SEQ ID NO: 12-14. H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V H Peptides and V L The peptide comprises a light chain CDR1 having the sequence of SEQ ID NO: 15, a light chain CDR2 having the sequence of SEQ ID NO: 16, a light chain CDR3 having the sequence of SEQ ID NO: 17, and / or a heavy chain CDR1 having the sequence of SEQ ID NO: 12, a heavy chain CDR2 having the sequence of SEQ ID NO: 13, and a heavy chain CDR3 having the sequence of SEQ ID NO: 14. In some embodiments, the V H or V L The CDRs of the chains are as set forth in the combinations provided herein.

[0090] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V LThe peptide comprises an LCDR1 having the sequence of SEQ ID NO: 15, an LCDR2 having the sequence of SEQ ID NO: 16, and an LCDR3 having the sequence of SEQ ID NO: 17, and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO:12, an HCDR2 having the sequence of SEQ ID NO:13, and an HCDR3 having the sequence of SEQ ID NO:14.

[0091] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 15 (wherein LCDR1 comprises at most one conservative amino acid substitution), an LCDR2 having the sequence of SEQ ID NO: 16 (wherein LCDR2 comprises at most one conservative amino acid substitution), an LCDR3 having the sequence of SEQ ID NO: 17 (wherein LCDR3 comprises at most one conservative amino acid substitution), and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO: 12 (wherein HCDR1 comprises at most one conservative amino acid substitution), an HCDR2 having the sequence of SEQ ID NO: 13 (wherein HCDR2 comprises at most one conservative amino acid substitution), and an HCDR3 having the sequence of SEQ ID NO: 14 (wherein HCDR3 comprises at most one conservative amino acid substitution).

[0092] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V HThe peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V H Peptides and V L The peptide comprises a light chain CDR1 having the sequence of SEQ ID NO: 15, a light chain CDR2 having the sequence of SEQ ID NO: 16, a light chain CDR1 having the sequence of SEQ ID NO: 17, and / or a heavy chain CDR1 having the sequence of SEQ ID NO: 18, a heavy chain CDR2 having the sequence of SEQ ID NO: 19, and a heavy chain CDR3 having the sequence of SEQ ID NO: 14. In some embodiments, V H or V L The CDRs of the chains are as set forth in the combinations provided herein.

[0093] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 15, an LCDR2 having the sequence of SEQ ID NO: 16, and an LCDR3 having the sequence of SEQ ID NO: 17, and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO:18, an HCDR2 having the sequence of SEQ ID NO:19, and an HCDR3 having the sequence of SEQ ID NO:14.

[0094] In some embodiments, the polypeptide is VH Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 15 (wherein LCDR1 comprises at most one conservative amino acid substitution), an LCDR2 having the sequence of SEQ ID NO: 16 (wherein LCDR2 comprises at most one conservative amino acid substitution), an LCDR3 having the sequence of SEQ ID NO: 17 (wherein LCDR3 comprises at most one conservative amino acid substitution), and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO: 18 (wherein HCDR1 comprises at most one conservative amino acid substitution), an HCDR2 having the sequence of SEQ ID NO: 19 (wherein HCDR2 comprises at most one conservative amino acid substitution), and an HCDR3 having the sequence of SEQ ID NO: 14 (wherein HCDR3 comprises at most one conservative amino acid substitution).

[0095] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V H Peptides and V LThe peptide comprises a light chain CDR1 having the sequence of SEQ ID NO: 23, a light chain CDR2 having the sequence of YA, a light chain CDR1 having the sequence of SEQ ID NO: 17, and / or a heavy chain CDR1 having the sequence of SEQ ID NO: 20, a heavy chain CDR2 having the sequence of SEQ ID NO: 21, and a heavy chain CDR3 having the sequence of SEQ ID NO: 22. In some embodiments, V H or V L The CDRs of the chains are as set forth in the combinations provided herein.

[0096] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 23, an LCDR2 having the sequence of YA, and an LCDR3 having the sequence of SEQ ID NO: 17, and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO:20, an HCDR2 having the sequence of SEQ ID NO:21, and an HCDR3 having the sequence of SEQ ID NO:22.

[0097] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 24, and LThe peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 25, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 23 (wherein LCDR1 contains up to one conservative amino acid substitution), an LCDR2 having the sequence of YA (wherein LCDR2 contains up to one conservative amino acid substitution), an LCDR3 having the sequence of SEQ ID NO: 17 (wherein LCDR3 contains up to one conservative amino acid substitution), and a V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO: 20 (wherein HCDR1 comprises at most one conservative amino acid substitution), an HCDR2 having the sequence of SEQ ID NO: 21 (wherein HCDR2 comprises at most one conservative amino acid substitution), and an HCDR3 having the sequence of SEQ ID NO: 22 (wherein HCDR3 comprises at most one conservative amino acid substitution).

[0098] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 24, L The peptide comprises the sequence of SEQ ID NO:25.

[0099] In some embodiments, the polypeptides provided herein bind to non-human primate CD7. In some embodiments, the polypeptides provided herein bind to human CD7.

[0100] As provided herein, the different polypeptides (V H or V L ) can be linked by a peptide linker or can be linked to a contiguous sequence without a peptide linker. In some embodiments, the peptide linker is (GGGGS) n(SEQ ID NO: 26), wherein each n is independently 1 to 5. In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. The binding peptide format comprises V H -ZV L or V L -ZV H and Z is a peptide linker. In some embodiments, Z is (GGGGS) n (SEQ ID NO: 26), and each n is independently 1 to 5.

[0101] In some embodiments, V L -ZV H The polypeptide comprising a connecting peptide of the formula: comprises a heavy chain variable region set forth in SEQ ID NO: 24 linked to a light chain variable region set forth in SEQ ID NO: 25 via the linker sequence GGGGSGGGGSGGGSGGGS (SEQ ID NO: 27). In some embodiments, the V H V connected to L The polypeptide comprising has the sequence set forth below. DILLTQSPAILSVSPGERVSFSCRASQSIGTSIHWYQQRTNDSPRLLIKYASESISGIPSRFSGSGSGTDFTLSINSVESEDIADYYCQQSNSWPTTFGGGTKLEIKRGGGGSGGGGSGGGGSGGGGSQVQLQQPGAELVKPGASVKLSCKASGYPFTSYWIHWVKQRPGRGLEWLGRIDPNSGDTKYNEKFKNKATLTVDKSSTTAYMQLSSLTSEDSAVYYCARSPYYSNDNSMDYWGQGTSVTVSS (SEQ ID NO: 28)

[0102] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 28. In some embodiments, the polypeptide comprises a sequence that is at least 90% identical to the sequence of SEQ ID NO: 28. In some embodiments, the polypeptide comprises a sequence that is at least 95% identical to the sequence of SEQ ID NO: 28. In some embodiments, the polypeptide comprises a sequence that is at least 99% identical to the sequence of SEQ ID NO: 28. In some embodiments, the polypeptide set forth in SEQ ID NO: 28 is an antibody or antigen-binding fragment thereof. In some embodiments, the antibody is an anti-CD7 antibody.

[0103] In some embodiments, V H -ZV L The polypeptide comprising a connecting peptide of the formula: comprises a light chain variable region set forth in SEQ ID NO: 25 linked to a heavy chain variable region set forth in SEQ ID NO: 24 via the linker sequence GGGGSGGGGSGGGSGGGS (SEQ ID NO: 27). In some embodiments, the V L V connected to H The polypeptide comprising has the sequence set forth below. QVQLQQPGAELVKPGASVKLSCKASGYPFTSYWIHWVKQRPGRGLEWLGRIDPNSGDTKYNEKFKNKATLTVDKSSTTAYMQLSSLTSEDSAVYYCARSPYYSNDNSMDYWGQGTSVTVSSGGGGSGGGGSGGGGSGGGGSDILLTQSPAILSVSPGERVSFSCRASQSIGTSIHWYQQRTNDSPRLLIKYASESISGIPSRFSGSGSGTDFTLSINSVESEDIADYYCQQSNSWPTTFGGGTKLEIKR (SEQ ID NO: 29)

[0104] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 29. In some embodiments, the polypeptide comprises a sequence that is at least 90% identical to the sequence of SEQ ID NO: 29. In some embodiments, the polypeptide comprises a sequence that is at least 95% identical to the sequence of SEQ ID NO: 29. In some embodiments, the polypeptide comprises a sequence that is at least 99% identical to the sequence of SEQ ID NO: 29. In some embodiments, the polypeptide set forth in SEQ ID NO: 29 is an antibody or antigen-binding fragment thereof. In some embodiments, the antibody is an anti-CD7 antibody. In some embodiments, the anti-CD7 antibody binds to non-human primate CD7. In some embodiments, the anti-CD7 antibody binds to human CD7.

[0105] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 28, and comprises an Fc region such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 28, and comprises an Fc region such as those provided herein, and a transmembrane domain such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 28, and comprises an Fc region such as provided herein, and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 28, and comprises an Fc region such as provided herein, a transmembrane domain such as provided herein, and an Env integration motif.

[0106] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 29, and comprises an Fc region such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 29, and comprises an Fc region such as those provided herein, and a transmembrane domain such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 29, and comprises an Fc region such as provided herein, and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 29, and comprises an Fc region such as provided herein, a transmembrane domain such as provided herein, and an Env integration motif.

[0107] As provided herein, polypeptides, antibodies or antigen-binding fragments thereof may be sequence variants.

[0108] The polypeptide or antibody sequence can be modified to generate a human IgG antibody. The sequence provided herein can be modified to generate other types of antibodies. The CDR can also be linked to other antibodies, proteins, or molecules to generate antibody fragments that bind to CD7.

[0109] In some embodiments, a polypeptide or antibody provided herein is a targeting moiety on the surface of a modified viral particle. In some embodiments, the targeting moiety enables binding to a target cell. In some embodiments, the targeting moiety is a CD7-binding moiety, such as a polypeptide or antibody provided herein. In some embodiments, the targeting moiety comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO:28. In some embodiments, the targeting moiety comprises a sequence that is at least 90% identical to the sequence of SEQ ID NO:28. In some embodiments, the targeting moiety comprises a sequence that is at least 95% identical to the sequence of SEQ ID NO:28. In some embodiments, the targeting moiety comprises a sequence that is at least 99% identical to the sequence of SEQ ID NO:28. In some embodiments, the targeting moiety set forth in SEQ ID NO:28 is an antibody or antigen-binding fragment thereof. In some embodiments, the targeting moiety is an anti-CD7 antibody.

[0110] In some embodiments, a polypeptide or antibody provided herein is a targeting moiety on the surface of a modified virus particle. In some embodiments, the modified virus particle is a pseudotyped virus-like particle. In some embodiments, the targeting moiety enables binding to a target cell. In some embodiments, the targeting moiety is a CD7-binding moiety, such as a polypeptide or antibody provided herein. In some embodiments, the targeting moiety comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO:29. In some embodiments, the targeting moiety comprises a sequence that is at least 90% identical to the sequence of SEQ ID NO:29. In some embodiments, the targeting moiety comprises a sequence that is at least 95% identical to the sequence of SEQ ID NO:29. In some embodiments, the targeting moiety comprises a sequence that is at least 99% identical to the sequence of SEQ ID NO:29. In some embodiments, the targeting moiety comprises the sequence set forth in SEQ ID NO:29. In some embodiments, the targeting moiety set forth in SEQ ID NO: 29 is an antibody or antigen-binding fragment thereof. In some embodiments, the targeting moiety is an anti-CD7 antibody. In some embodiments, the anti-CD7 antibody binds to non-human primate CD7. In some embodiments, the anti-CD7 antibody binds to human CD7.

[0111] In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 28 and comprises an Fc region, such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 28 and comprises an Fc region, such as those provided herein, and a transmembrane domain, such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 28 and comprises an Fc region, such as those provided herein, and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 28 and comprises an Fc region, such as those provided herein, a transmembrane domain, such as those provided herein, and an Env integration motif.

[0112] In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO:29 and comprises an Fc region such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO:29 and comprises an Fc region such as those provided herein and a transmembrane domain such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO:29 and comprises an Fc region such as those provided herein and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO:29 and comprises an Fc region such as those provided herein, a transmembrane domain such as those provided herein, and an Env integration motif.

[0113] In some embodiments, the targeting moiety (polypeptide) is capable of binding to CD8.

[0114] In some embodiments, the polypeptide binds to CD8. In some embodiments, the polypeptide binds to CD8-alpha. In some embodiments, the polypeptide binds to CD8-beta. In some embodiments, the polypeptide binds to a CD8 heterodimer. In some embodiments, the CD8 heterodimer comprises a CD8-alpha subunit and a CD8-beta subunit. In some embodiments, the polypeptide binds to a CD8-alpha homodimer. In some embodiments, the polypeptide that binds to CD8 is an antibody that binds to non-human primate CD8. In some embodiments, the antibody that binds to non-human primate CD8 is an antibody that binds to non-human primate CD8-alpha. In some embodiments, the antibody that binds to non-human primate CD8 is an antibody that binds to non-human primate CD8-beta. In some embodiments, the antibody that binds to non-human primate CD8 is an antibody that binds to non-human primate CD8-alpha homodimer. In some embodiments, the antibody that binds to non-human primate CD8 is an antibody that binds to non-human primate CD8 heterodimer. In some embodiments, the polypeptide that binds to CD8 is an antibody that binds to human CD8. In some embodiments, the antibody that binds to human CD8 is an antibody that binds to human CD8-alpha. In some embodiments, the antibody that binds to human CD8 is an antibody that binds to human CD8-beta. In some embodiments, the antibody that binds to human CD8 is an antibody that binds to human CD8-alpha homodimer. In some embodiments, the antibody that binds to human CD8 is an antibody that binds to human CD8 heterodimer. The sequence of human CD8-alpha (UniProtKB Q8TAW8) is as follows (SEQ ID NO: 30): MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGCYFCSALSNSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV (SEQ ID NO: 30)

[0115] The sequence of human CD8-beta (UniProtKB Q8TD28) is as follows (SEQ ID NO: 31): MRPRLWLLLAAQLTVLHGNSVLQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLRFMKQLYK (SEQ ID NO: 31)

[0116] In some embodiments, the CD8 to which the polypeptide binds is expressed on the surface of a cell. In some embodiments, the cell is an immune cell. In some embodiments, the immune cell is a CD7+ T cell, a CD4+ T cell, a CD8+ T cell, a NK cell, an alpha beta T cell, a gamma delta T cell, a lymphoid progenitor cell, a hematopoietic stem cell, a myeloid cell, a monocyte, a macrophage, a central memory T cell, an effector memory T cell, a stem cell-like memory T cell, a naive T cell, an activated T cell, a regulatory T cell (TReg), a terminally differentiated effector memory T cell (TEMRA), a resident memory T cell (TRM), or a CD8+CCR7+ T cell. In some embodiments, the cell is a CD8+ T cell. In some embodiments, the cell is a CD8+ cell.

[0117] In some embodiments, the antibody comprises an Fc region. The Fc region can bind to the heavy or light chain of the antibody. In some embodiments, the Fc region is an IgG Fc. In some embodiments, the IgG is selected from IgG1, IgG2, IgG3, or IgG4. In some embodiments, the IgG Fc is an IgG1 Fc and comprises the amino acid sequence of SEQ ID NO: 9 provided herein or a variant thereof. In some embodiments, the IgG Fc is an IgG2 Fc and comprises the amino acid sequence of SEQ ID NO: 10 provided herein or a variant thereof. In some embodiments, the IgG Fc is an IgG4 Fc and comprises the amino acid sequence of SEQ ID NO: 11 provided herein or a variant thereof.

[0118] In some embodiments, provided herein are polypeptides (e.g., CD8-binding polypeptides). In some embodiments, provided herein are antibodies (e.g., anti-CD8 antibodies). In some embodiments, the antibody is a recombinant antibody that binds to CD8. In some embodiments, the CD8 protein is a human CD8 protein. In some embodiments, the CD8 protein is a non-human CD8 protein (e.g., mouse, rat, pig, dog, non-human primate). As used herein, the term "recombinant antibody" refers to a non-naturally occurring antibody. In some embodiments, the term "recombinant antibody" refers to an antibody that is not isolated from a human subject.

[0119] In some embodiments, an antibody or antigen-binding fragment thereof is provided, wherein the antibody or antibody fragment comprises a peptide selected from the table below showing the CDRs according to Chothia numbering. [Table 6]

[0120] In some embodiments, an antibody or antigen-binding fragment thereof is provided, wherein the antibody or antibody fragment comprises a peptide selected from the table below showing the CDRs based on Kabat numbering. [Table 7]

[0121] In some embodiments, an antibody or antigen-binding fragment thereof is provided, wherein the antibody or antibody fragment comprises a peptide selected from the table below showing the CDRs according to IMGT numbering. [Table 8]

[0122] In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy or light chain CDR provided in the table above. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy or light chain CDR provided in the table above and binds to non-human primate CD8. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy or light chain CDR provided in the table above and binds to human CD8. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having a sequence selected from SEQ ID NOs: 35-37. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having the sequence of SEQ ID NO: 35. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having the sequence of SEQ ID NO: 36. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a light chain CDR having the sequence of SEQ ID NO: 37. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having a sequence selected from SEQ ID NOs: 32-34. In some embodiments, a polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having the sequence of SEQ ID NO: 32. In some embodiments, the polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having the sequence of SEQ ID NO: 33. In some embodiments, the polypeptide, antibody, or antibody-binding fragment thereof comprises a heavy chain CDR having the sequence of SEQ ID NO: 34. The CDRs referenced in embodiments throughout this specification are interchangeable with CDRs characterized in different formats, such as Kabat and IMGT.

[0123] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a light chain variable region having LCDR1, LCDR2 and LCDR3, wherein LCDR1 has the sequence of SEQ ID NO: 35, LCDR2 has the sequence of SEQ ID NO: 36 and LCDR3 has the sequence of SEQ ID NO: 37.

[0124] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a light chain variable region having LCDR1, LCDR2 and LCDR3, wherein LCDR1 has the sequence of SEQ ID NO: 43, LCDR2 has the sequence of LA, and LCDR3 has the sequence of SEQ ID NO: 37.

[0125] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a heavy chain variable region having HCDR1, HCDR2 and HCDR3, wherein HCDR1 has the sequence of SEQ ID NO: 32, HCDR2 has the sequence of SEQ ID NO: 33, and LCDR3 has the sequence of SEQ ID NO: 34.

[0126] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a heavy chain variable region having HCDR1, HCDR2 and HCDR3, wherein HCDR1 has the sequence of SEQ ID NO: 38, HCDR2 has the sequence of SEQ ID NO: 39, and LCDR3 has the sequence of SEQ ID NO: 34.

[0127] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises a heavy chain variable region having HCDR1, HCDR2 and HCDR3, wherein HCDR1 has the sequence of SEQ ID NO: 40, HCDR2 has the sequence of SEQ ID NO: 41 and LCDR3 has the sequence of SEQ ID NO: 42.

[0128] In some embodiments, the polypeptide, antibody or antibody-binding fragment thereof comprises (i) a light chain having any one of the above combinations of LCDR1, LCDR2 and LCDR3 sequences, and (ii) a heavy chain having any one of the above combinations of HCDR1, HCDR2 and HCDR3 sequences.

[0129] Different CDR motifs can be combined in any combination, including those not shown in the table above. For example, the following embodiments are provided as non-limiting examples of such combinations.

