Respiratory syncytial virus (RSV) g and f antibodies with high RSV-neutralizing potency

Abstract

Highly potent respiratory syncytial virus (RSV) neutralizing monoclonal antibodies that specifically bind RSV fusion protein (F) or RSV attachment glycoprotein (G) are described. The monoclonal antibodies were synthesized by sequencing RSV G- and RSV F-specific B cells from a human participant of an RSV challenge study. The RSV-specific monoclonal antibodies described herein exhibit potent neutralization of RSV (IC50 as low as 0.4 ng / ml) that is superior to previously disclosed RSV neutralizing antibodies. The RSV-specific monoclonal antibodies can be used, for example, to treat, inhibit and detect RSV infection.

Description

[0001] RESPIRATORY SYNCYTIAL VIRUS (RSV) G AND F ANTIBODIES WITH HIGH RSV- NEUTRALIZING POTENCY CROSS REFERENCE TO RELATED APPLICATIONS This application claims the benefit of U.S. Application No.63 / 566,064, filed March 15, 2024, which is herein incorporated by reference in its entirety. FIELD This disclosure concerns monoclonal antibodies that specifically bind respiratory syncytial virus (RSV) attachment glycoprotein (G) or fusion glycoprotein (F) and exhibit high ne7utralization activity against RSV. Use of the RSV-specific antibodies for treating, preventing, inhibiting, or detecting an RSV infection is also disclosed. INCORPORATION OF ELECTRONIC SEQUENCE LISTING The electronic sequence listing, submitted herewith as an XML file named 4239-111727- 02.xml (95,618 bytes), created on March 14, 2025, is herein incorporated by reference in its entirety. BACKGROUND Human respiratory syncytial virus (RSV) is an enveloped, non-segmented negative-sense single-stranded RNA virus in the family Paramyxoviridae, genus Pneumovirus. It is the most common cause of severe respiratory illness in children. In the United States each year, 10-20% of children under the age of 5 receive medical care due to RSV infection. Approximately 50-70% of children are infected by age 1 and nearly all children are infected by age 2. RSV also reinfects frequently later in life. Severe lower respiratory tract disease also occurs among the elderly or those with compromised cardiac, pulmonary, or immune systems. Passive antibody prophylaxis is available for infants, including the antibody products BEYFORTUS (nirsevimab-alip) and SYNAGIS (palivizumab), both of which target the RSV fusion glycoprotein (F). Three different vaccines, all of rely on forms of RSV F, are available for adults at least 60 years old: F subunit vaccines AREXVY and ABRYSVO, the latter of which is also authorized for use in pregnant women, and an mRNA vaccine mRESVIA, encoding the prefusion-stabilized form of RSV F. There are currently no approved antiviral drugs, vaccines or other therapeutics that target the RSV attachment glycoprotein (G). In view of the significant human health impact of RSV, a need exists for additional prophylactic agents and for therapeutic agents for the prevention and treatment of RSV infection. SUMMARY Described herein are highly potent RSV neutralizing monoclonal antibodies that specifically bind RSV F or RSV G. The disclosed monoclonal antibodies were derived from sequencing of B cell receptors of RSV G- and RSV F-specific B cells from a human participant of an RSV challenge study. Sequences of the variable regions were codon-optimized and synthetic DNAs encoding antibodies with these variable regions were generated and used to express RSV-specific monoclonal antibodies. The RSV-specific monoclonal antibodies described herein exhibit potent neutralization of RSV (IC50 as low as 0.4 ng / ml) that is superior to previously disclosed RSV neutralizing antibodies. The monoclonal antibodies of the present disclosure can be used, for example, to prevent, inhibit, treat, or detect RSV infection. Provided herein are monoclonal antibodies that specifically bind RSV G or RSV F. The monoclonal antibodies include a variable heavy (VH) domain having a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, and a variable light (VL) domain having a light chain complementarity determining region (LCDR)1, a LCDR2, and a LCDR3, wherein the monoclonal antibody has the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 sequences of any one of the 309-004, 309-018, 309-020, 309-024, and 309-007 antibodies. In some aspects, the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 sequences respectively include SEQ ID NOs: 3, 4, 5, 6, 7, and 8 (309-004); SEQ ID NOs: 11, 12, 13, 14, 15, and 16 (309-018); SEQ ID NOs: 19, 20, 21, 22, 23, and 24 (309-020); SEQ ID NOs: 27, 28, 29, 30, 31, and 32 (309-024); SEQ ID NOs: 35, 36, 37, 38, 39, and 40 (309-007); or SEQ ID NOs: 81, 82, 83, 84, 85, and 86 (309-007). In some examples, the monoclonal antibodies include the complete VH domain and complete VL domain sequences of 309-004, 309-018, 309-020, 309-024, or 309-007. In some aspects, the monoclonal antibodies further include at least one heavy chain constant region and / or a light chain constant region. In some examples, the at least one heavy chain constant region is a recombinant constant region that includes a modification that increases half-life of the antibody. Also provided herein are antigen-binding fragments of 309-004, 309-018, 309-020, 309-024, or 309-007, and bispecific antibodies that include the 309-004, 309-018, 309-020, 309-024, or 309- 007 antibody and an additional monoclonal antibody (such as an antibody that binds a different protein or binds a different epitope of RSV G or RSV F). Further provided herein are nucleic acid molecules that encode the VH domain, the VL domain, or both the VH domain and the VL domain of an antibody disclosed herein. In some aspects, the nucleotide sequence of the VH domain and / or VL domain is codon-optimized for expression in mammalian cells, such as human cells. Also provided are vectors that include a disclosed nucleic acid molecule, and host cells that include a disclosed vector. Further provided are compositions that include a pharmaceutically acceptable carrier and a disclosed monoclonal antibody, bispecific antibody, nucleic acid molecule, or vector. In some aspects, the composition is sterile and / or is in unit dosage form or a multiple thereof. Methods of detecting an RSV infection in a subject are also provided. In some aspects, the method includes contacting a biological sample from the subject with a disclosed monoclonal antibody under conditions sufficient to form an immune complex; and detecting the presence of the immune complex in the sample. The presence of the immune complex in the sample indicates that the subject has an RSV infection. Further provided are methods of preventing, inhibiting or treating an RSV infection in a subject. In some aspects, the method includes administering to a subject with or at risk of an RSV infection a therapeutically effective amount of a monoclonal antibody, bispecific monoclonal antibody, nucleic acid molecule, vector, or composition disclosed herein. In some examples, the subject to be treated has been exposed to RSV but does not have symptoms of RSV illness and / or has not been diagnosed with an RSV infection. In other examples, the subject has been diagnosed with an RSV infection and / or has symptoms of an RSV infection (e.g., the subject was diagnosed one or two days prior and / or exhibited symptoms one to two days prior). The foregoing and other features of this disclosure will become more apparent from the following detailed description of several aspects which proceeds with reference to the accompanying figures. BRIEF DESCRIPTION OF THE DRAWINGS FIG.1: Table showing clinical outcomes of 36 participants of an RSV challenge study. Donor 309, inoculated intranasally with 106.3plaque-forming units (PFU) of RSV A2, exhibited signs of RSV illness, defined as having at least two consecutive days of upper respiratory symptoms and at least two days of virus shedding. FIG.2: Graphs showing serum IgA and serum IgG titers of 16 study participants at -1, 28 and 56 days post-inoculation with a single intranasal dose of 106.3PFU of RSV A2. Donors 309 and 301 are indicated. FIG.3: Gating strategy for selection of RSV G- and F-specific B cells from donor 309. FIGS.4A-4B: Graphs showing the percentage of antibodies that bind RSV G or RSV F for donor 309 (FIG.4A) and for all 90 expressed antibodies from B cells detected on day 0, 7, or 28 after intranasal immunization with RSV A2 (FIG.4B), as measured by RSV G, preF, or postF ELISA. cDNAs encoding paired V(D)J sequences of 90 B cell receptors of RSV G, preF, or postF specific B cells detected on days 0, 7, or 28 among 7 donors were synthesized de novo and cloned into a matched expression vector (pTRIOZ or pFUSE / pFUSE2) to preserve the Ig subclass of each antibody. Expi293 cells were transfected with each antibody expression vector. Supernatants from transfected cells were evaluated by RSV G, preF, or postF ELISA to identify efficient binding antibodies specific for these RSV antigens. FIG.5: Graph showing RSV neutralization potency of G-specific antibodies 309-020, 309- 024, and 309-007 compared to reference antibodies CB017.5, CB002.5 and 3D3. The neutralization assay was performed using Hep2 cells and recombinant RSV A2 expressing enhanced green fluorescent protein (eGFP) in the presence of complement. The initial concentration of antibody was 0.5 µg / ml, followed by 8 four-fold dilutions in duplicate (n=3 independent experiments). The 50% inhibitory concentration (IC50) for each antibody was determined using four-parameter nonlinear regression analysis. FIG.6: Graph showing RSV neutralization potency of G-specific antibody 309-007 compared to F-specific reference antibodies. The neutralization assay was performed as in FIG.5. FIG.7: Graph comparing neutralization potency of antibody 309-007 as an IgG3 subclass compared to 309-007 as an IgG1 subclass. The neutralization assay was performed as in FIG.5. FIG.8: Graph showing neutralization potency of antibody 309-007 in IgG3 and IgG1 subclasses, in the presence and absence of complement. The neutralization assay was performed using Hep2 cells and wild-type RSV A2 expressing eGFP in the presence (solid lines) or absence (dashed lines) of complement. The initial concentration of antibody was 0.5 µg / ml, followed by 8 four-fold dilutions in duplicate (n=3 independent experiments). IC50 for each antibody was determined using four-parameter nonlinear regression analysis. Neutralization by 309-007 subclasses was achieved only in the presence of complement. FIG.9: Heatmap showing the epitope binning of F-specific antibodies, measured by biolayer interferometry (BLI). Streptavidin-coated biosensors were loaded with biotinylated RSV pre-F, then saturated with “blocking” mAb1. The biosensors were then moved into wells with “test” mAb2 to determine if a particular epitope is blocked. Heatmap values are a calculation of the proportion of signal “blocked’ or reduced by mAb1 when compared to a buffer-only control. Dark values close to zero suggest a different binding epitope, and lighter values, close to 1.0 suggest the same epitope for mAb binding. Known antibodies from the literature were included as references to determine the specific antigenic site. FIG.10: Heatmap showing the epitope binning of G-specific antibodies, measured by biolayer interferometry (BLI) by Octet, as described for FIG.9. FIGS.11A-11D: Crystal structure showing that the Fab of antibody 309-007 binds to the central conserved domain of the RSV G protein, with specificity to an epitope offset from the footprint of reference antibody CB0017.5. (FIG.11A) Ribbon diagram, determined by X-ray crystallography at 2.47 Å resolution, of side and top views of two heterodimer molecules, each composed of a 35 aa peptide of the central conserved domain (CCD) of the RSV G protein, bound to the fragment antigen-binding (Fab) region of the RSV antibody 309-007. (FIG.11B) Schematic diagram of the intra-molecule interactions involved in formation of the heterodimers, and the inter- molecule interactions between two heterodimer molecules. Salt bridges, hydrogen bonds, and non- bonded contacts are indicated by the indicated lines. (FIG.11C). Residues from the 309-007 heavy and light chains interact with residues of conformational epitopes [aa 171-175 (VPCSI, SEQ ID NO: 77)] of the strictly conserved central domain of the G protein (SEQ ID NO: 66), with aa S177 and W183 in the CX3C motif of the RSV G protein, as well as with aa 188-197 (RIPNKKPGKK; SEQ ID NO: 78) of its heparin binding domain, marked by black dots. Residues of the CCD shown to interact with reference antibodies CB017.5, 3D3, and CB002.5 are also indicated (Nunez Castrejon, et al., J. Virol,, 96(7):e0220121, 2022), showing that the footprint of 309-007 is slightly offset from that of reference antibody CB017.5, and different from that of 3D3 and CB002.5. (FIG.11D) The heterodimer-to-heterodimer interaction occurs through the proline residue 106 in the CDR3 of the 309-007 heavy chain that seems to interact with the residues I175, C176 and N178 of the RSV G CCD (marked by black dots). FIG.12: Alignment of the complementarity determining region 1 (CDR1) CDR2, and CDR3 (boldface and underlined) of antibody 309-007 heavy and light chain variable regions (SEQ ID NO: 33 and SEQ ID NO: 34, respectively) and reference antibody CB0017.5 heavy and light chain variable regions (SEQ ID NO: 79 and SEQ ID NO: 80, respectively), revealing a 4 aa insertion in the CDR3 region of the 309-007 heavy chain. The P106 residue with the putative ability to mediate inter- heterodimer interaction with residues 175, 176 and 178 of the CCD of the RSV G protein is located within this 4-aa insertion that is present in the CDR3 of the 309-007 heavy chain, but not in that of CB017.5. FIGS.13A-13C: Timeline and graphs showing the efficacy of various versions of the 309- 007 antibody, administered prophylactically prior to RSV challenge in hamsters. (FIG.13A) Timeline of the experiment. On day -1, groups of 12 hamsters received 12 mg / kg of the indicated antibody by intraperitoneal injection. One day later (day 0), animals were challenged intranasally with 6 log10PFU of wild-type RSV strain A2. On day 3 post-challenge, serum was collected to confirm the presence of the injected antibody by ELISA; animals were euthanized, and nasal turbinates and lungs were collected. Lungs from three hamsters per group were inflated and fixed with 10% neutral buffered formaldehyde for further histological analysis. Lungs from nine hamsters per group and NT from all hamsters (n = 12 hamsters per group) were homogenized, and RSV titers were determined by immunoplaque assay. (FIG.13B) Body weight change of hamsters expressed as mean percent relative to day -2 (n = 12 hamsters per group). Time of antibody injection and RSV challenge are indicated. Mixed-effects analysis with Dunnett post-test; exact p values are indicated for levels of significance p<0.05. (FIG.13C) RSV titers in lungs of challenged hamsters determined by immunoplaque assay and expressed in log10 PFU / g of tissue (n= 9 animals per group). The limit of detection is 50 PFU / g (indicated by a dashed line). One-way ANOVA with Tukey post-test; exact p values are indicated for levels of significance p<0.05. FIGS.14A-14B: Graphs showing serum antibody titers after passive immunization of hamsters via the intraperitoneal route (FIG.14A), and RSV titers in nasal turbinates of challenged hamsters (FIG.14B). (FIG.14A) Hamster sera were collected on day 3 after intraperitoneal administration of indicated antibodies, and RSV G antibody titers (or, for the CR3022 control group, SARS-CoV-2 S antibody titers) were determined by ELISA to control for accurate antibody delivery (n=12 animals per group). (FIG.14B) RSV titers in nasal turbinates of challenged hamsters determined by immunoplaque assay and expressed in log10PFU / g of tissue (n= 