[0130] In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises: (i) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 35, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 36, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 37; and (ii) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 32, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 33, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 34, or a variant of any of the foregoing.

[0131] In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises: (i) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 35, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 36, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 37; and (ii) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 38, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 39, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 34, or any variant of the foregoing.

[0132] In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises: (i) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 43, the light chain CDR2 has the amino acid sequence of LA, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 37; and (ii) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 40, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 41, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 42, or any variant of the foregoing.

[0133] In some embodiments, the light chain variable region CDR1 is replaced with any of other light chain CDR1 sequences. In some embodiments, the light chain variable region CDR2 is replaced with any of other light chain CDR2 sequences. In some embodiments, the light chain variable region CDR3 is replaced with any of other light chain CDR3 sequences. In some embodiments, the heavy chain variable region CDR1 is replaced with any of other heavy chain CDR1 sequences. In some embodiments, the heavy chain variable region CDR2 is replaced with any of other heavy chain CDR2 sequences. In some embodiments, the heavy chain variable region CDR3 is replaced with any of other heavy chain CDR3 sequences.

[0134] In some embodiments, the polypeptide comprises a heavy chain variable region peptide having one of the following sequences, or a variant thereof: [Table 9]

[0135] In some embodiments, the polypeptide comprises a light chain variable region peptide having one of the following sequences, or a variant thereof: [Table 10]

[0136] In some embodiments, the polypeptide, antibody or antigen-binding fragment thereof comprises V of SEQ ID NO:44. H In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises a peptide selected from the group consisting of V of SEQ ID NO: 45. L In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises a V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 44 or a variant thereof, LThe peptide comprises the sequence of SEQ ID NO: 45 or a variant thereof. In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof comprises V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 44 or a variant thereof, L The peptide comprises the sequence of SEQ ID NO: 45 or a variant thereof, and the polypeptide, antibody, or antigen-binding fragment thereof binds to non-human primate CD8. In some embodiments, the polypeptide, antibody, or antigen-binding fragment thereof binds to V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 44 or a variant thereof, L The peptide comprises the sequence of SEQ ID NO: 45 or a variant thereof, and the polypeptide, antibody or antigen-binding fragment thereof binds to human CD8. H The peptide comprises the sequence of SEQ ID NO: 44, L The peptide comprises the sequence of SEQ ID NO:45.

[0137] The VH and VL sequences can be in any format, including, but not limited to, an scFv format in which the VH and VL regions are linked by a peptide linker. An example of a peptide linker that can be used to link the various peptides provided herein is (GGGGS) n (SEQ ID NO:26) (each n is independently 1 to 5). In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. In some embodiments, the variable regions are not linked by a peptide linker. In some examples, the polypeptide comprises SEQ ID NO:44 and SEQ ID NO:45.

[0138] In some examples, the VH and VL polypeptides are linked to an Fc region. In some embodiments, the Fc region is as provided herein. As provided herein, the heavy chain can be linked to an Fc region. Non-limiting mutations in the Fc region are provided herein. In some embodiments, the Fc region further comprises a transmembrane domain. Examples of transmembrane domains include, but are not limited to, a CD8 / CD28 transmembrane domain. In some embodiments, the Fc region further comprises a CD8 or CD28 ("CD8 / CD28") transmembrane domain. In some embodiments, the Fc region further comprises a CD8 transmembrane domain. In some embodiments, the Fc region further comprises a CD28 transmembrane domain. In some embodiments, an Fc region comprising a transmembrane domain further comprises an Env integration motif. In some embodiments, an Fc region comprising a CD8 / CD28 transmembrane domain further comprises an Env integration motif. In some embodiments, the VH and VL polypeptides provided herein are linked to an Fc region comprising a transmembrane domain. In some embodiments, the VH and VL polypeptides provided herein are linked to an Fc region comprising a CD8 / CD28 transmembrane domain. In some embodiments, the VH and VL polypeptides provided herein are linked to an Fc region comprising a CD8 / CD28 transmembrane domain and an Env integration motif. In some embodiments, the VH and VL polypeptides provided herein linked to an Fc region comprising a CD8 / CD28 transmembrane domain are anchored to the plasma membrane on the surface of a cell. In some embodiments, the cell is an immune cell such as those provided herein. In some embodiments, a VH having the sequence set forth in SEQ ID NO: 44 and a VL having the sequence set forth in SEQ ID NO: 45 are linked to an Fc region comprising a transmembrane domain. In some embodiments, a VH having the sequence set forth in SEQ ID NO: 44 and a VL having the sequence set forth in SEQ ID NO: 45 are linked to an Fc region comprising a CD8 / CD28 transmembrane domain.In some embodiments, a VH having the sequence set forth in SEQ ID NO: 44 and a VL having the sequence set forth in SEQ ID NO: 45 are linked to an Fc region comprising a CD8 / CD28 transmembrane domain and an Env integration motif. In some embodiments, a VH having the sequence set forth in SEQ ID NO: 44 and a VL having the sequence set forth in SEQ ID NO: 45 linked to an Fc region comprising a CD8 / CD28 transmembrane domain are anchored to the plasma membrane on the surface of a cell. In some embodiments, the cell is an immune cell, such as those provided herein.

[0139] In some embodiments, a V comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO:44. H Peptides, V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45 L In some embodiments, the peptide is linked to an Fc region that includes a transmembrane domain. In some embodiments, the peptide is linked to a Vc region that includes a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO:44. H Peptides, V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45 L In some embodiments, the peptide is linked to an Fc region comprising a CD8 / CD28 transmembrane domain. In some embodiments, the peptide comprises a V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO:44. H Peptides, V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45 LThe peptide is linked to an Fc region comprising a CD8 / CD28 transmembrane domain and an Env integration motif. In some embodiments, a V peptide comprising a sequence at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 44 linked to an Fc region comprising a CD8 / CD28 transmembrane domain. H Peptides, V comprising a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45 L The peptide is anchored to the plasma membrane on the cell surface. In some embodiments, the cell is an immune cell, such as those provided herein.

[0140] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO:45.

[0141] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that VH Peptides and V L The peptide comprises a light chain CDR having the sequence of SEQ ID NO: 35-37 and / or a heavy chain CDR having the sequence of SEQ ID NO: 32-34. H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V H Peptides and V L The peptide comprises a light chain CDR1 having the sequence of SEQ ID NO: 35, a light chain CDR2 having the sequence of SEQ ID NO: 36, a light chain CDR3 having the sequence of SEQ ID NO: 37, and / or a heavy chain CDR1 having the sequence of SEQ ID NO: 32, a heavy chain CDR2 having the sequence of SEQ ID NO: 33, and a heavy chain CDR3 having the sequence of SEQ ID NO: 34. In some embodiments, the V H or V L The CDRs of the chains are as set forth in the combinations provided herein.

[0142] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V LThe peptide comprises an LCDR1 having the sequence of SEQ ID NO: 35, an LCDR2 having the sequence of SEQ ID NO: 36, and an LCDR3 having the sequence of SEQ ID NO: 37, and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO:32, an HCDR2 having the sequence of SEQ ID NO:33 and an HCDR3 having the sequence of SEQ ID NO:34.

[0143] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 35 (wherein LCDR1 comprises at most one conservative amino acid substitution), an LCDR2 having the sequence of SEQ ID NO: 36 (wherein LCDR2 comprises at most one conservative amino acid substitution), an LCDR3 having the sequence of SEQ ID NO: 37 (wherein LCDR3 comprises at most one conservative amino acid substitution), and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO: 32 (wherein HCDR1 comprises at most one conservative amino acid substitution), an HCDR2 having the sequence of SEQ ID NO: 33 (wherein HCDR2 comprises at most one conservative amino acid substitution), and an HCDR3 having the sequence of SEQ ID NO: 34 (wherein HCDR3 comprises at most one conservative amino acid substitution).

[0144] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V HThe peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V H Peptides and V L The peptide comprises a light chain CDR1 having the sequence of SEQ ID NO: 35, a light chain CDR2 having the sequence of SEQ ID NO: 36, a light chain CDR3 having the sequence of SEQ ID NO: 37, and / or a heavy chain CDR1 having the sequence of SEQ ID NO: 38, a heavy chain CDR2 having the sequence of SEQ ID NO: 39, and a heavy chain CDR3 having the sequence of SEQ ID NO: 34. In some embodiments, V H or V L The CDRs of the chains are as set forth in the combinations provided herein.

[0145] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 35, an LCDR2 having the sequence of SEQ ID NO: 36, and an LCDR3 having the sequence of SEQ ID NO: 37, and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO: 38, an HCDR2 having the sequence of SEQ ID NO: 39 and an HCDR3 having the sequence of SEQ ID NO: 34.

[0146] In some embodiments, the polypeptide is VH Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 35 (wherein LCDR1 comprises at most one conservative amino acid substitution), an LCDR2 having the sequence of SEQ ID NO: 36 (wherein LCDR2 comprises at most one conservative amino acid substitution), an LCDR3 having the sequence of SEQ ID NO: 37 (wherein LCDR3 comprises at most one conservative amino acid substitution), and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO: 38 (wherein HCDR1 comprises at most one conservative amino acid substitution), an HCDR2 having the sequence of SEQ ID NO: 39 (wherein HCDR2 comprises at most one conservative amino acid substitution), and an HCDR3 having the sequence of SEQ ID NO: 34 (wherein HCDR3 comprises at most one conservative amino acid substitution).

[0147] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V H Peptides and V LThe peptide comprises a light chain CDR1 having the sequence of SEQ ID NO: 43, a light chain CDR2 having the sequence of LA, a light chain CDR3 having the sequence of SEQ ID NO: 37, and / or a heavy chain CDR1 having the sequence of SEQ ID NO: 40, a heavy chain CDR2 having the sequence of SEQ ID NO: 41, and a heavy chain CDR3 having the sequence of SEQ ID NO: 42. In some embodiments, V H or V L The CDRs of the chains are as set forth in the combinations provided herein.

[0148] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and L The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 43, an LCDR2 having the sequence of LA, and an LCDR3 having the sequence of SEQ ID NO: 37, and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO:40, an HCDR2 having the sequence of SEQ ID NO:41 and an HCDR3 having the sequence of SEQ ID NO:42.

[0149] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 44, and LThe peptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 45, with the proviso that V L The peptide comprises an LCDR1 having the sequence of SEQ ID NO: 43 (wherein LCDR1 comprises at most one conservative amino acid substitution), an LCDR2 having the sequence of LA (wherein LCDR2 comprises at most one conservative amino acid substitution), an LCDR3 having the sequence of SEQ ID NO: 37 (wherein LCDR3 comprises at most one conservative amino acid substitution), and V H The peptide comprises an HCDR1 having the sequence of SEQ ID NO: 40, (wherein HCDR1 comprises at most one conservative amino acid substitution), an HCDR2 having the sequence of SEQ ID NO: 41, (wherein HCDR2 comprises at most one conservative amino acid substitution), and an HCDR3 having the sequence of SEQ ID NO: 42, (wherein HCDR3 comprises at most one conservative amino acid substitution).

[0150] In some embodiments, the polypeptide is V H Peptides and V L Contains peptides, V H The peptide comprises the sequence of SEQ ID NO: 44, L The peptide comprises the sequence of SEQ ID NO:45.

[0151] In some embodiments, the polypeptides provided herein bind to non-human primate CD8. In some embodiments, the polypeptides provided herein bind to human CD8.

[0152] As provided herein, the different polypeptides (V H or V L ) can be linked by a peptide linker or can be linked to a contiguous sequence without a peptide linker. In some embodiments, the peptide linker is (GGGGS) n(SEQ ID NO: 26), wherein each n is independently 1 to 5. In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. The binding peptide format comprises V H -ZV L or V L -ZV H and Z is a peptide linker. In some embodiments, Z is (GGGGS) n (SEQ ID NO: 26), and each n is independently 1 to 5.

[0153] In some embodiments, V L -ZV H The polypeptide comprising a connecting peptide of the formula: comprises a heavy chain variable region set forth in SEQ ID NO: 44 linked to a light chain variable region set forth in SEQ ID NO: 45 via the linker sequence GGGGSGGGGSGGGSGGGS (SEQ ID NO: 27). In some embodiments, the polypeptide comprising a connecting peptide of the formula: H V connected to L The polypeptide comprising has the sequence set forth below. NIVLTQSPASLAVSLGQRATISCRASESVDGFGNSFMNWYQQKPGQSPKLLIYLASNLESGVPARFSGSGSRTDFTLTIDPVEADDAATYYCQQNNEDPYTFGGGTKLEIKRGGGGSGGGGSGGGGSGGGGSEVQLQQSGPELVKPGASVKISCKASRYTFTDYNLHWVKLSHEKSLEWIGFIYPYNGGTGYNQKFKNKAKLTVDYSSSTAYMELRSLTSVDAAVYYCARDHRYNEGVSFDYWGQGTTLTVSS (SEQ ID NO: 46)

[0154] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 46. In some embodiments, the polypeptide comprises a sequence that is at least 90% identical to the sequence of SEQ ID NO: 46. In some embodiments, the polypeptide comprises a sequence that is at least 95% identical to the sequence of SEQ ID NO: 46. In some embodiments, the polypeptide comprises a sequence that is at least 99% identical to the sequence of SEQ ID NO: 46. In some embodiments, the polypeptide comprises the sequence set forth in SEQ ID NO: 46. In some embodiments, the polypeptide set forth in SEQ ID NO: 46 is an antibody or antigen-binding fragment thereof. In some embodiments, the antibody is an anti-CD8 antibody.

[0155] In some embodiments, V H -ZV L The polypeptide comprising a connecting peptide of the formula: comprises a light chain variable region set forth in SEQ ID NO: 45 linked to a heavy chain variable region set forth in SEQ ID NO: 44 via the linker sequence GGGGSGGGGSGGGSGGGS (SEQ ID NO: 27). In some embodiments, the polypeptide comprising a connecting peptide of the formula: L V connected to H The polypeptide comprising has the sequence set forth below. EVQLQQSGPELVKPGASVKISCKASRYTFTDYNLHWVKLSHEKSLEWIGFIYPYNGGTGYNQKFKNKAKLTVDYSSSTAYMELRSLTSVDAAVYYCARDHRYNEGVSFDYWGQGTTLTVSSGGGGSGGGGSGGGGSGGGGSNIVLTQSPASLAVSLGQRATISCRASESVDGFGNSFMNWYQQKPGQSPKLLIYLASNLESGVPARFSGSGSRTDFTLTIDPVEADDAATYYCQQNNEDPYTFGGGTKLEIKR (SEQ ID NO: 47)

[0156] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 47. In some embodiments, the polypeptide comprises a sequence that is at least 90% identical to the sequence of SEQ ID NO: 47. In some embodiments, the polypeptide comprises a sequence that is at least 95% identical to the sequence of SEQ ID NO: 47. In some embodiments, the polypeptide comprises a sequence that is at least 99% identical to the sequence of SEQ ID NO: 47. In some embodiments, the polypeptide set forth in SEQ ID NO: 47 is an antibody or antigen-binding fragment thereof. In some embodiments, the antibody is an anti-CD8 antibody. In some embodiments, the anti-CD8 antibody binds to non-human primate CD8. In some embodiments, the anti-CD8 antibody binds to human CD8.

[0157] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 46, and comprises an Fc region such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 46, and comprises an Fc region such as those provided herein, and a transmembrane domain such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 46, and comprises an Fc region such as provided herein, and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 46, and comprises an Fc region such as provided herein, a transmembrane domain such as provided herein, and an Env integration motif.

[0158] In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 47, and comprises an Fc region such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 47, and comprises an Fc region such as those provided herein, and a transmembrane domain such as those provided herein. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 47, and comprises an Fc region such as provided herein, and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to the sequence of SEQ ID NO: 47, and comprises an Fc region such as provided herein, a transmembrane domain such as provided herein, and an Env integration motif.

[0159] As provided herein, polypeptides, antibodies or antigen-binding fragments thereof may be sequence variants.

[0160] The polypeptide or antibody sequence can be modified to generate a human IgG antibody. The sequence provided herein can be modified to generate other types of antibodies. The CDRs can also be linked to other antibodies, proteins, or molecules to generate antibody fragments that bind to CD8.

[0161] In some embodiments, a polypeptide or antibody provided herein is a targeting moiety on the surface of a modified viral particle. In some embodiments, the targeting moiety enables binding to a target cell. In some embodiments, the targeting moiety is a CD8-binding moiety, such as a polypeptide or antibody provided herein. In some embodiments, the targeting moiety comprises a sequence at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 46. In some embodiments, the targeting moiety comprises a sequence at least 90% identical to the sequence of SEQ ID NO: 46. In some embodiments, the targeting moiety comprises a sequence at least 95% identical to the sequence of SEQ ID NO: 46. In some embodiments, the targeting moiety comprises a sequence at least 99% identical to the sequence of SEQ ID NO: 46. In some embodiments, the targeting moiety set forth in SEQ ID NO: 46 is an antibody or antigen-binding fragment thereof. In some embodiments, the targeting moiety is an anti-CD8 antibody.

[0162] In some embodiments, a polypeptide or antibody provided herein is a targeting moiety on the surface of a modified virus particle. In some embodiments, the modified virus particle is a pseudotyped virus-like particle. In some embodiments, the targeting moiety enables binding to a target cell. In some embodiments, the targeting moiety is a CD8-binding moiety, such as a polypeptide or antibody provided herein. In some embodiments, the targeting moiety comprises a sequence that is at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to the sequence of SEQ ID NO: 47. In some embodiments, the targeting moiety comprises a sequence that is at least 90% identical to the sequence of SEQ ID NO: 47. In some embodiments, the targeting moiety comprises a sequence that is at least 95% identical to the sequence of SEQ ID NO: 47. In some embodiments, the targeting moiety comprises a sequence that is at least 99% identical to the sequence of SEQ ID NO: 47. In some embodiments, the targeting moiety comprises the sequence set forth in SEQ ID NO: 47. In some embodiments, the targeting moiety set forth in SEQ ID NO: 47 is an antibody or antigen-binding fragment thereof. In some embodiments, the targeting moiety is an anti-CD8 antibody. In some embodiments, the anti-CD8 antibody binds to non-human primate CD8. In some embodiments, the anti-CD8 antibody binds to human CD8.

[0163] In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 46 and comprises an Fc region such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 46 and comprises an Fc region such as those provided herein and a transmembrane domain such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 46 and comprises an Fc region such as those provided herein and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 46 and comprises an Fc region such as those provided herein, a transmembrane domain such as those provided herein, and an Env integration motif.

[0164] In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 47 and comprises an Fc region such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 47 and comprises an Fc region such as those provided herein and a transmembrane domain such as those provided herein. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 47 and comprises an Fc region such as those provided herein and a CD8 / CD28 transmembrane domain. In some embodiments, the polypeptide comprises a sequence having the sequence set forth in SEQ ID NO: 70 and comprises an Fc region such as those provided herein, a transmembrane domain such as those provided herein, and an Env integration motif.

[0165] In some embodiments, viral particles comprising the carp spring viremia virus G protein and / or targeting moiety provided herein further comprise a gag protein. In some embodiments, the gag protein is a wild-type gag protein rather than a chimeric gag protein. In some embodiments, the gag protein is a chimeric gag protein. In some embodiments, the gag protein is an HIV gag protein. In some embodiments, the chimeric gag protein is an xHIV gag protein. The chimeric gag protein xHIV is described in Uchida et al. J. Virol. October 2009, pp. 9854-9862, the entire contents of which are incorporated herein by reference.

[0166] In some embodiments, the chimeric gag protein comprises SIV and HIV sequences. In some embodiments, the chimeric gag protein comprising SIV and HIV sequences is referred to as an xHIV gag protein. One non-limiting example of such an SIV / HIV xHIV gag protein is described in U.S. Patent No. 11,191,784, the entire contents of which are incorporated herein by reference.

[0167] In some embodiments, the xHIV comprises an HIV long terminal repeat (LTR), an HIV gag protein (gag), an SIV element, an HIV Pol protein (Pol), and an HIV envelope (Env) protein. In some embodiments, the gag, Pol, and / or Env proteins are a polyprotein. In some embodiments, the gag protein, SIV element, and Pol protein of the xHIV are encoded by the nucleic acid sequence set forth in SEQ ID NO:57.

[0168] In some embodiments, the gag protein is encoded by the nucleic acid sequence set forth in SEQ ID NO:58.

[0169] In some embodiments, the SIV element is encoded by a nucleic acid sequence set forth in SEQ ID NO: 59. In some embodiments, the nucleic acid sequence encoding the SIV element is located within the nucleic acid sequence encoding the gag protein set forth in SEQ ID NO: 58. (SEQ ID NO: 59)

[0170] In some embodiments, the Pol protein is encoded by the nucleic acid sequence set forth in SEQ ID NO:60.

[0171] In some embodiments, the nucleotide sequence encoding the gag protein encodes a protein comprising the sequence set forth in SEQ ID NO:61. MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNS QVSQNYPVQQIGGNYVHLPLSPRTLNAWVKLIEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIRDIINEEVADWDLQHPQPAPQQGQLREPSGSDIAGTTSSVDEQIQWMYRQQNP IPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDAAVKNWMTQTLLIQNANPDCKLVLKGLGPGATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPATIMIQKGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGEETTTPSQKQEPIDKELYPLASLRSLFGSDPSSQ (SEQ ID NO: 61)

[0172] In some embodiments, the nucleotide sequence encoding the Pol protein encodes a protein comprising the sequence set forth in SEQ ID NO:62. (SEQ ID NO: 62)

[0173] In some embodiments, viral particles comprising the Carp Spring Viremia Virus G protein and / or targeting moiety provided herein comprise a nucleic acid molecule encoding a heterologous molecule of interest or "cargo." For example, a heterologous molecule of interest refers to any product that can be encoded by a nucleic acid molecule. As non-limiting examples, "cargo" or "heterologous molecule of interest" can refer to an siRNA, shRNA, a peptide, a polypeptide, a protein, a viral payload, a viral genome, or a combination thereof. In some embodiments, the polypeptide is a chimeric antigen receptor ("CAR").

[0174] As used herein, "chimeric antigen receptor" or "CAR" refers to an antigen-binding domain fused directly or indirectly (e.g., via a hinge or transmembrane domain) to an intracellular signaling domain capable of activating or stimulating immune cells. Most commonly, the extracellular binding domain of a CAR is composed of a single-chain variable fragment (scFv) obtained by fusing the variable heavy and variable light chain regions of a murine or humanized monoclonal antibody. Alternatively, an Fab'-derived scFv (not derived from an antibody, e.g., obtained from a Fab library) can be used. In various embodiments, the scFv is fused to a transmembrane domain and then to an intracellular signaling domain. However, the antigen-binding domain can be any molecule capable of binding to a target on a cell. For example, the antigen-binding domain of a CAR can be an antibody, an scFv antibody, an antigen-binding domain, an ankyrin repeat (e.g., DARPIN), a VHH domain antibody, a nanobody, a single-domain antibody, an FN3 domain, or any combination thereof. In some embodiments, a CAR includes one that provides only a CD3ξ signal upon antigen binding. In some embodiments, CARs include those that provide both costimulation (e.g., CD28 or CD137) and activation (CD3ξ). In some embodiments, CARs include those that provide multiple costimulation (e.g., CD28 and CD137) and activation (CD3ξ). In various embodiments, the CAR is selected to have high affinity or avidity for the antigen. In some embodiments, the CAR also comprises a 4-1BB domain. These are merely exemplary and not limiting to the present embodiments, and any chimeric antigen receptor can be delivered in combination with the viral particles and vectors provided herein. These are non-limiting examples of CARs, and any CAR construct can be encoded by a nucleic acid molecule.

[0175] In some embodiments, the antigen binding domain of the CAR is V H Domain, V L Domain or V H and V L In some embodiments, the VH A domain comprises an amino acid sequence having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 48, or any value or range therebetween. EVQLVESGGGLVQPGRSLRLSCAASGFTFNDYAMHWVRQAPGKGLEWVSTISWNSGSIGYADSVKGRFTISRDNAKKSLYLQMNSLRAEDTALYYCAKDIQYGNYYYGMDVWGQGTTVTVSS (SEQ ID NO: 48)

[0176] In some embodiments, V H The V domain comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 48. In some embodiments, the V H The V domain comprises an amino acid sequence having at least 95% identity to SEQ ID NO: 48. In some embodiments, the V H The V domain comprises an amino acid sequence having at least 98% identity to SEQ ID NO: 48. In some embodiments, the V H The V domain comprises an amino acid sequence having at least 99% identity to SEQ ID NO: 48. In some embodiments, the V H The domain comprises an amino acid sequence having the sequence of SEQ ID NO:48.

[0177] In some embodiments, V L A domain comprises an amino acid sequence having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 49, or any value or range therebetween. EIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPITFGQGTRLEIK (SEQ ID NO: 49)

[0178] In some embodiments, V L The V domain comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 49. In some embodiments, the V L The V domain comprises an amino acid sequence having at least 95% identity to SEQ ID NO: 49. In some embodiments, the V L The V domain comprises an amino acid sequence having at least 98% identity to SEQ ID NO: 49. In some embodiments, the V L The V domain comprises an amino acid sequence having at least 99% identity to SEQ ID NO: 49. In some embodiments, the V L The domain comprises an amino acid sequence having the sequence of SEQ ID NO:49.

[0179] In some embodiments, the antigen binding domain of the CAR is V H Domain and V L In some embodiments, the V H Domains and V L The domains are not linked by a linker peptide. H Domains and V L The domains are linked by a linker peptide as provided herein, which is (GGGGS) n (SEQ ID NO: 26), but are not limited to: n is independently 1 to 5. In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5.

[0180] In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 48. Hdomain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:49. L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 48. H V domain and having at least 90% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 48. H V domain and having at least 95% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 48. H domain and having at least 98% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 48. H domain and having at least 99% identity to SEQ ID NO: 49L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 48. H V domain and having the sequence of SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 90% identity to SEQ ID NO: 48. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:49. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 95% identity to SEQ ID NO: 48. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:49. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 98% identity to SEQ ID NO: 48. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:49. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 99% identity to SEQ ID NO: 48.H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:49. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having the amino acid sequence of SEQ ID NO: 48. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:49. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 90% identity to SEQ ID NO: 48. H V domain and having at least 90% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 95% identity to SEQ ID NO: 48. H V domain and having at least 90% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 90% identity to SEQ ID NO: 48. H V domain and having at least 95% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 95% identity to SEQ ID NO: 48. H V domain and having at least 95% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and VL The antigen-binding domain of the CAR comprises a V domain having at least 98% identity to SEQ ID NO: 48. H domain and having at least 98% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 99% identity to SEQ ID NO: 48. H domain and having at least 99% identity to SEQ ID NO: 49 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having the amino acid sequence of SEQ ID NO: 48. H V domain and having the amino acid sequence of SEQ ID NO: 49 L Includes.

[0181] In some embodiments, the antigen binding domain of the CAR is V H -ZV L Contains the formula for V H is a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 48, Z is a linker comprising the amino acid sequence GGGGSGGGSGGGGS (SEQ ID NO: 50), and V L is a light chain variable region comprising the amino acid sequence of SEQ ID NO: 49. In some embodiments, V H -ZV L The antigen binding domain of the CAR comprising the formula has the amino acid sequence set forth below. EVQLVESGGGLVQPGRSLRLSCAASGFTFNDYAMHWVRQAPGKGLEWVSTISWNSGSIGYADSVKGRFTISRDNAKKSLYLQMNSLRAEDTALYYCAKDIQYGNYYYGMDVWGQGTTVTVSSGGGGSGGGGSGGGGSEIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPITFGQGTRLEIK (SEQ ID NO: 51)

[0182] In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identity to the sequence of SEQ ID NO: 51. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 90% identity to the sequence of SEQ ID NO: 51. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 95% identity to the sequence of SEQ ID NO: 51. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 98% identity to the sequence of SEQ ID NO: 51. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 99% identity to the sequence of SEQ ID NO: 51. In some embodiments, the antigen binding domain of the CAR comprises the amino acid sequence of SEQ ID NO: 51.

[0183] In some embodiments, the antigen binding domain of the CAR is V L -ZV H Contains the formula for V L is a light chain variable region comprising the amino acid sequence of SEQ ID NO: 49, Z is a linker comprising the amino acid sequence GGGGSGGGSGGGGS (SEQ ID NO: 50), and V H is a light chain variable region comprising the amino acid sequence of SEQ ID NO: 48. In some embodiments, V L -ZV H The antigen binding domain of the CAR comprising the formula has the amino acid sequence set forth below. EIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPITFGQGTRLEIKGGGGSGGGGSGGGGSEVQLVESGGGLVQPGRSLRLSCAASGFTFNDYAMHWVRQAPGKGLEWVSTISWNSGSIGYADSVKGRFTISRDNAKKSLYLQMNSLRAEDTALYYCAKDIQYGNYYYGMDVWGQGTTVTVSS (SEQ ID NO: 52)

[0184] In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identity to the sequence of SEQ ID NO: 52. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 90% identity to the sequence of SEQ ID NO: 52. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 95% identity to the sequence of SEQ ID NO: 52. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 98% identity to the sequence of SEQ ID NO: 52. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 99% identity to the sequence of SEQ ID NO: 52. In some embodiments, the antigen binding domain of the CAR comprises the amino acid sequence of SEQ ID NO: 52.

[0185] In some embodiments, the antigen binding domain of the CAR is V H Domain, V L Domain or V H and V L In some embodiments, the V HA domain comprises an amino acid sequence having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 53, or any value or range therebetween. DIVLTQSPAILSASPGEKVTMTCRASSSVNYMDWYQKKPGSSPKPWIYATSNLASGVPARFSGSGSGTSYSLTISRVEAEDAATYYCQQWSFNPPTFGGGTKLEIKGSTS (SEQ ID NO: 53)

[0186] In some embodiments, V H The V domain comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 53. In some embodiments, the V H The V domain comprises an amino acid sequence having at least 95% identity to SEQ ID NO: 53. In some embodiments, the V H The V domain comprises an amino acid sequence having at least 98% identity to SEQ ID NO: 53. In some embodiments, the V H The V domain comprises an amino acid sequence having at least 99% identity to SEQ ID NO: 53. In some embodiments, the V H The domain comprises an amino acid sequence having the sequence of SEQ ID NO:53.

[0187] In some embodiments, V L A domain comprises an amino acid sequence having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 54, or any value or range therebetween. EVQLQQSGAELVKPGASVKMSCKASGYTFTSYNMHWVKQTPGQGLEWIGAIYPGNGDTSYNQKFKGKATLTADKSSSTAYMQLSSLTSEDSADYYCARSNYYGSSYWFFDVWGAGTTVTVSS (SEQ ID NO: 54)

[0188] In some embodiments, VL The V domain comprises an amino acid sequence having at least 90% identity to SEQ ID NO: 54. In some embodiments, the V L The V domain comprises an amino acid sequence having at least 95% identity to SEQ ID NO: 54. In some embodiments, the V L The V domain comprises an amino acid sequence having at least 98% identity to SEQ ID NO: 54. In some embodiments, the V L The V domain comprises an amino acid sequence having at least 99% identity to SEQ ID NO: 54. In some embodiments, the V L The domain comprises an amino acid sequence having the sequence of SEQ ID NO:54.

[0189] In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 53. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 54. L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 53. H V domain and having at least 90% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V LThe antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 53. H V domain and having at least 95% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 53. H domain and having at least 98% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 53. H domain and having at least 99% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen binding domain of the CAR comprises a V domain having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 53. H V domain and having the sequence of SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 90% identity with SEQ ID NO: 53. Hdomain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 54. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 95% identity with SEQ ID NO: 53. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 54. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 98% identity to SEQ ID NO: 53. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 54. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 99% identity to SEQ ID NO: 53. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 54. L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having the amino acid sequence of SEQ ID NO: 53. H domain and having at least 75%, 80%, 85%, 85%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 54.L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 90% identity with SEQ ID NO: 53. H V domain and having at least 90% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 95% identity with SEQ ID NO: 53. H V domain and having at least 90% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 90% identity with SEQ ID NO: 53. H V domain and having at least 95% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 95% identity with SEQ ID NO: 53. H V domain and having at least 95% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 98% identity to SEQ ID NO: 53. H domain and having at least 98% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V L The antigen-binding domain of the CAR comprises a V domain having at least 99% identity to SEQ ID NO: 53. H domain and having at least 99% identity to SEQ ID NO: 54 L In some embodiments, V H Domain and V LThe antigen-binding domain of the CAR comprises a V domain having the amino acid sequence of SEQ ID NO: 53. H V domain and having the amino acid sequence of SEQ ID NO: 54 L Includes.

[0190] In some embodiments, the antigen binding domain of the CAR is V H -ZV L Contains the formula for V H is a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 53, Z is a linker comprising the amino acid sequence GGGGSGGGSGGGGGS (SEQ ID NO: 50), and V L is a light chain variable region comprising the amino acid sequence of SEQ ID NO: 54. In some embodiments, V H -ZV L The antigen binding domain of the CAR comprising the formula has the amino acid sequence set forth below. DIVLTQSPAILSASPGEKVTMTCRASSSVNYMDWYQKKPGSSPKPWIYATSNLASGVPARFSGSGSGTSYSLTISRVEAEDAATYYCQQWSFNPPTFGGGTKLEIKGSTSGGGGSGGGGSGGGGSSEVQLQQSGAELVKPGASVKMSCKASGYTFTSYNMHWVKQTPGQGLEWIGAIYPGNGDTSYNQKFKGKATLTADKSSSTAYMQLSSLTSEDSADYYCARSNYYGSSYWFFDVWGAGTTVTVSS (SEQ ID NO: 55)

[0191] In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identity to the sequence of SEQ ID NO: 55. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 90% identity to the sequence of SEQ ID NO: 55. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 95% identity to the sequence of SEQ ID NO: 55. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 98% identity to the sequence of SEQ ID NO: 55. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 99% identity to the sequence of SEQ ID NO: 55. In some embodiments, the antigen binding domain of the CAR comprises the amino acid sequence of SEQ ID NO: 55.

[0192] In some embodiments, the antigen binding domain of the CAR is V L -ZV H Contains the formula for V L is a light chain variable region comprising the amino acid sequence of SEQ ID NO: 54, Z is a linker comprising the amino acid sequence GGGGSGGGSGGGGS (SEQ ID NO: 50), and V H is a light chain variable region comprising the amino acid sequence of SEQ ID NO: 53. In some embodiments, V L -ZV H The antigen binding domain of the CAR comprising the formula has the amino acid sequence set forth below. SEVQLQQSGAELVKPGASVKMSCKASGYTFTSYNMHWVKQTPGQGLEWIGAIYPGNGDTSYNQKFKGKATLTADKSSSTAYMQLSSLTSEDSADYYCARSNYYGSSYWFFDVWGAGTTVTVSSGGGGSGGGGSGGGGSDIVLTQSPAILSASPGEKVTMTCRASSSVNYMDWYQKKPGSSPKPWIYATSNLASGVPARFSGSGSGTSYSLTISRVEAEDAATYYCQQWSFNPPTFGGGTKLEIKGSTS (SEQ ID NO: 56)

[0193] In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identity to the sequence of SEQ ID NO: 56. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 90% identity to the sequence of SEQ ID NO: 56. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 95% identity to the sequence of SEQ ID NO: 56. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 98% identity to the sequence of SEQ ID NO: 56. In some embodiments, the antigen binding domain of the CAR comprises an amino acid sequence having at least 99% identity to the sequence of SEQ ID NO: 56. In some embodiments, the antigen binding domain of the CAR comprises the amino acid sequence of SEQ ID NO: 56.

[0194] In some embodiments, the antigen-binding domain of the CAR comprises rituximab, ocrelizumab, obinutuzumab, ofatumumab, ibritumomab tiuxetan, tositumomab, or ublituximab. In some embodiments, the antigen-binding domain comprises rituximab. In some embodiments, the antigen-binding domain comprises ofatumumab. In some embodiments, the CAR also comprises a 4-1BB domain. These are merely exemplary and not limiting of the present embodiments; any chimeric antigen receptor can be delivered in combination with the viral particles and vectors provided herein. These are non-limiting examples of CARs; any CAR construct can be encoded by a nucleic acid molecule.

[0195] In some embodiments, the pseudotyped virus particle further comprises a heterologous nucleic acid molecule encoding a cargo of interest. The nucleic acid molecule may be useful for regulating the expression of a target gene. In some embodiments, the cargo may be used to regulate cellular activity or express a protein that is transported to the surface of a target cell. Thus, in some embodiments, the nucleic acid may comprise an siRNA or shRNA. The nucleic acid may also encode a cargo of interest. Thus, in some embodiments, the cargo of interest may comprise a polypeptide or portion thereof, a protein or portion thereof, a chimeric antigen receptor or portion thereof, or a tumor antigen or portion thereof. In some embodiments, the cargo of interest is an antibody produced by a virus, which may be secreted by a cell infected with the virus. The term "protein" refers to any polypeptide that performs its native function within a cellular environment. Thus, in some embodiments, the protein encoded by the nucleic acid cargo of interest may comprise an enzyme, a nuclear receptor, a transporter, a ribosomal protein, a membrane-bound protein, a cytoplasmic protein, a G protein-coupled receptor, a voltage-gated ion channel, a secreted protein, a mitochondrial protein, a cytokine, a chimeric antigen receptor, a tumor antigen, or portions or chimeric species thereof.

[0196] Without being bound by any particular theory, viral particles comprising the carp spring viremia virus G protein containing a targeting moiety provided herein can be used to express a heterologous molecule of interest in target cells. Thus, for example, a CAR can be expressed in a T cell targeted by a viral particle pseudotyped with the carp spring viremia virus G protein as provided herein. When a T cell is the intended target, the viral particle can include a targeting moiety that binds to a target on the surface of the T cell, such as, but not limited to, CD2, CD3, CD4, CD5, CD7, or CD8. In some embodiments, the target is CD2. In some embodiments, the target is CD3. In some embodiments, the target is CD4. In some embodiments, the target is CD5. In some embodiments, the target is CD6. In some embodiments, the target is CD7. In some embodiments, the target is CD8.

[0197] In some embodiments, the pseudotyped viral particle is a recombinant lentivirus. In some embodiments, the recombinant pseudotyped viral particle is replication-competent. In some embodiments, the recombinant pseudotyped viral particle is replication-incompetent.