12 animals per group). The limit of detection is 50 PFU / g (indicated by a dashed line). One-way ANOVA with Tukey post- test; exact p values are indicated for levels of significance p<0.05. SEQUENCES The nucleic acid and amino acid sequences listed in the accompanying sequence listing are shown using standard letter abbreviations for nucleotide bases, and single letter code for amino acids, as defined in 37 C.F.R.1.822. Only one strand of each nucleic acid sequence is shown, but the complementary strand is understood as included by any reference to the displayed strand. In the accompanying sequence listing: d I DETAILED DESCRIPTION I. Introduction The RSV attachment protein G and fusion protein F are the major neutralization antigens of RSV. Two antibody products directed against the RSV F protein are licensed for RSV immunoprophylaxis in infants; however, there are currently no licensed antibodies targeting RSV G. RSV G-specific antibodies generally are less efficient in neutralizing RSV than RSV F-specific antibodies. Previously described G-specific antibodies reduce but do not completely neutralize RSV infectivity. To generate improved RSV G-specific and F-specific antibodies, receptors of RSV G- specific and F-specific B cells from human participants in an RSV challenge study were sequenced. Using these B cell receptor sequences, antibodies were designed and expressed in eukaryotic cells, and their specificity against RSV G and F was confirmed. Several highly potent RSV neutralizing antibodies were identified, including an F-specific antibody that appears to bind a region of the prefusion form of the F protein that overlaps two previously described epitopes, sites 0 and II. Also identified was an ultra-potent antibody of the IgG3 subclass that specifically binds the central conserved domain of RSV G. This region is structurally constrained by its receptor-binding function and thus predicted to remain genetically stable. Any RSV escape mutants with coding changes in this region would be expected to exhibit reduced viral fitness. The RSV-specific antibodies disclosed herein can be used to inhibit or prevent an RSV infection or the development of RSV illness, and to treat an existing RSV infection, including severe RSV illness. The disclosed antibodies can also be used to detect RSV. II. Abbreviations BCR B cell receptor CCD central conserved domain CDR complementarity determining region dpi days post-inoculation EC50 half maximal effective concentration eGFP enhanced green fluorescent protein ELISA enzyme linked immunosorbent assay F RSV fusion glycoprotein Fab fragment antigen-binding FACS fluorescence activated cell sorting G RSV attachment glycoprotein HCDR heavy chain CDR HRV human rhinovirus IC5050% inhibitory concentration LCDR light chain CDR NT nasal turbinate PBMC peripheral blood mononuclear cells PFU plaque forming units RSV respiratory syncytial virus VH variable heavy VL variable light III. Summary of Terms Unless otherwise noted, technical terms are used according to conventional usage. Definitions of many common terms in molecular biology may be found in Krebs et al. (eds.), Lewin’s genes XII, published by Jones & Bartlett Learning, 2017. As used herein, the singular forms “a,” “an,” and “the,” refer to both the singular as well as plural, unless the context clearly indicates otherwise. For example, the term “an antigen” includes singular or plural antigens and can be considered equivalent to the phrase “at least one antigen.” As used herein, the term “comprises” means “includes.” It is further to be understood that any and all base sizes or amino acid sizes, and all molecular weight or molecular mass values, given for nucleic acids or polypeptides are approximate, and are provided for descriptive purposes, unless otherwise indicated. Although many methods and materials similar or equivalent to those described herein can be used, particular suitable methods and materials are described herein. In case of conflict, the present specification, including explanations of terms, will control. In addition, the materials, methods, and examples are illustrative only and not intended to be limiting. To facilitate review of the various aspects, the following explanations of terms are provided: Administration: The introduction of a composition into a subject by a chosen route. Administration can be local or systemic. For example, if the chosen route is intravenous, the composition is administered by introducing the composition into a vein of the subject. Exemplary routes of administration include, but are not limited to, oral, injection (such as subcutaneous, intramuscular, intradermal, intraperitoneal, and intravenous), infusion, sublingual, rectal, transdermal (for example, topical), intranasal, vaginal, and inhalation routes. Antibody and antigen binding fragment: An immunoglobulin, antigen-binding fragment, or derivative thereof, that specifically binds and recognizes an analyte (antigen) such as RSV F or G. The term “antibody” is used herein in the broadest sense and encompasses various antibody structures, including but not limited to monoclonal antibodies, polyclonal antibodies, multispecific antibodies (e.g., bispecific antibodies), and antibody fragments, so long as they exhibit the desired antigen- binding activity. Non-limiting examples of antibodies include, for example, intact immunoglobulins and variants and fragments thereof known in the art that retain binding affinity for the antigen. Examples of antibody fragments include but are not limited to Fv, Fab, Fab', Fab'-SH, F(ab')2; diabodies; linear antibodies; single-chain antibody molecules (e.g. scFv, VHH); and multispecific antibodies formed from antibody fragments. Antibody fragments include antigen binding fragments either produced by the modification of whole antibodies or those synthesized de novo using recombinant DNA methodologies (see, e.g., Kontermann and Dübel (Eds.), Antibody Engineering, Vols.1-2, 2nded., Springer-Verlag, 2010). A single-chain antibody (scFv) is a genetically engineered molecule containing the VHand VLdomains of one or more antibody(ies) linked by a suitable polypeptide linker as a genetically fused single chain molecule (see, for example, Bird et al., Science, 242(4877):423-426, 1988; Huston et al., Proc. Natl. Acad. Sci. U.S.A., 85(16):5879-5883, 1988; Ahmad et al., Clin. Dev. Immunol., 2012, doi:10.1155 / 2012 / 980250; Marbry and Snavely, IDrugs, 13(8):543-549, 2010). The intramolecular orientation of the VHdomain and the VLdomain in a scFv is typically not decisive for scFvs. Thus, scFvs with both possible arrangements (VHdomain-linker domain-VLdomain; VLdomain-linker domain-VH domain) may be used. In a dsFv, the VH and VL have been mutated to introduce a disulfide bond to stabilize the association of the chains. Diabodies also are included, which are bivalent, bispecific antibodies in which VH and VL domains are expressed on a single polypeptide chain, but using a linker that is too short to allow for pairing between the two domains on the same chain, thereby forcing the domains to pair with complementary domains of another chain and creating two antigen binding sites (see, for example, Holliger et al., Proc. Natl. Acad. Sci. U.S.A., 90(14):6444-6448, 1993; Poljak et al., Structure, 2(12):1121-1123, 1994). Antibodies also include genetically engineered forms such as chimeric antibodies (such as humanized murine or macaque antibodies) and heteroconjugate antibodies (such as bispecific antibodies). Typically, a naturally occurring mammalian immunoglobulin has heavy (H) chains and light (L) chains interconnected by disulfide bonds. Immunoglobulin genes include the kappa, lambda, alpha, gamma, delta, epsilon and mu constant region genes, as well as the myriad immunoglobulin variable domain genes. There are two types of light chain, lambda (λ) and kappa (κ). There are five main heavy chain classes (or isotypes) that determine the functional activity of