[0198] In some embodiments, pharmaceutical compositions are provided comprising the enveloped pseudotyped virus particles or vectors described herein, i.e., particles comprising the Spring Viremia of Carp Virus G protein described herein.

[0199] In some embodiments, methods for delivering a cargo of interest to a cell are provided, hi some embodiments, the methods comprise contacting the cell with a pseudotyped virus-like particle or viral vector provided herein, or a pharmaceutical composition comprising same.

[0200] In some embodiments, methods are provided for delivering a cargo of interest to cells of a subject. In some embodiments, the methods comprise administering to a subject a pseudotyped virus-like particle or viral vector described herein, or a pharmaceutical composition comprising the same. In some embodiments, the cargo is a chimeric antigen receptor, or as otherwise provided herein.

[0201] In some embodiments, methods for delivering a chimeric antigen receptor to T cells of a subject are provided, which methods comprise administering to the subject a pseudotyped virus-like particle or viral vector described herein, or a pharmaceutical composition comprising the same, wherein the pseudotyped virus-like particle or viral vector comprises a heterologous nucleic acid molecule encoding the chimeric antigen receptor.

[0202] Also provided herein are nucleic acid molecules encoding the Spring Viremia of Carp virus G protein described herein.

[0203] Also provided are methods for producing virus-like particles or vectors comprising the Carp Spring Viremia Virus G protein. In some embodiments, the methods comprise transfecting or transducing a packaging cell line with a nucleic acid molecule encoding the Carp Spring Viremia Virus G protein described herein under conditions sufficient to produce the pseudotyped virus-like particle or viral vector. In some embodiments, the methods comprise transfecting or transducing a packaging cell line with a plurality of nucleic acid molecules provided herein under conditions sufficient to produce the pseudotyped virus-like particle or viral vector. In some embodiments, the methods further comprise isolating the pseudotyped virus-like particle or viral vector. In some embodiments, the nucleic acid molecule also comprises a nucleic acid molecule encoding a targeting moiety and / or cargo to be delivered by the produced viral vector.

[0204] In some embodiments, the method comprises transfecting or transducing a viral packaging cell with a nucleic acid molecule encoding a polypeptide and a nucleic acid molecule encoding a targeting moiety under conditions sufficient to produce viral particles. In some embodiments, the method comprises transfecting or transducing a cell with a lentiviral transfer genome encoding a heterologous molecule of interest. A "lentiviral transfer genome" is a construct that includes appropriate viral elements, such as inverted terminal repeats, that allow the molecule of interest to be incorporated into viral particles. In some embodiments, the method comprises transfecting or transducing a cell with a nucleic acid molecule encoding gag-pol and / or rev. In some embodiments, the cell already expresses gag-pol and / or rev, such as by stable expression. In some embodiments, the cell is HEK293 (e.g., HEK293T cell). In some embodiments, the method comprises culturing the cell for at least 24 or 48 hours to produce virus. In some embodiments, the method comprises isolating viral particles from the cell supernatant. Any method can be used to isolate the viral particles, including, but not limited to, centrifugation.

[0205] Also provided herein are methods of treating cancer in a subject, in some embodiments, the methods comprise administering to a subject a pseudotyped virus-like particle or viral vector described herein, or a pharmaceutical composition comprising the same, wherein the pseudotyped virus-like particle or viral vector comprises a heterologous nucleic acid molecule encoding a chimeric antigen receptor.

[0206] Also provided herein are methods of treating a disease in a subject in need thereof.

[0207] In some embodiments, provided methods include, but are not limited to, methods of treating a disease in a subject in need thereof, comprising administering to the subject a viral particle(s) provided herein to treat the disease.

[0208] In certain embodiments, the disease is cancer. Furthermore, the compositions provided herein can be used in methods for treating any cancer-related condition, such as a cellular immune response against tumor cell(s), where treating or alleviating the disease is desirable. Types of cancer to be treated include, but are not limited to, carcinoma, blastoma, sarcoma, certain leukemias or lymphoid malignancies, benign and malignant tumors, and malignant tumors (e.g., sarcoma, carcinoma, and melanoma). Other exemplary cancers include, but are not limited to, breast cancer, prostate cancer, ovarian cancer, cervical cancer, skin cancer, pancreatic cancer, colorectal cancer, kidney cancer, liver cancer, brain cancer, lymphoma, leukemia, lung cancer, thyroid cancer, and the like. The cancer can be a non-solid tumor (such as a hematological tumor) or a solid tumor. Included are adult tumors / cancers and pediatric tumors / cancers. In one embodiment, the cancer is a hematological tumor. In one embodiment, the cancer is a carcinoma. In one embodiment, the cancer is a sarcoma. In one embodiment, the cancer is a leukemia. In one embodiment, the cancer is a solid tumor.

[0209] A solid tumor is an abnormal mass of tissue that usually does not contain cysts or liquid areas. A solid tumor can be benign or malignant. Various types of solid tumors are named according to the type of cells that form them (such as sarcoma, carcinoma, and lymphoma). Examples of solid tumors, such as sarcoma and carcinoma, include fibrosarcoma, myxosarcoma, liposarcoma, chondrosarcoma, osteosarcoma, synovioma, mesothelioma, Ewing's tumor, leiomyosarcoma, rhabdomyosarcoma, colorectal cancer, lymphoid malignancies, pancreatic cancer, breast cancer, lung cancer, ovarian cancer, prostate cancer, hepatocellular carcinoma, squamous cell carcinoma, basal cell carcinoma, adenocarcinoma, sweat gland carcinoma, medullary thyroid carcinoma, papillary thyroid carcinoma, pheochromocytoma, sebaceous gland carcinoma, papillary carcinoma, papillary adenocarcinoma, medullary carcinoma, bronchial carcinoma, renal cell carcinoma, liver carcinoma, Includes cholangiocarcinoma, choriocarcinoma, Wilms' tumor, cervical cancer, testicular tumor, seminoma, bladder cancer, melanoma, CNS tumors (such as gliomas (such as brain stem gliomas and mixed gliomas), glioblastomas (also called glioblastoma multiforme), astrocytomas, CNS lymphomas, germinomas, medulloblastomas, schwannomas, craniopharyngiomas, ependymomas, pinealomas, hemangioblastomas, acoustic neuromas, oligodendroglioma, meningiomas, neuroblastomas, retinoblastomas, and brain metastases).

[0210] Carcinomas treatable by the methods disclosed herein include, but are not limited to, esophageal carcinoma, hepatocellular carcinoma, basal cell carcinoma (a type of skin cancer), squamous cell carcinoma (various tissues), bladder cancer (including transitional cell carcinoma (malignant tumor of the bladder)), bronchial carcinoma, colon carcinoma, colorectal carcinoma, gastric cancer, lung cancer (including small cell lung carcinoma and non-small cell lung carcinoma), adrenocortical carcinoma, thyroid carcinoma, pancreatic carcinoma, breast cancer, ovarian cancer, prostate cancer, adenocarcinoma, sweat gland carcinoma, sebaceous gland carcinoma, papillary carcinoma, papillary adenocarcinoma, cystadenocarcinoma, medullary carcinoma, renal cell carcinoma, ductal carcinoma in situ or bile duct carcinoma, choriocarcinoma, seminoma, embryonal carcinoma, Wilms' tumor, cervical carcinoma, uterine carcinoma, testicular carcinoma, osteogenic carcinoma, epithelial carcinoma, and nasopharyngeal carcinoma.

[0211] In certain exemplary embodiments, the compositions provided herein can be used in methods for treating myeloma or a myeloma-related condition. Examples of myeloma or a myeloma-related condition include, but are not limited to, light-chain myeloma, non-secretory myeloma, monoclonal gammopathy of undetermined significance (MGUS), plasmacytoma (e.g., solitary, multiple solitary, extramedullary plasmacytoma), amyloidosis, and multiple myeloma. In some embodiments, methods for treating multiple myeloma are provided. In some embodiments, the multiple myeloma is refractory myeloma. In some embodiments, the multiple myeloma is relapsed myeloma.

[0212] In certain exemplary embodiments, the in vivo modified immune cells generated using the compositions provided herein are used to treat melanoma or a condition associated with melanoma. Examples of melanoma or a condition associated with melanoma include, but are not limited to, superficial spreading melanoma, nodular melanoma, lentigo maligna melanoma, acral lentigo melanoma, amelanotic melanoma, or cutaneous melanoma (e.g., melanoma of the skin, eye, vulva, vagina, or rectum). In some embodiments, the melanoma is cutaneous melanoma. In some embodiments, the melanoma is refractory melanoma. In some embodiments, the melanoma is recurrent melanoma.

[0213] In some embodiments, the compositions provided herein are used to treat sarcoma or a condition associated with sarcoma. Examples of sarcoma or a condition associated with sarcoma include, but are not limited to, angiosarcoma, chondrosarcoma, chordoma, endothelial sarcoma, Ewing's sarcoma, fibrosarcoma, gastrointestinal stromal tumor, leiomyosarcoma, liposarcoma, lymphangiosarcoma, lymphangioendothelial sarcoma, mesothelioma, malignant peripheral nerve sheath tumor, myxosarcoma, osteogenic sarcoma, osteosarcoma, pleomorphic sarcoma, rhabdomyosarcoma, synovium, and other soft tissue sarcomas. In some embodiments, the sarcoma is a synovial sarcoma. In some embodiments, the sarcoma is a liposarcoma, such as myxoid / round cell liposarcoma, differentiated / dedifferentiated liposarcoma, or pleomorphic liposarcoma. In some embodiments, the sarcoma is a myxoid / round cell liposarcoma. In some embodiments, the sarcoma is a refractory sarcoma. In some embodiments, the sarcoma is a recurrent sarcoma.

[0214] In some embodiments, the subject is treated with a therapeutic agent targeting a disease or condition, such as a tumor, prior to administration of the composition. In some aspects, the subject is refractory or non-responsive to other therapeutic agents. In some embodiments, the subject has persistent or recurrent disease after treatment with another therapeutic intervention, including, for example, chemotherapy, radiation, and / or hematopoietic stem cell transplantation (HSCT), e.g., allogeneic HSCT. In some embodiments, administration effectively treats the subject despite the subject becoming resistant to another therapy.

[0215] In some embodiments, the subject has responded to other therapeutic agents, and treatment with the therapeutic agent reduces the disease burden. In some aspects, the subject is initially responsive to the therapeutic agent, but exhibits a recurrence of the disease or symptoms over time. In some embodiments, the subject does not relapse. In some such embodiments, the subject is determined to be at risk of relapse, e.g., determined to be at high risk of relapse, and therefore the composition is administered prophylactically, e.g., to reduce the likelihood of relapse or prevent relapse. In some aspects, the subject has not previously been treated with other therapeutic agents.

[0216] The composition can be administered by any convenient method known to those skilled in the art. For example, the composition can be administered to a subject by aerosol inhalation, injection, ingestion, transfusion, implant, or transplantation. The compositions described herein can be administered to a patient intraarterially, subcutaneously, intradermally, intratumorally, intranodally, intramedullary, intramuscularly, intravenously (iv), intraperitoneally, intranasally, intracranially, or intraosseously. In another example, the composition is directly injected into a local disease site, lymph node, organ, tumor, or the like of a subject.

[0217] For the prevention or treatment of disease, the appropriate dosage will vary depending on the type of disease being treated, the severity and course of the disease, whether the composition is being administered for prophylactic or therapeutic purposes, previous treatments, the subject's medical history and response to treatment, and the discretion of the attending physician. In some embodiments, the compositions are suitably administered to the subject at one time or over a series of treatments.

[0218] In some embodiments, the composition is administered as part of a combination therapy, simultaneously with another therapeutic intervention, such as an antibody or produced cell or receptor, or an agent such as a cytotoxic substance or therapeutic agent, or sequentially in any order. In some embodiments, the composition(s) are administered simultaneously with one or more additional therapeutic agents or in conjunction with another therapeutic intervention, or sequentially in any order. In some situations, the composition is co-administered with another therapy sufficiently close in time so that the composition enhances the effect of the one or more additional therapeutic agents, or vice versa. In some embodiments, the composition is administered before one or more additional therapeutic agents. In some embodiments, the composition is administered after one or more additional therapeutic agents. In some embodiments, the one or more additional agents include a cytokine, such as IL-2, to enhance durability. In some embodiments, the method includes administering a chemotherapeutic agent. In some embodiments, the method does not include administering a chemotherapeutic agent.

[0219] In certain embodiments, the composition may be administered to a subject in combination with an immune checkpoint antibody (e.g., an anti-PD1 antibody, an anti-CTLA-4 antibody, or an anti-PDL1 antibody). For example, the viral vector may be administered in combination with, for example, an antibody or antibody fragment that targets PD-1 (programmed cell death 1 protein). Examples of anti-PD-1 antibodies include, but are not limited to, pembrolizumab (KEYTRUDA®, formerly known as lambrolizumab, also known as MK-3475) and nivolumab (BMS-936558, MDX-1106, ONO-4538, OPDIVO®) or an antigen-binding fragment thereof. In certain embodiments, the composition may be administered in combination with an anti-PD-L1 antibody or an antigen-binding fragment thereof. Examples of anti-PD-L1 antibodies include, but are not limited to, BMS-936559, MPDL3280A (TECENTRIQ®, atezolizumab), and MEDI4736 (durvalumab, Imfinzi). In certain embodiments, the compositions may be administered in combination with an anti-CTLA-4 antibody or antigen-binding fragment thereof. An example of an anti-CTLA-4 antibody includes, but is not limited to, ipilimumab (trade name Yervoy). Other types of immune checkpoint modulators may also be used, including, but not limited to, small molecules, siRNA, miRNA, and CRISPR systems. The immune checkpoint modulator may be administered before, after, or simultaneously with the viral vector. In certain embodiments, a combination therapy including an immune checkpoint modulator can enhance the therapeutic effect of a treatment including a composition provided herein. The other therapeutic agent may be administered simultaneously with, before, or after the composition provided herein is administered to a subject.

[0220] In certain embodiments, the subject is provided with a second-line treatment, including but not limited to chemotherapy, radiation therapy, surgery, and drug therapy, etc. In some embodiments, the subject is not provided with a second-line treatment.

[0221] In some embodiments, these methods are performed without a lymphodepletion step, such as administration of cyclophosphamide and / or fludarabine.

[0222] In some embodiments, after administration of the composition, the subject can undergo a conditioning therapy to kill specific immune cells that are not transduced with the CAR encoded by the composition. This can be accomplished by including a selectable marker encoded by the nucleic acid cargo of interest. In some embodiments, the conditioning therapy comprises administering an effective amount of cyclophosphamide to the subject. In some embodiments, the conditioning therapy comprises administering an effective amount of fludarabine to the subject. In some embodiments, the conditioning therapy comprises administering an effective amount of a combination of cyclophosphamide and fludarabine to the subject.

[0223] In some embodiments, particular dosing regimens of the present disclosure include a lymphodepletion step following administration of the composition. In exemplary embodiments, the lymphodepletion step includes administration of cyclophosphamide and / or fludarabine.

[0224] In some embodiments, the lymphocyte depletion step comprises administering cyclophosphamide at a dose of about 200 mg / m² / day to about 2000 mg / m² / day (e.g., 200 mg / m² / day, 300 mg / m² / day, or 500 mg / m² / day). In exemplary embodiments, the cyclophosphamide dosage is about 300 mg / m² / day. In some embodiments, the lymphocyte depletion step comprises administering fludarabine at a dose of about 20 mg / m² / day to about 900 mg / m² / day (e.g., 20 mg / m² / day, 25 mg / m² / day, 30 mg / m² / day, or 60 mg / m² / day). In exemplary embodiments, the fludarabine dosage is about 30 mg / m² / day.

[0225] In some embodiments, the lymphocyte depletion step comprises administering cyclophosphamide at a dose of about 200 mg / m² / day to about 2000 mg / m² / day (e.g., 200 mg / m² / day, 300 mg / m² / day, or 500 mg / m² / day) and fludarabine at a dose of about 20 mg / m² / day to about 900 mg / m² / day (e.g., 20 mg / m² / day, 25 mg / m² / day, 30 mg / m² / day, or 60 mg / m² / day). In exemplary embodiments, the lymphocyte depletion step comprises administering cyclophosphamide at a dose of about 300 mg / m² / day and fludarabine at a dose of about 30 mg / m² / day.

[0226] In an exemplary embodiment, the dose of cyclophosphamide is 300 mg / m2 / day for three days and the dose of fludarabine is 30 mg / m2 / day for three days.

[0227] It is known in the art that one of the side effects of CAR T cell use can be the development of immune activation known as cytokine release syndrome (CRS). CRS results from immune activation, resulting in an increase in inflammatory cytokines. CRS is a known target toxicity, and its occurrence likely correlates with efficacy. Clinical and laboratory evaluations range from mild CRS (systemic symptoms and / or grade 2 organ toxicity) to severe CRS (sCRS, grade 3 or higher organ toxicity, aggressive clinical intervention, and / or potentially life-threatening). Clinical features include high fever, malaise, fatigue, myalgia, nausea, anorexia, tachycardia / hypotension, capillary leak, cardiac dysfunction, renal dysfunction, liver failure, and disseminated intravascular coagulation. Dramatic increases in cytokines such as interferon-γ, granulocyte-macrophage colony-stimulating factor, IL-10, and IL-6 have been documented following CAR T cell infusion. One of the hallmarks of CRS is an increase in cytokines such as IL-6 (severe increase), IFN-γ, TNF-α (moderate increase), and IL-2 (mild increase). Increases in clinically available inflammatory markers such as ferritin and C-reactive protein (CRP) have also been observed to correlate with CRS syndrome. The presence of CRS generally correlates with proliferation of adoptively transferred cells and progressive immune activation. It has been demonstrated that the severity of CRS is determined by the disease burden at the time of infusion, as patients with a large tumor burden are more likely to develop sCRS.

[0228] Thus, in some embodiments, these methods include an appropriate CRS management strategy for alleviating the physiological symptoms of uncontrolled inflammation after CRS diagnosis without reducing the anti-tumor effect of in vivo generated cells (e.g., CAR T cells). CRS management strategies are known in the art. For example, administration of systemic corticosteroids can rapidly improve the symptoms of sCRS (e.g., grade 3 CRS) without compromising the initial anti-tumor response.

[0229] In some embodiments, an anti-IL-6R antibody may be administered. An example of an anti-IL-6R antibody is the monoclonal antibody tocilizumab (also known as atlizumab, sold as Actemra or RoActemra), which has been approved by the U.S. Food and Drug Administration. Tocilizumab is a humanized monoclonal antibody against the interleukin-6 receptor (IL-6R). Administration of tocilizumab has been shown to improve CRS almost immediately.

[0230] CRS is typically managed based on the severity of the syndrome observed, and interventions are tailored accordingly. Decisions regarding the management of CRS are based on clinical signs and symptoms and response to interventions, not laboratory values ​​alone.