a mammalian antibody molecule: IgM, IgD, IgG, IgA and IgE. Each heavy and light chain contain a constant region (or constant domain) and a variable region (or variable domain). In several aspects, the VHand VLcombine to specifically bind the antigen. In additional aspects, only the VH is required. For example, naturally occurring camelid antibodies consisting of a heavy chain only (VHH) are functional and stable in the absence of light chain. Any of the disclosed antibodies can include a heterologous constant domain. For example, the antibody can include a constant domain that is different from a native constant domain, such as a constant domain including one or more modifications (such as the “LS” mutations) to increase half- life. References to “VH” or “VH” refer to the variable region of an antibody heavy chain, including that of an antigen binding fragment, such as Fv, scFv, dsFv or Fab. References to “VL” or “VL” refer to the variable domain of an antibody light chain, including that of an Fv, scFv, dsFv or Fab. The VH and VL contain a “framework” region interrupted by three hypervariable regions, also called “complementarity-determining regions” or “CDRs” (see, e.g., Kabat et al., Sequences of Proteins of Immunological Interest, 5thed., NIH Publication No.91-3242, Public Health Service, National Institutes of Health, U.S. Department of Health and Human Services, 1991). The sequences of the framework regions of different light or heavy chains are relatively conserved within a species. The framework region of an antibody, that is the combined framework regions of the constituent light and heavy chains, serves to position and align the CDRs in three-dimensional space. The CDRs are primarily responsible for binding to an epitope of an antigen. The amino acid sequence boundaries of a given CDR can be readily determined using any of a number of well-known schemes, including those described by Kabat et al. (Sequences of Proteins of Immunological Interest, U.S. Department of Health and Human Services, 1991; the “Kabat” numbering scheme), Chothia et al. (see Chothia and Lesk, J Mol Biol 196:901-917, 1987; Chothia et al., Nature 342:877, 1989; and Al-Lazikani et al., JMB 273,927-948, 1997; the “Chothia” numbering scheme), Kunik et al. (see Kunik et al., PLoS Comput Biol 8:e1002388, 2012; and Kunik et al., Nucleic Acids Res 40(Web Server issue):W521-524, 2012; “Paratome CDRs”) and the ImMunoGeneTics (IMGT) database (see, Lefranc, Nucleic Acids Res 29:207-9, 2001; the “IMGT” numbering scheme). The Kabat, Paratome and IMGT databases are maintained online. In addition, the AbRSA tool can be used to determine the CDR boundaries according to Kabat, IMGT or Chothia (online at aligncdr.labshare.cn / aligncdr / abrsa.php). The CDRs of each chain are typically referred to as CDR1, CDR2, and CDR3 (from the N-terminus to C-terminus), and are also typically identified by the chain in which the particular CDR is located. Thus, a VHCDR3 is the CDR3 from the VHof the antibody in which it is found, whereas a VL CDR1 is the CDR1 from the VL of the antibody in which it is found. Light chain CDRs are sometimes referred to as LCDR1, LCDR2, and LCDR3. Heavy chain CDRs are sometimes referred to as HCDR1, HCDR2, and HCDR3. A “monoclonal antibody” is an antibody obtained from a population of substantially homogeneous antibodies, that is, the individual antibodies comprising the population are identical and / or bind the same epitope, except for possible variant antibodies, for example, containing naturally occurring mutations or arising during production of a monoclonal antibody preparation, such variants generally being present in minor amounts. In contrast to polyclonal antibody preparations, which typically include different antibodies directed against different determinants (epitopes), each monoclonal antibody of a monoclonal antibody preparation is directed against a single determinant on an antigen. Thus, the modifier “monoclonal” indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies, and is not to be construed as requiring production of the antibody by any particular method. For example, the monoclonal antibodies may be made by a variety of techniques, including but not limited to the hybridoma method, recombinant DNA methods, phage-display methods, and methods utilizing transgenic animals containing all or part of the human immunoglobulin loci, such methods and other exemplary methods for making monoclonal antibodies are well-known. In some examples, monoclonal antibodies are isolated from a subject. Monoclonal antibodies can have conservative amino acid substitutions which have substantially no effect on antigen binding or other immunoglobulin functions. (See, for example, Greenfield (Ed.), Antibodies: A Laboratory Manual, 2nded. New York: Cold Spring Harbor Laboratory Press, 2014.) A “humanized” antibody or antigen binding fragment includes a human framework region and one or more CDRs from a non-human (such as a non-human primate, mouse, rat, or synthetic) antibody or antigen binding fragment. The non-human antibody or antigen binding fragment providing the CDRs is termed a “donor,” and the human antibody or antigen binding fragment providing the framework is termed an “acceptor.” Constant regions need not be present, but if they are, they can be substantially identical to human immunoglobulin constant regions, such as at least about 85-90%, such as about 95% or more identical. Hence, all parts of a humanized antibody or antigen binding fragment, except possibly the CDRs, are substantially identical to corresponding parts of natural human antibody sequences. A “chimeric antibody” is an antibody that includes sequences derived from two different antibodies, which typically are of different species. In some examples, a chimeric antibody includes one or more CDRs and / or framework regions from one human antibody and CDRs and / or framework regions from another human antibody. A “fully human antibody” or “human antibody” is an antibody which includes sequences from (or derived from) the human genome, and does not include sequence from another species. In some aspects, a human antibody includes CDRs, framework regions, and (if present) an Fc region from (or derived from) the human genome. Human antibodies can be identified and isolated using technologies for creating antibodies based on sequences derived from the human genome, for example by phage display or using transgenic animals (see, e.g., Barbas et al. Phage display: A Laboratory Manuel.1sted. New York: Cold Spring Harbor Laboratory Press, 2004; Lonberg, Nat. Biotechnol., 23(9): 1117-1125, 2005; Lonberg, Curr. Opin. Immunol.20(4):450-459, 2008). Binding affinity: Affinity of an antibody (or bispecific antibody) for an antigen. In one aspect, affinity is calculated by a modification of the Scatchard method described by Frankel et al., Mol. Immunol., 16:101-106, 1979. In another aspect, binding affinity is measured by an antigen / antibody dissociation rate. In another aspect, a binding affinity is measured by a competition radioimmunoassay. In another aspect, binding affinity is measured by ELISA. In some aspects, binding affinity is measured using bio-layer interferometry (BLI) technology, such as by using the Octet system (Creative Biolabs). In other aspects, Kd is measured using a surface plasmon resonance (SPR) assay, such as by using a BIACORES-2000 or a BIACORES-3000 (BIAcore, Inc., Piscataway, N.J.). In other aspects, antibody affinity is measured by flow cytometry. An antibody that “specifically binds” an antigen (such as RSV F or G) is an antibody that binds the antigen with high affinity and does not significantly bind other unrelated antigens. Biological sample: A sample obtained from a subject. Biological samples include all clinical samples useful for detection of disease or infection (for example, RSV infection) in subjects, including, but not limited to, peripheral blood, serum, plasma, urine, feces, saliva, cerebral