[0231] Mild to moderate cases are generally treated with symptom management using fluid therapy, nonsteroidal anti-inflammatory drugs (NSAIDs), and antihistamines as needed to adequately relieve symptoms. More severe cases include patients with any degree of hemodynamic instability, in which case tocilizumab is recommended. The first-line treatment for CRS is tocilizumab, which in some embodiments is administered at the labeled dose of 8 mg / kg IV over 60 minutes (not to exceed 800 mg per dose), and tocilizumab can be repeated every 8 hours. If the response to the initial dose of tocilizumab is suboptimal, additional doses of tocilizumab may be considered. Tocilizumab can be administered alone or in combination with corticosteroid therapy. Patients with persistent or progressive CRS symptoms, inadequate clinical improvement within 12–18 hours, or poor response to tocilizumab can be treated with high-dose corticosteroid therapy (typically IV hydrocortisone 100 mg or methylprednisolone 1–2 mg / kg). Patients with more severe hemodynamic instability or more severe respiratory symptoms may receive high-dose corticosteroid therapy earlier in the course of CRS. CRS management guidance may be based on published criteria (Lee et al. (2019) Biol Blood Marrow Transplant, doi.org / 10.1016 / j.bbmt.2018.12.758; Neelapu et al. (2018) Nat Rev Clin Oncology, 15:47; Teachey et al. (2016) Cancer Discov, 6(6):664–679).

[0232] In patients undergoing CAR-T therapy, features consistent with macrophage activation syndrome (MAS) or hemophagocytic lymphohistiocytosis (HLH) have been observed, consistent with the clinical manifestations of CRS (Henter, 2007). MAS appears to be a response to immune activation resulting from CRS and should be considered a manifestation of CRS. MAS resembles HLH (a response to immune stimulation). The clinical syndrome of MAS is characterized by severe, unremitting fever, cytopenias affecting at least two of the three blood systems, and hepatosplenomegaly. This is associated with elevated serum ferritin, soluble interleukin-2 receptor, and triglycerides, and decreased circulating natural killer (NK) activity.

[0233] In some embodiments, methods of treating cancer in a subject in need thereof are provided, the methods comprising administering to the subject any of the compositions, such as viral particle(s), provided herein.

[0234] The compositions disclosed herein can include pharmaceutical compositions, for example, can include a pharmaceutically acceptable carrier and / or a pharmaceutical agent.

[0235] The term "pharmaceutical formulation" refers to a preparation that is in a form that allows the biological activity of the active ingredient contained therein to be effective and does not contain any additional components that are unacceptably toxic to the subject to which the formulation is administered. A "pharmaceutically acceptable carrier" refers to an ingredient in a pharmaceutical formulation, other than the active ingredient, that is non-toxic to the subject. Pharmaceutically acceptable carriers include, but are not limited to, buffers, excipients, stabilizers, or preservatives. In some embodiments, the choice of carrier is determined in part by the particular cell and / or method of administration. Accordingly, a variety of suitable formulations exist. For example, the pharmaceutical composition can include a preservative. Suitable preservatives can include, for example, methylparaben, propylparaben, sodium benzoate, and benzalkonium chloride. In some embodiments, a mixture of two or more preservatives is used. The preservative or mixtures thereof are typically present in an amount of about 0.0001% to about 2% by weight of the total composition. Carriers are described, for example, in Remington's Pharmaceutical Sciences 16th edition, Osol, A. Ed. (1980).Pharmaceutically acceptable carriers are typically nontoxic to recipients at the dosages and concentrations employed and include, but are not limited to, buffers (such as phosphate, citric acid, and other organic acids), antioxidants (including ascorbic acid and methionine), preservatives (such as octadecyldimethylbenzylammonium chloride, hexamethonium chloride, benzalkonium chloride, benzethonium chloride, phenol, butyl or benzyl alcohol, alkyl parabens such as methyl or propyl paraben, catechol, resorcinol, cyclohexanol, 3-pentanol, and m-cresol), low molecular weight (less than about 10 residues) polypeptides, These include, but are not limited to, proteins (such as serum albumin, gelatin, or immunoglobulins), hydrophilic polymers (such as polyvinylpyrrolidone), amino acids (such as glycine, glutamine, asparagine, histidine, arginine, or lysine), monosaccharides, disaccharides, and other carbohydrates such as glucose, mannose, or dextrin, chelating agents (such as EDTA), sugars (such as sucrose, mannitol, trehalose, or sorbitol), salt-forming counterions (such as sodium), metal complexes (e.g., Zn-protein complexes), and / or non-ionic surfactants (such as polyethylene glycol (PEG)).

[0236] In some embodiments, the composition includes a buffer. Suitable buffers include, for example, citric acid, sodium citrate, phosphoric acid, potassium phosphate, and various other acids and salts. In some embodiments, a mixture of two or more buffers is used. The buffer or mixture is typically present in an amount of about 0.001% to about 4% by weight of the total composition. Methods for preparing administrable pharmaceutical compositions are known. Exemplary methods are described in detail, for example, in Remington: The Science and Practice of Pharmacy, Lippincott Williams & Wilkins; 21st ed. (May 1, 2005).

[0237] The formulation may comprise an aqueous solution. The formulation or composition may contain more than one active ingredient useful for the particular indication, disease, or condition being treated with the composition, preferably those with complementary activities that do not adversely affect each other. Such active ingredients are preferably present in combination in amounts effective for the intended purpose. Thus, in some embodiments, the pharmaceutical composition further comprises another pharmaceutically active agent or drug, such as a chemotherapeutic agent, e.g., asparaginase, busulfan, carboplatin, cisplatin, daunorubicin, doxorubicin, fluorouracil, gemcitabine, hydroxyurea, methotrexate, paclitaxel, rituximab, vinblastine, and / or vincristine. In some embodiments, the pharmaceutical composition contains the composition in an amount effective to treat or prevent the disease or condition, e.g., a therapeutically or prophylactically effective amount. In some embodiments, the therapeutic or prophylactic effect is monitored by periodic evaluation of the treated subject. The desired dose may be delivered by a single bolus administration of the composition, by multiple bolus administrations of the composition, or by continuous infusion administration of the composition. In some embodiments, the pharmaceutical composition does not include a chemotherapeutic agent.

[0238] Formulations include those for oral, intravenous, intraperitoneal, subcutaneous, pulmonary, transdermal, intramuscular, intranasal, buccal, sublingual, or suppository administration. In some embodiments, the compositions are administered parenterally. As used herein, the term "parenteral" includes intravenous, intramuscular, subcutaneous, rectal, vaginal, and intraperitoneal administration. In some embodiments, the compositions are administered to a subject using peripheral systemic delivery via intravenous, intraperitoneal, or subcutaneous injection. In some embodiments, the compositions are provided as sterile liquid preparations, such as isotonic aqueous solutions, suspensions, emulsions, dispersions, or viscous compositions, which in some embodiments may be buffered to a selected pH. Liquid preparations are generally easier to prepare than gels, other viscous compositions, and solid compositions. Additionally, liquid compositions can be administered somewhat more conveniently, particularly by injection. Viscous compositions, on the other hand, may be formulated within an appropriate viscosity range to provide longer contact periods with specific tissues. Liquid or viscous compositions may contain a carrier which may be a solvent or dispersion medium containing, for example, water, saline, phosphate buffered saline, polyol (for example, glycerol, propylene glycol, liquid polyethylene glycol, and the like), and suitable mixtures thereof.

[0239] Sterile injectable solutions can be prepared by incorporating the composition in a solvent, such as by mixing with a suitable carrier, diluent, or excipient, such as sterile water, saline, glucose, dextrose, etc. The composition can contain auxiliary substances, such as wetting agents, dispersing or emulsifying agents (e.g., methylcellulose), pH buffering agents, gelling or thickening agents, preservatives, flavoring agents, and / or coloring agents, depending on the route of administration and the desired preparation. In some embodiments, standard texts may be consulted to prepare appropriate formulations.

[0240] Various additives can be added to enhance the stability and sterility of the compositions, including antimicrobial preservatives, antioxidants, chelating agents, and buffers. Prevention of microbial action can be ensured by various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, and sorbic acid. Prolonged absorption of injectable pharmaceutical forms can be brought about by the use of agents delaying absorption, for example, aluminum monostearate and gelatin.

[0241] Formulations to be used for in vivo administration are typically sterile. Sterility is readily accomplished, for example, by filtration through sterile filtration membranes.

[0242] The embodiments provided herein can be used for many purposes, as they allow the delivery of a gene of interest or other heterologous sequence using a pseudotyped virus capable of fusing with a target cell.

[0243] Enumerated Embodiments In some embodiments, the following embodiments are provided: 1. A viral particle comprising a targeting moiety and a polypeptide comprising a viral structural protein comprising an amino acid sequence that is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2. 2. The viral particle of embodiment 1, wherein the viral structural protein comprises a polypeptide comprising the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2. 3. The viral particle of embodiment 1 or 2, wherein the viral particle is a pseudotyped lentivirus. 4. The viral particle of any one of embodiments 1 to 3, wherein the viral particle further comprises a nucleic acid molecule encoding a heterologous molecule of interest. 5. The viral particle of embodiment 4, wherein the heterologous molecule of interest is an siRNA, shRNA, non-coding RNA (e.g., a guide RNA in a CRISPR system), a peptide, a polypeptide, a protein, a viral payload, a viral genome, or a combination thereof. 6. The viral particle of embodiment 4 or 5, wherein said heterologous molecule of interest is a chimeric antigen receptor ("CAR"). 7. The viral particle of embodiment 6, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 51. 8. The viral particle of embodiment 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 90% identity to SEQ ID NO: 51. 9. The viral particle of embodiment 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 95% identity to SEQ ID NO: 51. 10. The viral particle of embodiment 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 98% identity to SEQ ID NO: 51. 11. The viral particle of embodiment 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 99% identity to SEQ ID NO: 51. 12. The viral particle of embodiment 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having the amino acid sequence of SEQ ID NO: 51. 13. The viral particle of embodiment 6, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 52. 14. The viral particle of embodiment 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 90% identity to SEQ ID NO: 52. 15. The viral particle of embodiment 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 95% identity to SEQ ID NO: 52. 16. The viral particle of embodiment 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 98% identity to SEQ ID NO: 52. 17. The viral particle of embodiment 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 99% identity to SEQ ID NO: 52. 18. The viral particle of embodiment 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having the amino acid sequence of SEQ ID NO: 52. 19. The viral particle of any one of embodiments 1-18, wherein the targeting moiety binds to a T cell, a B cell, an NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell, or an immune cell, such as, for example, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD20+ cancer cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, an NKG2D+ natural killer cell, a SLC1A3+ astrocyte, or a SLC7A10+ adipocyte. 20. The targeting moiety is selected from the group consisting of CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed on acute leukemia or lymphoma but not on hematopoietic progenitor cells, a glycosylated CD43 epitope expressed on non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin l8.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also known as CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), mutant elongation factor 2 (ELF2M), ephrin B2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSH) R), Fos-related antigen 1, fucosyl-GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(ll)Cer), ganglioside GM3 (aNeu5Ac(2-3)bDClalp(l-4)bDGlcp(ll)Cer), GD3, GFR alpha 4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide moiety of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV-1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer-testis antigen 1 (MAD-CT-1), melanoma cancer-testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface-associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin-4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), and O-acetylglucosaminyltransferase V (O-acetylglucosaminyltransferase V). Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta-specific 1 (PLAC1), platelet-derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin-binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate-specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, kidney ubiquitous 1 (RU1), kidney ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF-beta R2, antigen recognized by TNT antibodies, thyroid-stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn 20. The viral particle of any one of embodiments 1-19, which binds to ag, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B-cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7-related (TEM7R), tumor protein p53 (p53), tumor-associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase-related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1). 21. The viral particle of any one of embodiments 1 to 20, wherein the targeting moiety is an antibody, an scFv antibody, an antigen-binding domain, ankyrin repeats (e.g., DARPIN), a VHH domain antibody, a nanobody, a single domain antibody, an FN3 domain, or any combination thereof. 22. The targeting moiety is IgG Fc stalk, Polypeptide stalk, envelope glycoprotein G or H of a Paramyxoviridae virus, such as a Morbillivirus, such as the measles virus, or a Henipavirus, such as the Nipah virus, Cedar virus, or Hendra virus; Glycoproteins of Rhabdoviridae viruses such as New Jersey vesicular stomatitis virus, vesicular stomatitis Indiana virus, vesicular stomatitis Alagoas virus, vesicular stomatitis Maraba virus, vesicular stomatitis Carajas virus, parainfluenza virus, fall armyworm rhabdovirus isolate Sf G, Drosophila obscura sigma virus 10A, Wuhan insect virus 7, Perch virus, or spring viremia of carp virus, glycoproteins of Filoviridae viruses such as Ebola virus, or 22. The virus particle according to any one of embodiments 1 to 21, which is attached to the viral surface via a glycoprotein of an Arenaviridae virus, such as Machupo virus. 23. The viral particle of any one of embodiments 1 to 22, wherein the viral particle comprises an IgG Fc stalk attached to a targeting moiety, e.g., the IgG Fc stalk is attached to the viral surface. 24. The viral particle of embodiment 22 or 23, wherein the IgG Fc stalk comprises a transmembrane domain, such as, but not limited to, a CD28 transmembrane domain. 25. The viral particle of embodiment 22, wherein the targeting moiety is attached to the viral surface via a polypeptide stalk. 26. The viral particle of any one of embodiments 1 to 25, wherein the targeting moiety binds to CD7. 27. The viral particle of embodiment 26, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising: (i) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 12, the heavy chain CDR2 has the amino acid sequence of SEQ ID NO: 13, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 14, or any variant thereof; and (ii) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 15, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 16, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 17, or any variant thereof. 28. The heavy chain comprises a heavy chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 24, and the polypeptide comprises an HCDR1 set forth in SEQ ID NO: 12, 28. The viral particle of embodiment 27, which maintains the amino acid sequences of HCDR2 set forth in SEQ ID NO: 13 and HCDR3 set forth in SEQ ID NO: 14. 29. The viral particle of embodiment 27 or 28, wherein the light chain comprises a light chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 25, and the polypeptide maintains the amino acid sequences of LCDR1 set forth in SEQ ID NO: 15, LCDR2 set forth in SEQ ID NO: 16, and LCDR3 set forth in SEQ ID NO: 17. 30. A viral particle according to any one of embodiments 27 to 29, comprising a heavy chain and a light chain, wherein the polypeptide comprises a heavy chain variable region of the heavy chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 24 and a light chain variable region of the light chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 25, and the polypeptide maintains the amino acid sequences of HCDR1 set forth in SEQ ID NO: 12, HCDR2 set forth in SEQ ID NO: 13, HCDR3 set forth in SEQ ID NO: 14, LCDR1 set forth in SEQ ID NO: 15, LCD2 set forth in SEQ ID NO: 16 and LCDR3 set forth in SEQ ID NO: 17. 31. The virus particle of any one of embodiments 27 to 30, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain that has at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 24, and a light chain variable region of the light chain that has at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 25. 32. The virus particle of any one of embodiments 27 to 31, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain that has at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 24, and a light chain variable region of the light chain that has at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 25. 33. The virus particle of any one of embodiments 27 to 32, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain that has at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 24, and a light chain variable region of the light chain that has at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 25. 34. A virus particle described in any one of embodiments 27 to 33, wherein the light chain and heavy chain comprise a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 24 and a light chain variable region comprising the amino acid sequence of SEQ ID NO: 25. 35. A viral particle described in any one of embodiments 27 to 34, wherein the heavy chain variable region and the light chain variable region are linked by a linker, such as a peptide linker, which may be, for example, a glycine / serine linker, or are not linked. 36. The peptide linker is (GGGGS) n (SEQ ID NO: 26), wherein n is independently 1 to 5. 37. The viral particle according to any one of embodiments 26 to 36, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 28, or the amino acid sequence set forth in SEQ ID NO: 28. 38. The viral particle of any one of embodiments 26 to 36, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 29, or the amino acid sequence set forth in SEQ ID NO: 29. 39. The viral particle of any one of embodiments 1 to 25, wherein the targeting moiety binds to CD8. 40. The viral particle of embodiment 39, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising: (i) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 32, the heavy chain CDR2 has the amino acid sequence of SEQ ID NO: 33, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 34, or any variant thereof; and (ii) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 35, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 36, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 37, or any variant thereof. 41. The viral particle of embodiment 40, wherein the heavy chain comprises a heavy chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 44, and the polypeptide maintains the amino acid sequences of HCDR1 set forth in SEQ ID NO: 32, HCDR2 set forth in SEQ ID NO: 33, and HCDR3 set forth in SEQ ID NO: 34. 42. The viral particle of embodiment 40 or 41, wherein the light chain comprises a light chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 45, and the polypeptide maintains the amino acid sequences of LCDR1 set forth in SEQ ID NO: 35, LCDR2 set forth in SEQ ID NO: 36, and LCDR3 set forth in SEQ ID NO: 37. 43. The viral particle according to any one of embodiments 40 to 42, comprising a heavy chain and a light chain, wherein the polypeptide comprises a heavy chain variable region of the heavy chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 44 and a light chain variable region of the light chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 45, and the polypeptide maintains the amino acid sequences of HCDR1 set forth in SEQ ID NO: 32, HCDR2 set forth in SEQ ID NO: 33, HCDR3 set forth in SEQ ID NO: 34, LCDR1 set forth in SEQ ID NO: 35, LCD2 set forth in SEQ ID NO: 36, and LCDR3 set forth in SEQ ID NO: 37. 44. The virus particle of any one of embodiments 40 to 43, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 44, and a light chain variable region of the light chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 45. 45. The virus particle of any one of embodiments 40 to 44, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain that has at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 44, and a light chain variable region of the light chain that has at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 45. 46. ​​The viral particle of any one of embodiments 40 to 45, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 44, and a light chain variable region of the light chain having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 45. 47. A virus particle described in any one of embodiments 40 to 46, wherein the light chain and heavy chain comprise a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 44 and a light chain variable region comprising the amino acid sequence of SEQ ID NO: 45. 48. A viral particle described in any one of embodiments 40 to 47, wherein the heavy chain variable region and the light chain variable region are linked by a linker, such as a peptide linker, which may be, for example, a glycine / serine linker, or are not linked. 49. The peptide linker is (GGGGS) n(SEQ ID NO: 26), wherein n is independently 1 to 5. 50. The viral particle according to any one of embodiments 39 to 49, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 46, or the amino acid sequence set forth in SEQ ID NO: 46. 51. The viral particle of any one of embodiments 39 to 49, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 47, or the amino acid sequence set forth in SEQ ID NO: 47. 52. A method for preparing a viral particle according to any one of embodiments 1 to 51, the method comprising transfecting or transducing a viral packaging cell with a nucleic acid molecule encoding the polypeptide and a nucleic acid molecule encoding the targeting moiety under conditions sufficient to produce the viral particle. 53. The method of embodiment 52, wherein the method further comprises transfecting or transducing the cells with a lentiviral transfer genome encoding a heterologous molecule of interest. 54. The method of embodiment 53, wherein the heterologous molecule of interest is an siRNA, shRNA, non-coding RNA (e.g., a guide RNA in a CRISPR system), a peptide, a polypeptide, a protein, a viral payload, a viral genome, or a combination thereof. 55. The method of embodiment 54, wherein the heterologous molecule of interest is a chimeric antigen receptor. 56. The method of embodiment 55, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO: 51. 57. The method of embodiment 55, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO: 52. 58. The method of any one of embodiments 52 to 57, wherein the method further comprises transfecting or transducing the cells with a nucleic acid molecule encoding gag-pol and / or rev. 59. The method of embodiment 52, wherein the cells express gag-pol and / or rev. 60. The method of any one of embodiments 52 to 59, wherein the cells are HEK293, such as HEK293T cells. 61. The method of any one of embodiments 52 to 60, wherein the method further comprises culturing the cells for at least 24 or 48 hours to produce virus. 62. The method of embodiment 61, wherein the method further comprises, but is not limited to, isolating the viral particles from the cell supernatant, such as by centrifugation. 63. A method for delivering a heterologous molecule to a target cell, the method comprising contacting the cell with a viral particle according to any one of embodiments 4 to 51. 64. The method of embodiment 63, wherein the target cell is a T cell, a B cell, an NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell, or an immune cell, such as, for example, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, an NKG2D+ natural killer cell, an SLC1A3+ astrocyte, or an SLC7A10+ adipocyte. 65. The targeting moiety is selected from the group consisting of CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed on acute leukemia or lymphoma but not on hematopoietic progenitor cells, a glycosylated CD43 epitope expressed on non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin l8.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also known as CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), mutant elongation factor 2 (ELF2M), ephrin B2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSH) R), Fos-related antigen 1, fucosyl-GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(ll)Cer), ganglioside GM3 (aNeu5Ac(2-3)bDClalp(l-4)bDGlcp(ll)Cer), GD3, GFR alpha 4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide moiety of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV-1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer-testis antigen 1 (MAD-CT-1), melanoma cancer-testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface-associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin-4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), and O-acetylglucosaminyltransferase V (O-acetylglucosaminyltransferase V). Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta-specific 1 (PLAC1), platelet-derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin-binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate-specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, kidney ubiquitous 1 (RU1), kidney ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF-beta R2, antigen recognized by TNT antibodies, thyroid-stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn 65. The method of embodiment 63 or 64, wherein the antibody binds to ag, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B-cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7-related (TEM7R), tumor protein p53 (p53), tumor-associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase-related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1) on said target cell. 66. The method of any one of embodiments 63 to 65, wherein the targeting moiety binds to CD7. 67. The method of embodiment 66, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 28, or the amino acid sequence set forth in SEQ ID NO: 28. 68. The method of embodiment 66, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 29, or the amino acid sequence set forth in SEQ ID NO: 29. 69. The method of any one of embodiments 63 to 65, wherein the targeting moiety binds to CD8. 70. The method of embodiment 69, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 46, or the amino acid sequence set forth in SEQ ID NO: 46. 71. The method of embodiment 69, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 47, or the amino acid sequence set forth in SEQ ID NO: 47. 72. A method for delivering a heterologous molecule to a target cell in a subject, the method comprising administering to the subject a viral particle described in any one of embodiments 4 to 51. 73. The method of embodiment 72, wherein the target cell is a T cell, a B cell, an NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell, or an immune cell, such as, for example, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD20+ cancer cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, an NKG2D+ natural killer cell, an SLC1A3+ astrocyte, or an SLC7A10+ adipocyte. 74. The targeting moiety is selected from the group consisting of CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed on acute leukemia or lymphoma but not on hematopoietic progenitor cells, a glycosylated CD43 epitope expressed on non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin l8.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also known as CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), mutant elongation factor 2 (ELF2M), ephrin B2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSH) R), Fos-related antigen 1, fucosyl-GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(ll)Cer), ganglioside GM3 (aNeu5Ac(2-3)bDClalp(l-4)bDGlcp(ll)Cer), GD3, GFR alpha 4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide moiety of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV-1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer-testis antigen 1 (MAD-CT-1), melanoma cancer-testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface-associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin-4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), and O-acetylglucosaminyltransferase V (O-acetylglucosaminyltransferase V). Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta-specific 1 (PLAC1), platelet-derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin-binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate-specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, kidney ubiquitous 1 (RU1), kidney ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF-beta R2, antigen recognized by TNT antibodies, thyroid-stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn 74. The method of embodiment 72 or 73, wherein the antibody binds to ag, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B-cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7-related (TEM7R), tumor protein p53 (p53), tumor-associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase-related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1) on said target cell. 75. The method of any one of embodiments 72 to 74, wherein the targeting moiety binds to CD7. 76. The method of embodiment 75, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 28, or the amino acid sequence set forth in SEQ ID NO: 28. 77. The method of embodiment 75, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 29, or the amino acid sequence set forth in SEQ ID NO: 29. 78. The method of any one of embodiments 72 to 74, wherein the targeting moiety binds to CD8. 79. The method of embodiment 78, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 46, or the amino acid sequence set forth in SEQ ID NO: 46. 80. The method of embodiment 78, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 47, or the amino acid sequence set forth in SEQ ID NO: 47. 81. The method of any one of embodiments 72 to 80, wherein the heterologous molecule is an siRNA, shRNA, non-coding RNA (e.g., guide RNA of a CRISPR system), peptide, polypeptide, protein, viral payload, viral genome, or a combination thereof, such as a chimeric antigen receptor ("CAR"). 82. The method of embodiment 81, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO: 51. 83. The method of embodiment 81, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO: 52. 84. A method for treating cancer in a subject, comprising administering to the subject a viral particle according to any one of embodiments 4 to 51. 85. The method of embodiment 84, wherein the heterologous molecule is a chimeric antigen receptor. 86. The method of embodiment 85, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO: 51. 87. The method of embodiment 85, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO: 52. 88. The method of any one of embodiments 84 to 87, wherein the target cells are T cells, B cells, NK cells, dendritic cells, neutrophils, macrophages, cancer cells, or immune cells such as, for example, CD3+ T cells, CD4+ T cells, CD7+ T cells, CD8+ T cells, CD19+ B cells, CD19+ cancer cells, CD20+ B cells, CD30+ lung epithelial cells, CD34+ hematopoietic stem cells, CD105+ endothelial cells, CD105+ hematopoietic stem cells, CD117+ hematopoietic stem cells, CD133+ cancer cells, EpCAM+ cancer cells, GluA2+ neurons, GluA4+ neurons, hematopoietic stem cells, hepatocytes, Her2 / Neu+ cancer cells, NKG2D+ natural killer cells, SLC1A3+ astrocytes, SLC7A10+ adipocytes. 89. The targeting moiety can be CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed on acute leukemia or lymphoma but not on hematopoietic progenitor cells, a glycosylated CD43 epitope expressed on non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin l8.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also known as CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), mutant elongation factor 2 (ELF2M), ephrin B2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSH) R), Fos-related antigen 1, fucosyl-GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(ll)Cer), ganglioside GM3 (aNeu5Ac(2-3)bDClalp(l-4)bDGlcp(ll)Cer), GD3, GFR alpha 4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide moiety of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV-1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer-testis antigen 1 (MAD-CT-1), melanoma cancer-testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface-associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin-4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), and O-acetylglucosaminyltransferase V (O-acetylglucosaminyltransferase V). Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta-specific 1 (PLAC1), platelet-derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin-binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate-specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, kidney ubiquitous 1 (RU1), kidney ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF-beta R2, antigen recognized by TNT antibodies, thyroid-stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn 89. The method of any one of embodiments 84-88, wherein the antibody binds to ag, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B-cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7-related (TEM7R), tumor protein p53 (p53), tumor-associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase-related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1) on said target cell. 90. The method of any one of embodiments 84-89, wherein the targeting moiety binds to CD7. 91. The method of embodiment 90, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 28, or the amino acid sequence set forth in SEQ ID NO: 28. 92. The method of embodiment 90, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 29, or the amino acid sequence set forth in SEQ ID NO: 29. 93. The method of any one of embodiments 84-89, wherein the targeting moiety binds to CD8. 94. The method of embodiment 93, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 46, or the amino acid sequence set forth in SEQ ID NO: 46. 95. The method of embodiment 93, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 47, or the amino acid sequence set forth in SEQ ID NO: 47. 96. The method of any one of embodiments 84-95, wherein the cancer is a cancer provided herein, such as a T-cell disorder or a B-cell disorder. 97. A viral particle comprising a targeting moiety, a polypeptide comprising a viral structural protein, and a nucleic acid molecule encoding a heterologous molecule of interest; the targeting moiety comprises an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:46, or SEQ ID NO:47; the polypeptide comprising a viral structural protein comprises an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2; the nucleic acid molecule encoding the heterologous molecule of interest encodes a chimeric antigen receptor; The viral particle, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:55, or SEQ ID NO:56. 98. A viral particle comprising a targeting moiety, a polypeptide comprising a viral structural protein, and a nucleic acid molecule encoding a heterologous molecule of interest; the targeting moiety comprises an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:46, or SEQ ID NO:47; the polypeptide comprising a viral structural protein comprises an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2; the nucleic acid molecule encoding the heterologous molecule of interest encodes a chimeric antigen receptor; The viral particle, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence that is at least 95% identical to the amino acid sequence of SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:55, or SEQ ID NO:56. 99. A viral particle comprising a targeting moiety, a polypeptide comprising a viral structural protein, and a nucleic acid molecule encoding a heterologous molecule of interest; the targeting moiety comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:46, or SEQ ID NO:47; the polypeptide comprising a viral structural protein comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2; the nucleic acid molecule encoding the heterologous molecule of interest encodes a chimeric antigen receptor; The viral particle, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence that is at least 98% identical to the amino acid sequence of SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:55, or SEQ ID NO:56. 100. The viral particle of any one of embodiments 97 to 99, wherein the chimeric antigen receptor comprises an antigen-binding domain comprising the amino acid sequence of SEQ ID NO: 51 or SEQ ID NO: 52. 101. A method for treating cancer in a subject in need thereof, comprising administering to the subject a viral particle according to any one of embodiments 97 to 100. 102. The method of embodiment 101, wherein the cancer is a cancer provided herein, such as a T-cell disorder or a B-cell disorder.

[0244] The following examples are illustrative, but not limiting, of the compounds, compositions, and methods described herein. Other suitable modifications and adaptations known to those skilled in the art are within the scope of the following embodiments. [Example]

[0245] Example 1: Spring viremia of carp virus G protein can promote cell-specific fusion.

[0246] method

[0247] Plasmid / sequence. All rhabdovirus GP sequences are codon-optimized and synthesized by Genscript.Sequences are shown below, and accession numbers are listed in the following table, Table 1, and are incorporated herein by reference in their entirety. [Table 11]

[0248] The targeting moiety comprises an anti-CD7 antibody (clone MT701, single-chain format) membrane-anchored via an IgG-based Fc stalk containing the CD28 transmembrane domain.

[0249] Cells. HEK293T cells were cultured in DMEM containing 10% FBS. SupT1 cells were maintained in RPMI medium containing 10% FBS. Human PBMCs were purchased from AllCells and cultured in X-Vivo 10 (Lonza) supplemented with 20 ng / mL IL-2 (Peprotech). PBMCs were activated using anti-CD3 / CD28 Dynabeads (Cell Therapy Systems) 48 hours before transduction.

[0250] Generation of lentiviral particles. Recombinant lentiviral particles co-expressing rhabdovirus G glycoprotein and binding molecules were generated by introducing plasmids into HEK293T cells using Lipofectamine 3000 (ThermoFisher Scientific). A total of five plasmids were transfected: (1) a plasmid expressing rhabdovirus G glycoprotein, (2) a plasmid expressing a binder protein (where indicated), (3) a plasmid expressing a lentiviral transfer genome encoding CAR20, (4) a plasmid expressing gag-pol, and (5) a plasmid expressing rev. Transfected cell supernatants were harvested 48 hours later. Virus in the cell supernatant was concentrated by centrifugation through a sucrose cushion and resuspended in x-vivo medium. Lentiviral particle titers were measured using the Lenti-X p24 Rapid Titer Kit (Takara Bio, San Jose, CA).

[0251] Lentiviral transduction assay. Serial 5-fold dilutions of concentrated lentivirus (in cell culture medium) were performed and used to infect SupT1 and activated human PBMCs. Medium was changed after 6 hours, and transduced cells were analyzed by flow cytometry on days 4 and 7 post-transduction. Cells were stained with a viability stain, an anti-CD7 antibody to detect CD7-positive cells, and an anti-CAR antibody to detect CAR20 expression as a measure of transduction efficiency.

[0252] result:

[0253] SVCV-G mediates fusion to human cells. Most non-mammalian rhabdovirus G proteins failed to mediate transduction in human cells, with the exception of spring viremia of carp virus G (SVCV-G). This glycoprotein did not target SupT1 or human PBMC cells by itself, as transduction was highly inefficient in the absence of a CD7 binder (approximately 1 log lower than blinded VSV-G I182E). CD7 binder-mediated targeted transduction reached titers comparable to those of retargeted VSV-G I182E.

[0254] This surprising and unexpected result indicates that viral structural proteins alone cannot infect immune cells, but that when the virus expresses a targeting moiety, such as an anti-CD7 scFv, it can be used to infect cells. This result was unexpected and is not due to the effect of the anti-CD7 scFv itself, as the presence of the anti-CD7 scFv targeting moiety was not sufficient to induce infection using other non-human rhabdovirus GP proteins. The data are presented in Figure 1.

[0255] Example 2: SVCV-G pseudotyped lentivirus carrying CD7 binders transduces PBMCs.

[0256] Human PBMC cells were maintained in X-Vivo 10 medium containing 5% human serum and 20 ng / mL human IL-2. Non-human primate cells were maintained in RPMI medium containing 10% FBS, 1% Pen / Strep, 1 mM sodium pyruvate, and 100 units / mL hIL-2. Concentrated lentivirus was used to infect human and non-human primate cells. The medium was changed after 24 hours, and transduced cells were analyzed by flow cytometry 7 days after transduction to determine CAR transduction. Two separate binder constructs were evaluated: a CD7 binder attached to the viral surface via the Fc domain and a CD7 binder attached to the viral surface via a polypeptide stalk as provided herein. For the CD7 binder attached to the viral surface via the Fc domain, CAR expression was observed in all human and non-human primate PBMCs evaluated (Figure 2A), compared to the binder alone, which showed no transduction (Figure 2B). Data are also presented as a function of CAR expression rate versus multiplicity of infection (Figure 2C). For CD7 binders attached to the viral surface via the polypeptide stalk, CAR expression was also observed in PBMCs from all human and non-human primates evaluated (Figure 3A), compared to binder alone, which showed no transduction (Figure 3B). Data are also presented as a function of CAR expression rate versus multiplicity of infection (Figure 3C).

[0257] The data in this example show that SVCV-G pseudotyped lentivirus can successfully transduce PBMCs utilizing binder constructs with variable viral attachment sequences, demonstrating the utility of SVCV-G for pseudotyping a variety of viral constructs.

[0258] Example 3: SVCV-G pseudotyped lentiviruses carrying CD7 binders show minimal off-target transduction.

[0259] Off-target transduction of B cells via SVCV-G pseudotyped lentiviral constructs utilizing a CD7 binder attached to the viral surface via the Fc domain was evaluated in several B cell populations. B cells were maintained in X-Vivo10 medium containing 5% human serum and 20 ng / mL human IL-2. Non-human primate cells were maintained in RPMI medium containing 10% FBS, 1% Pen / Strep, 1 mM sodium pyruvate, and 100 units / mL hIL-2. Concentrated lentivirus was used to infect various B cell populations. The medium was changed after 24 hours, and transduced cells were analyzed by flow cytometry 5 days after transduction to determine GFP transduction. As a control, SupT1 cells were also infected with the same lentiviral construct. None of the B cell populations evaluated showed significant levels of GFP expression (Figure 4A). At the highest lentiviral concentration used, the percentage of GFP-positive cells in the DB line only exceeded 1%.

[0260] Lentiviral constructs delivering the CAR20-T2A-GFP transgene were also evaluated in a similar manner (Figure 4B). SVCV-G pseudotyped lentivirus demonstrated minimal off-target transduction of B cells in five of the six cell populations evaluated. At the highest lentivirus concentration used, the percentage of CAR-T2A-GFP-positive cells in the HT line only exceeded 1%.

[0261] As provided herein, we also evaluated off-target transduction of B cells via SVCV-G pseudotyped lentiviral constructs utilizing a CD7 binder attached to the viral surface via a polypeptide stalk. In GFP transduction experiments, none of the evaluated B cell populations exhibited significant levels of GFP expression (Figure 5A). In CAR20-T2A-GFP transduction experiments, SVCV-G pseudotyped lentivirus demonstrated minimal off-target transduction of B cells in five of the six evaluated cell populations (Figure 5B). At none of the lentiviral concentrations used, the percentage of CAR-T2A-GFP-positive cells in Daudi, GA10, HT, Raji, or Ramos cell lines exceeded 1%. Transduction of the B cell line DB exceeded 1% at the two highest lentiviral concentrations used, but still remained lower than that of the control SupT1 cell line.

[0262] The data in this example demonstrate that SVCV-G pseudotyped lentiviral constructs minimize off-target transduction of B cells, and delivery of the CAR20 transgene instead of the GFP transgene does not significantly increase off-target transduction in B cells.