spinal fluid (CSF), bronchoalveolar lavage (BAL) fluid, nasal wash, tissue, cells, tissue biopsy, fine needle aspirate, surgical specimen, and autopsy material. In a particular example, a biological sample is obtained from a subject having or suspected of having an RSV infection. Bispecific antibody: A recombinant molecule composed of two different antigen binding portions that consequently binds to two different antigenic epitopes. Bispecific antibodies include chemically or genetically linked molecules of two antigen-binding domains. The antigen binding domains can be linked using a linker. The antigen binding domains can be monoclonal antibodies, antigen-binding fragments (e.g., Fab, scFv), or combinations thereof. A bispecific antibody can include one or more constant domains, but does not necessarily include a constant domain. Similarly, a multi-specific antibody is a recombinant protein that includes antigen-binding fragments of at least two different monoclonal antibodies, such as two, three or four different monoclonal antibodies. Codon-optimized: A nucleic acid molecule encoding a protein can be codon-optimized for expression of the protein in a particular organism by including the codon most likely to encode a particular amino acid at each position of the sequence. Codon usage bias is the difference in the frequency of occurrence of synonymous codons (encoding the same amino acid) in coding DNA. A codon is a series of three nucleotides (a triplet) that encodes a specific amino acid residue in a polypeptide chain or for the termination of translation. There are 20 different naturally-occurring amino acids, but 64 different codons (61 codons encoding for amino acids plus 3 stop codons). Thus, there is degeneracy because one amino acid can be encoded by more than one codon. A nucleic acid sequence can be optimized for expression in a particular organism (such as a human) by evaluating the codon usage bias in that organism and selecting the codon most likely to encode a particular amino acid. Multivariate statistical methods, such as correspondence analysis and principal component analysis, are widely used to analyze variations in codon usage. Computer programs are available to implement the statistical analyses related to codon usage, such as Codon W, GCUA, and INCA. Conditions sufficient to form an immune complex: Conditions that allow an antibody or antigen binding fragment to bind to its cognate epitope to a detectably greater degree than, and / or to the substantial exclusion of, binding to substantially all other epitopes. Conditions sufficient to form an immune complex are dependent upon the format of the binding reaction and typically are those utilized in immunoassay protocols or those conditions encountered in vivo. See Harlow & Lane, Antibodies, A Laboratory Manual, 2nded. Cold Spring Harbor Publications, New York (2013) for a description of immunoassay formats and conditions. The conditions employed in the methods are “physiological conditions” which include reference to conditions (such as temperature, osmolarity, pH) that are typical inside a living mammal or a mammalian cell. While it is recognized that some organs are subject to extreme conditions, the intra-organismal and intracellular environment normally lies around pH 7 (for example, from pH 6.0 to pH 8.0, more typically pH 6.5 to 7.5), contains water as the predominant solvent, and exists at a temperature above 0°C and below 50°C. Osmolarity is within the range that is supportive of cell viability and proliferation. The formation of an immune complex can be detected through conventional methods, for instance immunohistochemistry, immunoprecipitation, flow cytometry, immunofluorescence microscopy, ELISA, immunoblotting (for example, Western blot), magnetic resonance imaging, CT scans, X-ray and affinity chromatography. Immunological binding properties of selected antibodies may be quantified using well-known methods. Conjugate: A complex of two molecules linked together, for example, linked together by a covalent bond. In some aspects, an antibody or a bispecific antibody disclosed herein is linked to an effector molecule, such as covalently linked to an effector molecule, or to a detectable label. The linkage can be by chemical or recombinant means. In one aspect, the linkage is chemical, wherein a reaction between the antibody moiety and the effector molecule has produced a covalent bond formed between the two molecules to form one molecule. A peptide linker (short peptide sequence) can optionally be included between the antibody / bispecific antibody and the effector molecule. Conservative amino acid substitution: “Conservative” amino acid substitutions are those substitutions that do not substantially affect a function of a protein, such as the ability of the protein to interact with a target protein. In some aspects, a conservative amino acid substitution in an RSV F- or G-specific antibody is one that does not reduce binding of the antibody to RSV F or G by more than 10% (such as by more than 5%) compared to the F or G binding of the corresponding antibody lacking the conservative amino acid substitution. In some aspects, the RSV F- or G-specific antibody can include up to 1, 2, 3, 4, 5, 6, 7, 8, 9, or up to 10 conservative substitutions compared to a reference antibody and retain specific binding activity for RSV F or G, and / or retain RSV neutralization activity. Typically, individual substitutions, deletions or additions which alter, add or delete a single amino acid or a small percentage of amino acids (for instance less than 5%, in some aspects less than 1%) in an encoded sequence are conservative variations where the alterations result in the substitution of an amino acid with a chemically similar amino acid. The following six groups are examples of amino acids that are considered to be conservative substitutions for one another: 1) Alanine (A), Serine (S), Threonine (T); 2) Aspartic acid (D), Glutamic acid (E); 3) Asparagine (N), Glutamine (Q); 4) Arginine (R), Lysine (K); 5) Isoleucine (I), Leucine (L), Methionine (M), Valine (V); and 6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W). Contacting: Placement in direct physical association; includes both in solid and liquid form, which can take place either in vivo or in vitro. Contacting includes contact between one molecule and another molecule, for example the amino acid on the surface of one polypeptide, such as an antigen, that contacts another polypeptide, such as an antibody. Contacting can also include contacting a cell for example by placing an antibody in direct physical association with a cell. Control: A reference standard. In some aspects, the control is a negative control sample obtained from a healthy patient. In other aspects, the control is a positive control sample obtained from a patient diagnosed with RSV infection. In still other aspects, the control is a historical control or standard reference value or range of values (such as a previously tested control sample, such as a group of RSV patients with known prognosis or outcome, or group of samples that represent baseline or normal values). A difference between a test sample and a control can be an increase or conversely a decrease. The difference can be a qualitative difference or a quantitative difference, for example a statistically significant difference. In some examples, a difference is an increase or decrease, relative to a control, of at least about 5%, such as at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, at least about 100%, at least about 150%, at least about 200%, at least about 250%, at least about 300%, at least about 350%, at least about 400%, at least about 500%, or greater than 500%. Degenerate variant: In the context of the present disclosure, a “degenerate variant” refers to a polynucleotide encoding a protein (for example, an antibody or portion thereof, such as a variable region, that