[0263] Reference is made herein to various sequences as set forth herein and below. Carp Spring Viremia Virus-G (SEQ ID NO: 1 - including leader sequence): MSIISYIAFLLLIDSNLGIPIFVPSGRNISWQPVIQPFDYQCPIHGNLPNTMGLSATKLTIKSPSVFSTDKVSGWICHAAEWKTTCDYRWYGPQYITHSIHPISPTIDECRRIIQRIASGTDEDDLGF PPQSCGWASVTTVSNTNYRVVPHSVHLEPYGGHWIDHEFNGGECREKVCEMKGNHSIWITEETVQHECAKHIEEVEGIMYGNVPRGDVMYANNFIIDRHHRVYRFGGSCQMKFCNKDGIKFARGDWV EKTAGTLTTIHDNVPKCVDGTLVSGHRPGLDLIDTVFNLENVVEYTLCEGTKRKINKQEKLTSVDLSYLAPRIGGFGSVFRVRNGTLERGSTTYIRIEVEGPIVDSLNGTDPRTNASRVFWDDWELD GNIYQGFNGVYKGKDGKIHIPLNMIESGIIDDELQHAFQADIIPHPHYDDDEIREDDIFFDNTGENGNPVDAVVEWVSGWGTSLKFFGMTLVALILIFLLIRCCVACTYLMKRSKRPATESHEMRSLV Carp Spring Viremia Virus-G (SEQ ID NO: 2 - no leader sequence): IPIFVPSGRNISWQPVIQPFDYQCPIHGNLPNTMGLSATKLTIKSPSVFSTDKVSGWICHAAEWKTTCDYRWYGPQYITHSIHPISPTIDECRRIIQRIASGTDEDLGFPPQSCGWASVTTVSNTNYRVVPHSVHLEPYGGHWIDHEFNGGECREKVCEMKGNHSIWITEETVQHECAKHIEEVEGIMYGNVPRGDVMYANNFIIDRHHRVYRFGGSCQMKFCNKDGIKFARGDWVEKTAGTLTT IHDNVPKCVDGTLVSGHRPGLDLIDTVFNLENVVEYTLCEGTKRKINKQEKLTSVDLSYLAPRIGGFGSVFRVRNGTLERGSTTYIRIEVEGPIVDSNLGTDPRTNASRVFWDDWELDGNIYQGFNGVYKGKDGKIHIPLNMIESGIIDDELQHAFQADIIPHPHYDDDEIREDDIFFDNTGENPVDAVVEWVSGWGTSLKFFGMTLVALILIFLLIRCCVACTYLMKRSKRPATESHEMRSLV VSV-G I182E: MKCLLYLAFLFIGVNCKFTIVFPHNQKGNWKNVPSNYHYCPSSSDLNWHNDLIGTALQVKMPKSHKAIQADGWMCHASKWVTTCDFRWYGPKYITHSIRSFTPSVEQCKESIEQTKQGTWLNPGFPP QSCGYATVTDAEAVIVQVTPHHVLVDEYTGEWVDSQFINGKCSNYICPTVHNSTTWHSDYKVKGLCDSNLESMDITFFSEDGELSSLGKEGTGFRSNYFAYETGGKACKMQYCKHWGVRLPSGVWFEM ADKDLFAAARFPECPEGSSISAPSQTSVDVSLIQDVERILDYSLCQETWSKIRAGLPISPVDLSYLAPKNPGTGPAFTIINGTLKYFETRYIRVDIAAPILSRMVGMISGTTTERELWDDWAPYEDVE IGPNGVLRTSSGYKFPLYMIGHGMLDSDLHLSSKAQVFEHPHIQDAASQLPDDESLFFGDTGLSKNPIELVEGWFSSWKSSIASFFFIIGLIIGLFLVLRVGIHLCIKLKHTKKRQIYTDIEMNRLGK Perthyrhabdovirus-G (SEQ ID NO: 4): MNTLIKILLIIIILREARSHIVLVPLDLGDWRTTEADQLDCPPMHGDLSNQGTQAIELEYHTASWGLKNNIAGSLCVTAKWSITCDYRWYGSKYISTVIEYLPTTPEMCKEAKRASDRGESLAPHFPTEN CGWNNVLTESQEFTTLTSHPVKLDAYSFILIDSMFEGGRCQSKECPVVFHQGMWIADQEAFGFCKDLDKHRGLLFKTGLRNSLGEIVRQEWNLNSVFQPEIGREKHFKGACKMSYCGNSGVRFSDREWFQ LGTPSDNGIKKIIIEGLPECGEDNLIHSHDTSNTLKELAEHVDEIALNAICLQEVRRARDTKAVSDWLLSMMSPFSEGIGKVYRIHKGRLESTVGFYRKVVLEGDGTPERLGVGLDKKPVSWDQFVVKTND TRIQSMFNGNTVVNGKIKWVKNVLGAHILDEISALEFDVPLIPHPHLDGLKFNESHTISSHHPNGKGVNFVESVTHWAGGLWESIGSSAVIIVVLLICAFVAVKFCQRLIPSRRPPTRESSENVFMLRTV Drosophila obscura sigma virus 10A-G (SEQ ID NO: 5): MKKTTEFTWPLKMYSSKFLLVTLSILVPRVISLFLPDYNPELFKPAVIHKLTCPNLSATSQINKYASMDTIYVNLGRPKPNFKVTVEGYLCTKIVLQTVCEAFLFSANEVNHIRKEAPIDKSECDSAIYRFIKGDVIDETFL PDYFSGYKRTVRQRIYIKVITHEVSYDPYLEKYVDSWFPGGATPYNYSTTIHDSTLWKMKGQKPPCTDFETINGEYTVLPDPKDLEHPLRFIWALGIKEKSYKNSCVVKFCGRPGILFEDGEWFSISTPESPTNYDVFITNLP ACNSSASIKTRTVEQEMDAEFSNEYQLNLRFWCMEVLQGLTSGSILPQYKLAFLTQNSPGLGNVYKILNGTLMVTVGHYKKVKLNQLDSLHEIGADDAGNPVYVTDTQLTPGPIPDSYEWINGLVFSDKRWSIPLVDLVRNNL DNLLTMPLKLQAIEHSAASFMSASSSHLIEGDVITQYGGPTSKHDNWFVNYTTKSWEWLHWIVYIGVIVGGIFVLIILEKLGCYKIVYYLLKKLCQSKSSKKTKQPKVEYKKASSNQAQQIESRHEVIPQEDSVIVSLDRFDW Fall armyworm virus-G (SEQ ID NO: 6): MVFLSLSTIIFILSLRAVTCSNPLSYPNGILTNNSTNHPLSDFYIFYENSSLTYTQFPVAPDCSSILDTRDEQYPTTVTLWKVDQESQAEWGLLLWQERIDTTCSWNFWGNYKGSIVSKSSVPLKDIPSGSARNGYWALSNDEVQEIDHVP YNLRYYCYWCRNEYPGSFYMRYVKKVRIIRNPDGSIKTPRGSWVHELDNLWGDQMRYLVIRRFGGESSCPLKIYDVRAGVLSKSRSNFILVSLPSLNLQFSVSLESTETKCSFGDKTYDIVQSMGYLLSIDIGNANWRGPWDPTPQHPGRER RSIMEFPDQTSFRYNQFINYHSSPRHKRHDQEFEFPLSLKSSYDYAQFRYEQNFIIRQINKNFGLLQKSICDIQFSKWQNLSPPNLAMKIAHYVTGSIHSIGGVHHGSYSIQRTEKSITKVNLVFPIVIVHGMYCQREPSKEVVWAEPVTG ILFKSPIPTHFSLSSSWLPGVNGSSIVPLTGQILLPEITMDHLEVVQQVEAKMVKSMYTNVELFGSTEEFQRYQTQGITSDEQSNTVNPWIGLLIHGGVSIATGILVALLIPSILKLFRHIIEKGEASLEERLHLRETSRKEFVKVRGKPWGV Virus 7-G MFPSIFFCLMLLVMTSSVGQFILPIKEITPPRPINEHHLSCRLGPGALYPTTSSSVVVRSIHPDSNPVPIQGYLCSKKEYTLTCSENFLWMETVKKDSRSVPVTPSECVDAVNSWLQDKLDKDTQLTKDCG WMSTNTVKKEIFDIQGKHVRLNPYEMEYIDEILHRGKCSSKICQTKYADMLWVSEGDLNQTCPKMIGADVRMSLGDQKTPSSVILHSNYVPGVSLEGACRDFSFCGHRGMVLRTGHFVVVSSDFPSTIVKM YNLFQVCQKDLTIVSDNMNSEITSSKLDLMKIFLLDKCQQVVARIKGGLSVTRYDLGFLSPQISGVGSGYVASNRSVLVGQYKYMLVHSYVANCHSCRSCVINAVTDEGVIPVHLTPDQCPCANFNGCYL PNGIKVYKDKVYNPLLDIDEEFYHQMTEVELNPNYISHPKDVKETFLSLPATEEVEQHHGRTLDSVVGSLVPDFSFSIWPYFVGLGALVIIIIILWRRRSYKPAEAPIRDFPVIYTPQSSFGPIAQIRWN

[0264] The disclosures of all patents, patent applications, and publications cited herein are incorporated herein by reference in their entirety. While various embodiments are disclosed with reference to particular aspects, it will be apparent that other aspects and modifications of these embodiments may be devised by those skilled in the art without departing from the true spirit and scope of the embodiments. The appended claims are intended to be construed to include all such aspects and equivalent variations.

Claims

1. 1. A viral particle comprising a targeting moiety and a polypeptide comprising a viral structural protein comprising an amino acid sequence that is at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical to the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:

2.

2. The viral particle of claim 1 , wherein the viral structural protein comprises a polypeptide comprising the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:

2.

3. The viral particle of claim 1 or 2, wherein the viral particle is a pseudotyped lentivirus.

4. The viral particle according to any one of claims 1 to 3, further comprising a nucleic acid molecule encoding a heterologous molecule of interest.

5. 5. The viral particle of claim 4, wherein the heterologous molecule of interest is an siRNA, shRNA, a non-coding RNA (e.g., a guide RNA of the CRISPR system), a peptide, a polypeptide, a protein, a viral payload, a viral genome, or a combination thereof.

6. The viral particle of claim 4 or 5, wherein the heterologous molecule of interest is a chimeric antigen receptor ("CAR").

7. 7. The viral particle of claim 6, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:

51.

8. The viral particle of claim 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 90% identity to SEQ ID NO:

51.

9. The viral particle of claim 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 95% identity to SEQ ID NO:

51.

10. The viral particle of claim 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 98% identity to SEQ ID NO:

51.

11. The viral particle of claim 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 99% identity to SEQ ID NO:

51.

12. The viral particle of claim 7, wherein the CAR comprises an antigen-binding domain having an amino acid sequence of SEQ ID NO:

51.

13. 7. The viral particle of claim 6, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:

52.

14. The viral particle of claim 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 90% identity to SEQ ID NO:

52.

15. The viral particle of claim 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 95% identity to SEQ ID NO:

52.

16. The viral particle of claim 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 98% identity to SEQ ID NO:

52.

17. The viral particle of claim 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having at least 99% identity to SEQ ID NO:

52.

18. The viral particle of claim 13, wherein the CAR comprises an antigen-binding domain having an amino acid sequence having the amino acid sequence of SEQ ID NO:

52.

19. 19. The viral particle of any one of claims 1 to 18, wherein the targeting moiety binds to a T cell, a B cell, a NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell or an immune cell such as, for example, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD20+ cancer cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, a NKG2D+ natural killer cell, a SLC1A3+ astrocyte, a SLC7A10+ adipocyte.

20. The targeting moiety can be any of the following: CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed in acute leukemias or lymphomas but not in hematopoietic progenitor cells, a glycosylated CD43 epitope expressed in non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie1, Tie2, Tie3, Tie4, Tie5, Tie6, Tie7, Tie8, Tie9, Tie10, Tie11, Tie12, Tie13, Tie14, Tie15, Tie16, Tie17, Tie18, Tie19, Tie20, Tie21, Tie22, Tie23, Tie24, Tie25, Tie26, Tie27, Tie28, Tie29, Tie30, Tie31, Tie32, Tie33, Tie34, Tie35, Tie36, Tie37, Tie38, Tie39 ...9, Tie39, Tie39, 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (like BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin 18.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also called CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), elongation factor 2 mutant (ELF2M), ephrinB2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSHR ), Fos-related antigen 1, fucosyl GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer), ganglioside GM3 (a Neu5Ac(2-3)bDCLarlp(l-4)bDGlcp(l-l)Cer), GD3, GFRalpha4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), Hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide portion of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer testis antigen 1 (MAD-CT-1), melanoma cancer testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin 4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), ... Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta specific 1 (PLAC1), platelet derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, renal ubiquitous 1 (RU1), renal ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF beta R2, antigen recognized by TNT antibodies, thyroid stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn 20. The virus particle of any one of claims 1 to 19, which binds to TNF receptor family member B cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7 related (TEM7R), tumor protein p53 (p53), tumor associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1).

21. 21. The viral particle of any one of claims 1 to 20, wherein the targeting moiety is an antibody, an scFv antibody, an antigen binding domain, ankyrin repeats (e.g. DARPIN), a VHH domain antibody, a nanobody, a single domain antibody, an FN3 domain or any combination thereof.

22. The targeting moiety comprises IgG Fc stalk, Polypeptide stalk, envelope glycoprotein G or H of a Paramyxoviridae virus, such as a Morbillivirus, such as the Measles virus, or a Henipavirus, such as the Nipah virus, the Cedar virus, or the Hendra virus; glycoproteins of Rhabdoviridae viruses such as New Jersey vesicular stomatitis virus, vesicular stomatitis Indiana virus, vesicular stomatitis Alagoas virus, vesicular stomatitis Maraba virus, vesicular stomatitis Carajas virus, parainfluenza virus, Fall armyworm rhabdovirus isolate Sf G, Drosophila obscura sigma virus 10A, Wuhan insect virus 7, Perch virus, or spring viremia of carp virus; glycoproteins of Filoviridae viruses, such as Ebola virus, or 22. The virus particle according to any one of claims 1 to 21, which is attached to the viral surface via a glycoprotein of an Arenaviridae virus, such as Machupo virus.

23. 23. The viral particle of any one of claims 1 to 22, wherein the viral particle comprises an IgG Fc stalk linked to a targeting moiety, e.g. the IgG Fc stalk is attached to the viral surface.

24. 24. The viral particle of claim 22 or 23, wherein the IgG Fc stalk comprises a transmembrane domain, such as, but not limited to, a CD28 transmembrane domain.

25. The viral particle of claim 22, wherein the targeting moiety is attached to the viral surface via a polypeptide stalk.

26. The viral particle of any one of claims 1 to 25, wherein the targeting moiety binds to CD7.

27. 27. The viral particle of claim 26, wherein the targeting moiety that binds CD7 comprises a polypeptide comprising: (i) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 12, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 13, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 14, or any variant thereof; and (ii) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 15, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 16, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 17, or any variant thereof.

28. The viral particle of claim 27, wherein the heavy chain comprises a heavy chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 24, and the polypeptide maintains the amino acid sequences of HCDR1 set forth in SEQ ID NO: 12, HCDR2 set forth in SEQ ID NO: 13, and HCDR3 set forth in SEQ ID NO:

14.

29. The viral particle described in claim 27 or 28, wherein the light chain comprises a light chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 25, and the polypeptide maintains the amino acid sequences of LCDR1 set forth in SEQ ID NO: 15, LCDR2 set forth in SEQ ID NO: 16, and LCDR3 set forth in SEQ ID NO:

17.

30. 30. The viral particle of any one of claims 27 to 29, wherein the polypeptide comprises a heavy chain and a light chain, the heavy chain comprising a heavy chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 24 and a light chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 25, and the polypeptide maintains the amino acid sequences of HCDR1 set forth in SEQ ID NO: 12, HCDR2 set forth in SEQ ID NO: 13, HCDR3 set forth in SEQ ID NO: 14, LCDR1 set forth in SEQ ID NO: 15, LCD2 set forth in SEQ ID NO: 16 and LCDR3 set forth in SEQ ID NO:

17.

31. The viral particle according to any one of claims 27 to 30, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 90% sequence identity with the amino acid sequence of SEQ ID NO: 24 and a light chain variable region of the light chain having at least 90% sequence identity with the amino acid sequence of SEQ ID NO:

25.

32. The viral particle according to any one of claims 27 to 31, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 95% sequence identity with the amino acid sequence of SEQ ID NO: 24 and a light chain variable region of the light chain having at least 95% sequence identity with the amino acid sequence of SEQ ID NO:

25.

33. The viral particle according to any one of claims 27 to 32, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 24 and a light chain variable region of the light chain having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:

25.

34. The virus particle according to any one of claims 27 to 33, wherein the light and heavy chains comprise a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 24 and a light chain variable region comprising the amino acid sequence of SEQ ID NO:

25.

35. 35. The viral particle of any one of claims 27 to 34, wherein the heavy chain variable region and the light chain variable region are linked by a linker, such as a peptide linker, which may be, for example, a glycine / serine linker, or are not linked.

36. The peptide linker is (GGGGS) ｎ (SEQ ID NO: 26), wherein n is independently 1 to 5.

37. 37. The viral particle of any one of claims 26 to 36, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:28, or the amino acid sequence set forth in SEQ ID NO:

28.

38. 37. The viral particle of any one of claims 26 to 36, wherein the targeting moiety that binds to CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:29, or the amino acid sequence set forth in SEQ ID NO:

29.

39. The viral particle of any one of claims 1 to 25, wherein the targeting moiety binds to CD8.

40. 40. The viral particle of claim 39, wherein the targeting moiety that binds CD8 comprises a polypeptide comprising: (i) a heavy chain variable region comprising heavy chain CDR1, CDR2, and CDR3 sequences, wherein the heavy chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 32, the heavy chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 33, and the heavy chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 34, or any variant of the foregoing; and (ii) a light chain variable region comprising light chain CDR1, CDR2, and CDR3 sequences, wherein the light chain CDR1 sequence has the amino acid sequence of SEQ ID NO: 35, the light chain CDR2 sequence has the amino acid sequence of SEQ ID NO: 36, and the light chain CDR3 sequence has the amino acid sequence of SEQ ID NO: 37, or any variant of the foregoing.

41. The viral particle of claim 40, wherein the heavy chain comprises a heavy chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 44, and the polypeptide maintains the amino acid sequences of HCDR1 set forth in SEQ ID NO: 32, HCDR2 set forth in SEQ ID NO: 33, and HCDR3 set forth in SEQ ID NO:

34.

42. The viral particle of claim 40 or 41, wherein the light chain comprises a light chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 45, and the polypeptide maintains the amino acid sequences of LCDR1 set forth in SEQ ID NO: 35, LCDR2 set forth in SEQ ID NO: 36, and LCDR3 set forth in SEQ ID NO:

37.

43. The viral particle of any one of claims 40 to 42, wherein the polypeptide comprises a heavy chain and a light chain, the heavy chain comprising a heavy chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 44 and a light chain variable region having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 45, and the polypeptide maintains the amino acid sequences of HCDR1 set forth in SEQ ID NO: 32, HCDR2 set forth in SEQ ID NO: 33, HCDR3 set forth in SEQ ID NO: 34, LCDR1 set forth in SEQ ID NO: 35, LCD2 set forth in SEQ ID NO: 36 and LCDR3 set forth in SEQ ID NO:

37.

44. The viral particle according to any one of claims 40 to 43, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 44 and a light chain variable region of the light chain having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:

45.

45. The viral particle according to any one of claims 40 to 44, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 44 and a light chain variable region of the light chain having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:

45.

46. The viral particle according to any one of claims 40 to 45, wherein the light and heavy chains comprise a heavy chain variable region of the heavy chain having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 44 and a light chain variable region of the light chain having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:

45.

47. The virus particle according to any one of claims 40 to 46, wherein the light and heavy chains comprise a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 44 and a light chain variable region comprising the amino acid sequence of SEQ ID NO:

45.

48. 48. The viral particle of any one of claims 40 to 47, wherein the heavy chain variable region and the light chain variable region are linked by a linker, such as a peptide linker, which may be, for example, a glycine / serine linker, or are not linked.

49. The peptide linker is (GGGGS) ｎ The viral particle of claim 48, comprising the sequence of (SEQ ID NO: 26), wherein n is independently 1 to 5.

50. 50. The viral particle of any one of claims 39 to 49, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 46, or the amino acid sequence set forth in SEQ ID NO:

46.

51. 50. The viral particle of any one of claims 39 to 49, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 47, or the amino acid sequence set forth in SEQ ID NO:

47.

52. 52. A method for preparing a viral particle according to any one of claims 1 to 51, said method comprising transfecting or transducing a nucleic acid molecule encoding said polypeptide and a nucleic acid molecule encoding said targeting moiety into a viral packaging cell under conditions sufficient to produce said viral particle.

53. 53. The method of claim 52, wherein the method further comprises transfecting or transducing the cell with a lentiviral transfer genome encoding a heterologous molecule of interest.

54. 54. The method of claim 53, wherein the heterologous molecule of interest is an siRNA, shRNA, a non-coding RNA (e.g., a guide RNA of the CRISPR system), a peptide, a polypeptide, a protein, a viral payload, a viral genome, or a combination thereof.

55. 55. The method of claim 54, wherein the heterologous molecule of interest is a chimeric antigen receptor.

56. 56. The method of claim 55, wherein the chimeric antigen receptor comprises an antigen binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO:

51.

57. 56. The method of claim 55, wherein the chimeric antigen receptor comprises an antigen binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO:

52.