specifically binds RSV F or G) that includes a sequence that is degenerate as a result of the genetic code. There are twenty natural amino acids, most of which are specified by more than one codon. Therefore, all degenerate nucleotide sequences are included as long as the amino acid sequence of the antibody encoded by the nucleotide sequence is unchanged. Detectable label: A detectable molecule (also known as a detectable marker) that is conjugated directly or indirectly to a second molecule, such as an antibody, to facilitate detection of the second molecule. For example, the detectable label can be capable of detection by ELISA, spectrophotometry, flow cytometry, microscopy or diagnostic imaging techniques (such as CT scans, MRIs, ultrasound, fiberoptic examination, and laparoscopic examination). Specific, non-limiting examples of detectable labels include fluorophores, chemiluminescent agents, enzymatic linkages, radioactive isotopes, nucleic acids (such as DNA barcodes), and heavy metals or compounds (for example super paramagnetic iron oxide nanocrystals for detection by MRI). In one example, a “labeled antibody” refers to incorporation of another molecule in the antibody. For example, the label is a detectable label, such as the incorporation of a radiolabeled amino acid or attachment to a polypeptide of biotinyl moieties that can be detected by marked avidin (for example, streptavidin containing a fluorescent marker or enzymatic activity that can be detected by optical or colorimetric methods). Various methods of labeling polypeptides (such as antibodies) are known and may be used. Examples of labels for polypeptides include, but are not limited to, the following: radioisotopes or radionuclides (such as35S or131I), fluorescent labels (such as fluorescein isothiocyanate (FITC), rhodamine, lanthanide phosphors), enzymatic labels (such as horseradish peroxidase, beta- galactosidase, luciferase, alkaline phosphatase), chemiluminescent markers, biotinyl groups, predetermined polypeptide epitopes recognized by a secondary reporter (such as a leucine zipper pair sequences, binding sites for secondary antibodies, metal binding domains, epitope tags), or magnetic agents, such as gadolinium chelates. In some aspects, labels are attached by spacer arms of various lengths to reduce potential steric hindrance. Methods for using detectable labels and guidance in the choice of detectable labels appropriate for various purposes are discussed for example in Sambrook et al. (Molecular Cloning: A Laboratory Manual, 4thed, Cold Spring Harbor, New York, 2012) and Ausubel et al. (In Current Protocols in Molecular Biology, John Wiley & Sons, New York, through supplement 104, 2013). Effective amount (or therapeutically effective amount): A quantity of a specific substance sufficient to achieve a desired effect in a subject to whom the substance is administered. For instance, this can be the amount necessary to inhibit, prevent or treat an RSV infection, or to measurably alter outward symptoms of the infection. In some aspects, a therapeutically effective amount of a disclosed antibody (or bispecific antibody) that binds to RSV F or G is an amount necessary to reduce or inhibit a RSV infection (for example, as measured by infection of cells, or by number or percentage of subjects infected by RSV, or by reduction in symptoms associated with the infection) by a desired amount, for example by at least 10%, at least 20%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, or even at least 100% (elimination or prevention of detectable RSV infection), as compared to a suitable control. The effective amount (or therapeutically effective amount) of an antibody disclosed herein that is administered to a subject to inhibit RSV infection will vary depending upon a number of factors associated with that subject, for example the overall health and / or weight of the subject. An effective amount can be determined by varying the dosage and measuring the resulting response, such as, for example, a reduction in RSV titer. Effective amounts also can be determined through various in vitro, in vivo or in situ immunoassays. An effective or therapeutically effective amount encompasses a fractional dose that contributes in combination with previous or subsequent administrations to attaining an effective response. For example, an effective amount of an agent can be administered in a single dose, or in several doses, for example daily, during a course of treatment lasting several days or weeks. However, the effective amount can depend on the subject being treated, the severity and type of the condition being treated, and the manner of administration. A unit dosage form of an antibody or bispecific antibody can be packaged in an amount, or in multiples of the effective amount, for example, in a vial (e.g., with a pierceable lid) or syringe having sterile components. Effector molecule: A molecule intended to have or produce a desired effect; for example, a desired effect on a cell to which the effector molecule is targeted. Effector molecules can include, for example, polypeptides, small molecules, drugs, toxins, therapeutic agents, detectable labels, nucleic acids, lipids, nanoparticles, or carbohydrates. Some effector molecules may have or produce more than one desired effect. Epitope: An antigenic determinant. Epitopes are particular chemical groups or peptide sequences on a molecule that are antigenic (elicit a specific immune response). An antibody specifically binds a particular antigenic epitope on a polypeptide (such as RSV F or G). In some examples a disclosed antibody specifically binds to an epitope on RSV F or G. In some examples, a bispecific antibody specifically binds to two different epitopes on RSV F or G (a first antigen binding portion of the bispecific antibody binds a first epitope of F or G and a second antigen binding portion of the bispecific antibody binds a second epitope of F or G). Heterologous: Originating from a separate genetic source or species. For example, a promoter can be heterologous to an operably linked nucleic acid sequence. IgG: A polypeptide belonging to the class or isotype of antibodies that are substantially encoded by a recognized immunoglobulin gamma gene. In humans, this class comprises IgG1, IgG2, IgG3, and IgG4. In mice, this class comprises IgG1, IgG2a, IgG2b, IgG3. Immune complex: The binding of an antibody to a soluble antigen forms an immune complex. The formation of an immune complex can be detected through conventional methods, for instance immunohistochemistry, immunoprecipitation, flow cytometry, immunofluorescence microscopy, ELISA, immunoblotting (for example, Western blot), magnetic resonance imaging, CT scans, X-ray and affinity chromatography. Immunological binding properties of selected antibodies may be quantified using well-known methods. Isolated: A biological component (such as a nucleic acid, peptide, protein or protein complex, for example an antibody) that has been substantially separated, produced apart from, or purified away from other biological components in the cell of the organism in which the component occurs, that is, other chromosomal and extra-chromosomal DNA and RNA, and proteins. Thus, isolated nucleic acids, peptides and proteins include nucleic acids and proteins purified by standard purification methods. The term also embraces nucleic acids, peptides and proteins prepared by recombinant expression in a host cell, as well as chemically synthesized nucleic acids. An isolated nucleic acid, peptide or protein, for example an antibody, can be at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% pure. Linker: A bi-functional molecule that can be used to link two molecules into one contiguous molecule, for example, to link an effector molecule to an antibody. Non-limiting examples of peptide linkers include glycine-serine linkers. The terms “conjugating,” “joining,” “bonding,” or “linking” can refer to making two molecules into one contiguous molecule; for example, linking two polypeptides into one contiguous polypeptide, or covalently attaching an effector molecule or detectable marker radionuclide or other molecule to a polypeptide, such as an antibody or antibody fragment. The linkage can be either by chemical or recombinant means. “Chemical means” refers to a reaction between the antibody moiety and the effector molecule such that there is a covalent bond formed between the two molecules to form one molecule. Neutralizing antibody: An antibody (or bispecific antibody) that reduces the infectious titer of an infectious agent by binding to a specific antigen on the infectious agent, such as a virus (e.g., RSV). In some aspects, an antibody or bispecific antibody that is specific for RSV G or RSV F neutralizes the infectious titer of RSV. For example, an antibody or bispecific antibody that neutralizes RSV may interfere with the virus by binding it directly and limiting entry into cells. Alternately, a neutralizing antibody may interfere with one or more post-attachment interactions of the pathogen with a receptor, for example, by interfering with viral entry using the receptor. In some aspects, an antibody or bispecific antibody that specifically binds to RSV G or RSV F and neutralizes RSV inhibits infection of cells, for example, by at least 50%, by at least 60%, by at least 70%, by at least 80%, by at least 90%, by at least 95%, or by at least 99% compared to a control antibody. In some aspects herein, the neutralization inhibitory concentration 50 (IC50) of the monoclonal antibody is less than 50 ng / ml, less than 40 ng / ml, less than 30 ng / ml, less than 20 ng / ml, less than 10 ng / ml, less than 5 ng / ml, or less than 1 ng / ml. Operably linked: A first nucleic acid sequence is operably linked with a second nucleic acid sequence when the first nucleic acid sequence is placed in a functional relationship with the second nucleic acid sequence. For instance, a promoter, such as the CMV promoter, is operably linked to a coding sequence if the promoter affects the transcription or expression of the coding sequence. Generally, operably linked DNA sequences are contiguous and, where necessary to join two protein- coding regions, in the same reading frame. Pharmaceutically acceptable carriers: The pharmaceutically acceptable carriers of use are conventional. Remington: The Science and Practice of Pharmacy, 22nded., London, UK: Pharmaceutical Press, 2013, describes compositions and formulations suitable for pharmaceutical delivery of the disclosed antibodies. In general, the nature of the carrier will depend on the particular mode of administration being employed. For instance, parenteral formulations usually include injectable fluids that include pharmaceutically and physiologically acceptable fluids such as water, physiological saline, balanced salt solutions, aqueous dextrose, glycerol or the like as a vehicle. For solid compositions (e.g., powder, pill, tablet, or capsule forms), conventional non-toxic solid carriers can include, for example, pharmaceutical grades of mannitol, lactose, starch, or magnesium stearate. In addition to biologically neutral carriers, pharmaceutical compositions to be administered can contain minor amounts of non- toxic auxiliary substances, such as wetting or emulsifying agents, added preservatives (such as non- natural preservatives), and pH buffering agents and the like, for example sodium acetate or sorbitan monolaurate. In particular examples, the pharmaceutically acceptable carrier is sterile and suitable for parenteral administration to a subject for example, by injection. In some aspects, the active agent and pharmaceutically acceptable carrier are provided in a unit dosage form such as a pill or in a selected quantity in a vial. Unit dosage forms can include one dosage or multiple dosages (for example, in a vial from which metered dosages of the agents can selectively be dispensed). Recombinant: A recombinant nucleic acid is one that has a sequence that is not naturally occurring or has a sequence that is made by an artificial combination of two otherwise separated segments of sequence. This artificial combination can be accomplished by chemical synthesis or by the artificial manipulation of isolated segments of nucleic acids, for example, by genetic engineering techniques. A recombinant protein is one that has a sequence that is not naturally occurring or has a sequence that is made by an artificial combination of two otherwise separated segments of sequence. In several aspects, a recombinant protein is encoded by a heterologous (for example, recombinant) nucleic acid that has been introduced into a host cell, such as a bacterial or eukaryotic cell. The nucleic acid can be introduced, for example, on an expression vector having signals capable of expressing the protein encoded by the introduced nucleic acid or the nucleic acid can be integrated into the host cell chromosome. Respiratory syncytial virus (RSV): A virus in the order Mononegavirales, family Paramyxoviridae, genus Pneumovirus. RSV is an enveloped virus with a non-segmented, negative- sense, single-stranded RNA genome of approximately 15.2 kb. RSV has 10 genes encoding 11 proteins: non-structural protein 1 (NS1), NS2, small hydrophobic (SH) protein, attachment glycoprotein (G), fusion glycoprotein (F), matrix protein (M), M2-1 (a transcription elongation factor), a regulatory protein (M2-2), nucleoprotein (N), phosphoprotein (P), and polymerase (L). There are two antigenic subtypes of human RSV (subtype A and subtype B), determined largely by antigenic drift and duplications in RSV G sequences. Human RSV is the most common cause of bronchiolitis and pneumonia among children in their first year of life. RSV also causes repeated infections including severe lower respiratory tract disease, which may occur at any age, especially among the elderly or those with compromised cardiac, pulmonary, or immune systems. Passive immunization currently is used to prevent severe illness caused by RSV infection, especially in infants with prematurity, bronchopulmonary dysplasia, or congenital heart disease. The RSV fusion glycoprotein (F) is an envelope glycoprotein that facilitates fusion of viral and cellular membranes. RSV F is a type I glycoprotein of approximately 574 amino acids that forms homotrimers. This protein is conserved among RSV strains. RSV F exists in pre-fusion (preF) and post-fusion (postF) conformations. The RSV attachment glycoprotein (G) is a surface glycoprotein that mediates attachment of the virus to cellular receptors. RSV G is a type II transmembrane protein of approximately 298 amino acids and is highly glycosylated. The RSV G protein includes a central conserved domain (CCD), two mucin-like domains, a transmembrane domain (TMD) and cytoplasmic tail (CT). The CT, TMD and CCD are conserved between RSV subtypes A and B. Sequence identity: The identity between two or more nucleic acid sequences, or two or more amino acid sequences, is expressed in terms of the identity between the sequences. Sequence identity can be measured in terms of percentage identity; the higher the percentage, the more identical the sequences. Homologs and variants of a VL or a VH of an antibody that specifically binds a target antigen are typically characterized by possession of at least about 75%, for example at least about 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity counted over the full-length alignment with the amino acid sequence of interest. Methods of alignment of sequences for comparison are well known in the art. Various programs and alignment algorithms are described in: Smith and Waterman, Adv. Appl. Math. 2(4):482-489, 1981; Needleman and Wunsch, J. Mol. Biol.48(3):443-453, 1970; Pearson and Lipman, Proc. Natl. Acad. Sci. U.S.A.85(8):2444-2448, 1988; Higgins and Sharp, Gene, 73(1):237- 244, 1988; Higgins and Sharp, Bioinformatics, 5(2):151-3, 