58. 58. The method of any one of claims 52 to 57, wherein the method further comprises transfecting or transducing the cell with a nucleic acid molecule encoding gag-pol and / or rev.

59. The method of claim 52, wherein the cells express gag-pol and / or rev.

60. 60. The method of any one of claims 52 to 59, wherein the cell is a HEK293, such as a HEK293T cell.

61. 61. The method of any one of claims 52 to 60, wherein the method further comprises culturing the cells for at least 24 or 48 hours to produce virus.

62. 62. The method of claim 61, further comprising isolating the viral particles from the cell supernatant, such as by centrifugation, but not limited to this.

63. A method for delivering a heterologous molecule to a target cell, said method comprising contacting said cell with a viral particle according to any one of claims 4 to 51.

64. 64. The method of claim 63, wherein the target cell is a T cell, a B cell, an NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell, or an immune cell such as, for example, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, a NKG2D+ natural killer cell, a SLC1A3+ astrocyte, a SLC7A10+ adipocyte.

65. The targeting moiety can be any of the following: CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed in acute leukemias or lymphomas but not in hematopoietic progenitor cells, a glycosylated CD43 epitope expressed in non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie1, Tie2, Tie3, Tie4, Tie5, Tie6, Tie7, Tie8, Tie9, Tie10, Tie11, Tie12, Tie13, Tie14, Tie15, Tie16, Tie17, Tie18, Tie19, Tie20, Tie21, Tie22, Tie23, Tie24, Tie25, Tie26, Tie27, Tie28, Tie29, Tie30, Tie31, Tie32, Tie33, Tie34, Tie35, Tie36, Tie37, Tie38, Tie39 ...9, Tie39, Tie39, 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (like BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin 18.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also called CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), elongation factor 2 mutant (ELF2M), ephrinB2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSHR ), Fos-related antigen 1, fucosyl GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer), ganglioside GM3 (a Neu5Ac(2-3)bDCLarlp(l-4)bDGlcp(l-l)Cer), GD3, GFRalpha4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), Hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide portion of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer testis antigen 1 (MAD-CT-1), melanoma cancer testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin 4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), ... Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta specific 1 (PLAC1), platelet derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, renal ubiquitous 1 (RU1), renal ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF beta R2, antigen recognized by TNT antibodies, thyroid stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn ag, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7 related (TEM7R), tumor protein p53 (p53), tumor associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1) on the target cell.

66. The method of any one of claims 63 to 65, wherein the targeting moiety binds to CD7.

67. 67. The method of claim 66, wherein the targeting moiety that binds CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:28, or the amino acid sequence set forth in SEQ ID NO:

28.

68. 67. The method of claim 66, wherein the targeting moiety that binds CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:29, or the amino acid sequence set forth in SEQ ID NO:

29.

69. The method of any one of claims 63 to 65, wherein the targeting moiety binds to CD8.

70. 70. The method of claim 69, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:46, or the amino acid sequence set forth in SEQ ID NO:

46.

71. 70. The method of claim 69, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:47, or the amino acid sequence set forth in SEQ ID NO:

47.

72. A method for delivering a heterologous molecule to a target cell in a subject, the method comprising administering to the subject a viral particle according to any one of claims 4 to 51.

73. 73. The method of claim 72, wherein the target cell is a T cell, a B cell, an NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell, or an immune cell such as, for example, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD20+ cancer cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, a NKG2D+ natural killer cell, a SLC1A3+ astrocyte, a SLC7A10+ adipocyte.

74. The targeting moiety can be any of the following: CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed in acute leukemias or lymphomas but not in hematopoietic progenitor cells, a glycosylated CD43 epitope expressed in non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie1, Tie2, Tie3, Tie4, Tie5, Tie6, Tie7, Tie8, Tie9, Tie10, Tie11, Tie12, Tie13, Tie14, Tie15, Tie16, Tie17, Tie18, Tie19, Tie20, Tie21, Tie22, Tie23, Tie24, Tie25, Tie26, Tie27, Tie28, Tie29, Tie30, Tie31, Tie32, Tie33, Tie34, Tie35, Tie36, Tie37, Tie38, Tie39 ...9, Tie39, Tie39, 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (like BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin 18.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also called CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), elongation factor 2 mutant (ELF2M), ephrinB2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSHR ), Fos-related antigen 1, fucosyl GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer), ganglioside GM3 (a Neu5Ac(2-3)bDCLarlp(l-4)bDGlcp(l-l)Cer), GD3, GFRalpha4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), Hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide portion of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer testis antigen 1 (MAD-CT-1), melanoma cancer testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin 4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), ... Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta specific 1 (PLAC1), platelet derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, renal ubiquitous 1 (RU1), renal ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF beta R2, antigen recognized by TNT antibodies, thyroid stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn ag, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7 related (TEM7R), tumor protein p53 (p53), tumor associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1) on the target cell.

75. The method of any one of claims 72 to 74, wherein the targeting moiety binds to CD7.

76. 76. The method of claim 75, wherein the targeting moiety that binds CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:28, or the amino acid sequence set forth in SEQ ID NO:

28.

77. 76. The method of claim 75, wherein the targeting moiety that binds CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:29, or the amino acid sequence set forth in SEQ ID NO:

29.

78. The method of any one of claims 72 to 74, wherein the targeting moiety binds to CD8.

79. 79. The method of claim 78, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:46, or the amino acid sequence set forth in SEQ ID NO:

46.

80. 79. The method of claim 78, wherein the targeting moiety that binds CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:47, or the amino acid sequence set forth in SEQ ID NO:

47.

81. 81. The method of any one of claims 72-80, wherein the heterologous molecule is an siRNA, shRNA, non-coding RNA (e.g. guide RNA of the CRISPR system), peptide, polypeptide, protein, viral payload, viral genome, or combinations thereof, such as a chimeric antigen receptor ("CAR").

82. 82. The method of claim 81, wherein the chimeric antigen receptor comprises an antigen binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO:

51.

83. 82. The method of claim 81, wherein the chimeric antigen receptor comprises an antigen binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO:

52.

84. 52. A method of treating cancer in a subject, comprising administering to the subject a viral particle according to any one of claims 4 to 51.

85. 85. The method of claim 84, wherein the heterologous molecule is a chimeric antigen receptor.

86. 86. The method of claim 85, wherein the chimeric antigen receptor comprises an antigen binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO:

51.

87. 86. The method of claim 85, wherein the chimeric antigen receptor comprises an antigen binding domain having an amino acid sequence having at least 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the amino acid sequence of SEQ ID NO:

52.

88. 88. The method of any one of claims 84 to 87, wherein the target cell is a T cell, a B cell, a NK cell, a dendritic cell, a neutrophil, a macrophage, a cancer cell, or an immune cell such as, for example, a CD3+ T cell, a CD4+ T cell, a CD7+ T cell, a CD8+ T cell, a CD19+ B cell, a CD19+ cancer cell, a CD20+ B cell, a CD30+ lung epithelial cell, a CD34+ hematopoietic stem cell, a CD105+ endothelial cell, a CD105+ hematopoietic stem cell, a CD117+ hematopoietic stem cell, a CD133+ cancer cell, an EpCAM+ cancer cell, a GluA2+ neuron, a GluA4+ neuron, a hematopoietic stem cell, a hepatocyte, a Her2 / Neu+ cancer cell, a NKG2D+ natural killer cell, a SLC1A3+ astrocyte, a SLC7A10+ adipocyte.

89. The targeting moiety can be any of the following: CD7, CD8, cKit (CD117), CD4, CD3, CD5, CD6, CD2, TCR alpha, TCR beta, TCR gamma, TCR delta, CD10, CD34, CD110, CD33, CD14, CD68, CCR7, CD62L, CD25, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, or CXCR3, a glycosylated CD43 epitope expressed in acute leukemias or lymphomas but not in hematopoietic progenitor cells, a glycosylated CD43 epitope expressed in non-hematopoietic cancers, kinase anchor protein 4 (AKAP-4), adrenoceptor beta 3 (ADRB3), AFP, anaplastic lymphoma kinase (ALK), androgen receptor, angiopoietin-binding cell surface receptor 2 (Tie1, Tie2, Tie3, Tie4, Tie5, Tie6, Tie7, Tie8, Tie9, Tie10, Tie11, Tie12, Tie13, Tie14, Tie15, Tie16, Tie17, Tie18, Tie19, Tie20, Tie21, Tie22, Tie23, Tie24, Tie25, Tie26, Tie27, Tie28, Tie29, Tie30, Tie31, Tie32, Tie33, Tie34, Tie35, Tie36, Tie37, Tie38, Tie39 ...9, Tie39, Tie39, 2), autoantibodies to desmoglein 1 (Dsgl), autoantibodies to desmoglein 3 (Dsg3), B7H3 (CD276), biotin, bone marrow stromal cell antigen 2 (BST2), BST1 / CD157, cancer / testis antigen 1 (NY-ESO-1), cancer / testis antigen 2 (LAGE-la), carbonic anhydrase IX (CA1X), carcinoembryonic antigen (CEA), CCCTC-binding factor (zinc finger protein)-like (like BORIS or regulator of imprinted sites), CCR4, CD5, CD19, CD20, CD22, CD24, CD30, CD3 2 (FCGR2A), CD33, CD34, CD38, CD44v6, CD72, CD79a, CD79b, CD97, CD99, CD123, CD171, CD179a, CD179b-IGLll, CD200R, CD276 / B7H3, CD300 molecule-like family member f (CD300LF), CDH1-CD324, CDH6, CDH17, CDH19, chromosome X open reading frame 61 (CXORF61), claudin 6 (CLDN6), claudin 18.2 (CLD18A2 or CLDN18A.2), CMVpp65, C-MYC epitope tag, Cripto, CS1 (also called CD2 subset 1 or CRACC or SLAMF7 or CD319 or 19A24), CSF2RA (GM-CSFR-alpha), C-type lectin domain family 12 member A (CLEC12A), C-type lectin-like molecule 1 (CLL-1 or CLECL1), cyclin B1, cytochrome P450 IB 1 (CYP1B 1), DLL3, EBV-EBNA3c, EGF-bke module-containing mucin-like hormone receptor-like 2 (EMR2), elongation factor 2 mutant (ELF2M), ephrinB2, ephrin type A receptor 2 (EphA2), epidermal growth factor receptor (EGFR), epidermal growth factor receptor variant III (EGFRviii), epithelial cell adhesion molecule (EPCAM), ERG, ETS translocation mutant gene 6 located on chromosome 12p (ETV6-AML), Fc fragment of IgA receptor (FCAR or CD89), Fc receptor-like 5 (FCRL5), fibroblast activation protein alpha (FAP), FITC, Fms-like tyrosine kinase 3 (FLT3), folate receptor alpha (FRa or FR1), folate receptor beta (FRb), follicle-stimulating hormone receptor (FSHR ), Fos-related antigen 1, fucosyl GMl, G protein-coupled receptor class C group 5 member D (GPRC5D), G protein-coupled receptor 20 (GPR20), GAD, ganglioside G2 (GD2), ganglioside GD3 (aNeu5Ac(2-8)aNeu5Ac(2-3)bDGalp(l-4)bDGlcp(l-l)Cer), ganglioside GM3 (a Neu5Ac(2-3)bDCLarlp(l-4)bDGlcp(l-l)Cer), GD3, GFRalpha4, glycoprotein 100 (gplOO), glypican-3 (GPC3), gonadotropin hormone receptor (CGHR or GR), GpA33, GpNMB, GPRC5D, guanylate cyclase C (GCC), heat shock protein 70-2 mutant (muthsp70-2), Hepatitis A virus cellular receptor 1 (HAVCR1), hexasaccharide portion of globoH glycoceramide (GloboH), high molecular weight melanoma-associated antigen (HMWMAA), HIV-1 envelope glycoprotein, HLA, HLA-DOA, HLA-A, HLA-A2, HLA-B, HLA-C, HLA-DM, HLA-DOB, HLA-DP, HLA-DQ, HLA-DR, HLA-G, HTLV1-Tax, human papillomavirus E6 (HPV E6), human papillomavirus E7 (HPV E7), human telomerase reverse transcriptase (hTERT), IgE, IL13Ra2, IL1 lRa, immunoglobulin lambda-like polypeptide 1 (IGLL1), influenza A hemagglutinin (HA), insulin-like growth factor 1 receptor (IGF-I receptor), interleukin-11 receptor alpha (IL-llRa), interleukin-13 receptor subunit alpha-2 (IL-13Ra2 or CD213A2), intestinal carboxylesterase, KIT (CD117), KSHV K8.1, KSHV-gH, LAMP1, legumain, leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), leukocyte-associated immunoglobulin-like receptor 1 (LAIR1), luteinizing hormone receptor (LHR), Lewis (Y) antigen, Lewis Ag, Livl, Locus K9 (LY6K), low-conductance chloride channel, lymphocyte antigen 6 complex, lymphocyte antigen 75 (LY75), lymphocyte-specific protein tyrosine kinase (LCK), mammary differentiation antigen (NY-BR-1), melanoma antigen 1 recognized by T cells (MelanA or MARTI), melanoma-associated antigen 1 (MAGE-A1), melanoma cancer testis antigen 1 (MAD-CT-1), melanoma cancer testis antigen 2 (MAD-CT-2), melanoma inhibitor of apoptosis (ML-IAP), mesothelin, MPL, mucin 1 cell surface associated (MUC1), N-acetylglucosaminyltransferase V (NA17), nectin 4, neural cell adhesion molecule (NCAM), NKG2D, NYBR1, O-acetylglucosaminyltransferase V (NA17), ... Cetyl-GD2 ganglioside (OAcGD2), olfactory receptor 51E2 (OR51E2), oncogene fusion protein consisting of breakpoint cluster region (BCR) and Abelson murine leukemia viral oncogene homolog 1 (Abl) (bcr-abl), P53 mutant, paired box protein Pax-3 (PAX3), paired box protein Pax-5 (PAX5), pannexin 3 (PANX3), PDL1, P-glycoprotein, placenta specific 1 (PLAC1), platelet derived growth factor receptor beta (PDGFR-beta), polysialic acid, proacrosin binding protein sp32 (OY-TES1), prostase, prostate cancer tumor antigen-1 (PCT A-1 or galectin 8), prostate stem cell antigen (PSCA), prostate specific membrane antigen (PSMA), prostatic acid phosphatase (PAP), prostein, protease serine 21 (testosin or PRSS21), proteasome (prosomal macropain) subunit beta type 9 (LMP2), PTK7, RasG12V, Ras homolog family member C (RhoC), rat sarcoma (Ras) mutant, receptor for advanced glycation end products (RAGE-1), receptor tyrosine kinase-like orphan receptor 1 (ROR1), receptor tyrosine protein kinase ERBB2 or Her-22 / neu, renal ubiquitous 1 (RU1), renal ubiquitous 2 (RU2), sarcoma translocation breakpoint, serine 2 (TMPRSS2) ETS fusion gene, sialyl Lewis adhesion molecule (sLe), SLAMF4, SLAMF6, Slea (CA19.9 or sialyl Lewis antigen), sperm protein 17 (SPA17), squamous cell carcinoma antigen recognized by T cells 3 (SART3), stage-specific embryonic antigen 4 (SSEA-4), STEAP1, survivin, synovial sarcoma X breakpoint 2 (SSX2), TCR gamma alternative reading frame protein (TARP), TCR-beta 1 chain, TCR-beta 2 chain, TCR-delta chain, TCR-gamma chain, TCR-gamma delta, telomerase, TGF beta R2, antigen recognized by TNT antibodies, thyroid stimulating hormone receptor (TSHR), Timl- / HVCR1, tissue factor 1 (TF1), Tn ag, Tn antigen ((Tn Ag) or (GalNAca-Ser / Thr)), TNF receptor family member B cell maturation (BCMA), transglutaminase 5 (TGS5), transmembrane protease, TROP2, tumor endothelial marker 1 (TEM1 / CD248), tumor endothelial marker 7 related (TEM7R), tumor protein p53 (p53), tumor associated glycoprotein 72 (TAG72), tyrosinase, tyrosinase related protein 2 (TRP-2), uroplakin 2 (UPK2), vascular endothelial growth factor receptor 2 (VEGFR2), V-myc avian myelocytomatosis viral oncogene neuroblastoma-derived homolog (MYCN), Wilms tumor protein (WT1), or X antigen family member 1A (XAGE1) on the target cell.

90. The method of any one of claims 84 to 89, wherein the targeting moiety binds to CD7.

91. 91. The method of claim 90, wherein the targeting moiety that binds CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:28, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:28, or the amino acid sequence set forth in SEQ ID NO:

28.

92. 91. The method of claim 90, wherein the targeting moiety that binds CD7 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:29, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:29, or the amino acid sequence set forth in SEQ ID NO:

29.

93. The method of any one of claims 84 to 89, wherein the targeting moiety binds to CD8.

94. 94. The method of claim 93, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:46, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:46, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:46, or the amino acid sequence set forth in SEQ ID NO:

46.

95. 94. The method of claim 93, wherein the targeting moiety that binds to CD8 comprises a polypeptide comprising a sequence having at least 90% sequence identity to the amino acid sequence of SEQ ID NO:47, a sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:47, a sequence having at least 99% sequence identity to the amino acid sequence of SEQ ID NO:47, or the amino acid sequence set forth in SEQ ID NO:

47.

96. 96. The method of any one of claims 84 to 95, wherein the cancer is a cancer provided herein, such as a T cell disorder or a B cell disorder.

97. A viral particle comprising a targeting moiety, a polypeptide comprising a viral structural protein, and a nucleic acid molecule encoding a heterologous molecule of interest; the targeting moiety comprises an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:46, or SEQ ID NO:47; The polypeptide comprising a viral structural protein comprises an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2, the nucleic acid molecule encoding a heterologous molecule of interest encodes a chimeric antigen receptor; The viral particle, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 90% identity to the amino acid sequence of SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:55, or SEQ ID NO:

56.

98. A viral particle comprising a targeting moiety, a polypeptide comprising a viral structural protein, and a nucleic acid molecule encoding a heterologous molecule of interest; the targeting moiety comprises an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:46, or SEQ ID NO:47; The polypeptide comprising a viral structural protein comprises an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2, the nucleic acid molecule encoding a heterologous molecule of interest encodes a chimeric antigen receptor; The viral particle, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:55, or SEQ ID NO:

56.

99. A viral particle comprising a targeting moiety, a polypeptide comprising a viral structural protein, and a nucleic acid molecule encoding a heterologous molecule of interest; the targeting moiety comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:46, or SEQ ID NO:47; The polypeptide comprising a viral structural protein comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO:1 or SEQ ID NO:2, the nucleic acid molecule encoding a heterologous molecule of interest encodes a chimeric antigen receptor; The viral particle, wherein the chimeric antigen receptor comprises an antigen-binding domain having an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO:51, SEQ ID NO:52, SEQ ID NO:55, or SEQ ID NO:

56.

100. The viral particle of any one of claims 97 to 99, wherein the chimeric antigen receptor comprises an antigen-binding domain comprising the amino acid sequence of SEQ ID NO:51 or SEQ ID NO:

52.

101. 101. A method of treating cancer in a subject in need thereof, comprising administering to said subject a viral particle according to any one of claims 97 to 100.

102. 102. The method of claim 101, wherein the cancer is a cancer provided herein, such as a T cell disorder or a B cell disorder.

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