1989; Corpet, Nucleic Acids Res. 16(22):10881-10890, 1988; Huang et al. Bioinformatics, 8(2):155-165, 1992; and Pearson, Methods Mol. Biol.24:307-331, 1994. Altschul et al., J. Mol. Biol.215(3):403-410, 1990, presents a detailed consideration of sequence alignment methods and homology calculations. The NCBI Basic Local Alignment Search Tool (BLAST) (Altschul et al., J. Mol. Biol.215(3):403-410, 1990) is available from several sources, including the National Center for Biological Information and on the Internet, for use in connection with the sequence analysis programs blastp, blastn, blastx, tblastn, and tblastx. Blastn is used to compare nucleic acid sequences, while blastp is used to compare amino acid sequences. Additional information can be found at the NCBI web site. Once aligned, the number of matches is determined by counting the number of positions where an identical nucleotide or amino acid residue is present in both sequences. The percent sequence identity is determined by dividing the number of matches either by the length of the sequence set forth in the identified sequence, or by an articulated length (such as 100 consecutive nucleotides or amino acid residues from a sequence set forth in an identified sequence), followed by multiplying the resulting value by 100. Specifically bind: When referring to an antibody or bispecific antibody, refers to a binding reaction that determines the presence of a target protein in the presence of a heterogeneous population of proteins and other biologics. Thus, under designated conditions, an antibody binds preferentially to a particular target protein, peptide or polysaccharide (such as an antigen present on the surface of a pathogen, for example RSV F or RSV G) and does not bind in a significant amount to other proteins present in the sample or subject. Specific binding can be determined by methods known in the art. See Greenfield (Ed.), Antibodies: A Laboratory Manual, 2nded. New York: Cold Spring Harbor Laboratory Press, 2014, for a description of immunoassay formats and conditions that can be used to determine specific immunoreactivity. An antibody (or antigen-binding fragment) that specifically binds to an epitope on RSV F or RSV G is an antibody that binds substantially to RSV F or RSV G, including cells or tissue expressing RSV F or RSV G, substrates to which the RSV F or RSV G is attached, or RSV F or RSV G in a biological specimen. It is recognized that a certain degree of non-specific interaction may occur between an antibody and a non-target (such as a cell that does not express RSV F or RSV G). Typically, specific binding results in a much stronger association between the antibody and protein or cells bearing the antigen than between the antibody and protein or cells lacking the antigen. Specific binding typically results in greater than 2-fold, such as greater than 5-fold, greater than 10-fold, or greater than 100-fold increase in the amount of bound antibody (per unit time) to a protein including the epitope or cell or tissue expressing the target epitope as compared to a protein or cell or tissue lacking this epitope. Specific binding to a protein under such conditions requires an antibody that is selected for its specificity for a particular protein. A variety of immunoassay formats (e.g., ELISA, BLI, SPR and flow cytometry) are appropriate for selecting antibodies or other ligands specifically immunoreactive with a particular protein. Subject: Living multicellular vertebrate organisms, a category that includes human and non- human mammals. In some examples, the subject is a human. In some examples, the subject has an RSV infection or is at risk of an RSV infection. Synthetic: Produced by artificial means in a laboratory, for example a synthetic nucleic acid or protein (for example, an antibody) can be chemically synthesized in a laboratory. Treating or inhibiting a disease or condition: Reducing the full development of a disease or condition in a subject, for example, reducing the full development of RSV illness in a subject who has an RSV infection (e.g., reducing viremia), and / or reducing RSV infection in a subject or in a population of subjects at risk thereof. This includes neutralizing, antagonizing, prohibiting, preventing, restraining, slowing, disrupting, stopping, or reversing progression, severity or spread of the disease or condition. Treating a disease or condition (such as an RSV infection) refers to a therapeutic intervention that ameliorates a sign or symptom of a disease or pathological condition after it has begun to develop. The term “ameliorating” refers to any observable beneficial effect of the treatment. The beneficial effect can be evidenced, for example, by a delayed onset of clinical symptoms of the disease in a susceptible subject, a reduction in severity of some or all clinical symptoms of the disease, a slower progression of the disease, a reduction in the viral load, an improvement in the overall health or well-being of the subject, or by other parameters that are specific to the particular disease. Inhibiting a disease or condition refers to a prophylactic intervention administered before the disease or condition has begun to develop (for example a treatment initiated in a subject at risk of an RSV infection, but not infected by an RSV) that reduces subsequent development of the disease or condition, and also ameliorates one or more signs or symptoms of the disease or condition following development. A “prophylactic” treatment is a treatment administered to a subject who does not exhibit signs of a disease for the purpose of reducing the risk of developing pathology. In some aspects, an antibody that specifically binds to RSV F or RSV G inhibits infection of a human subject by RSV, for example, by at least 25%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, or at least 95%, compared to a control or compared to the absence of treatment. Under conditions sufficient for: A phrase that is used to describe any environment that permits a desired activity. In some examples, the desired activity is formation of an immune complex. In other examples, the desired activity is treatment of an RSV infection. Vector: An entity containing a nucleic acid molecule (such as a DNA or RNA molecule) bearing a promoter(s) that is operationally linked to the coding sequence of a protein of interest and can express the coding sequence. Non-limiting examples include a naked or packaged (lipid and / or protein) DNA, a naked or packaged RNA, a subcomponent of a virus or bacterium or other microorganism that may be replication-incompetent, or a virus or bacterium or other microorganism that may be replication-competent. A vector is sometimes referred to as a construct. Recombinant DNA vectors are vectors having recombinant DNA. A vector can include nucleic acid sequences that permit it to replicate in a host cell, such as an origin of replication. A vector can also include one or more selectable marker genes and other genetic elements known in the art. Viral vectors are recombinant nucleic acid vectors having at least some nucleic acid sequences derived from one or more viruses. In some aspects, a viral vector comprises a nucleic acid molecule encoding a disclosed antibody or bispecific antibody that specifically binds to RSV G or RSV F. Viral vectors include, but are not limited to, lentiviral vectors, adenovirus vectors and adeno-associated virus (AAV) vectors. IV. Neutralizing Monoclonal Antibodies Specific for RSV F and G Described herein are highly potent RSV neutralizing monoclonal antibodies that specifically bind RSV F or RSV G. The disclosed monoclonal antibodies were derived from sequences determined by variable diversity joining region (VDJ) sequencing of expressed B cell receptors by single-cell sequencing of RSV G- and RSV F-specific B cells from a human participant (“donor 309”) of an RSV challenge study. The sequences of VH and VL domains determined by single-cell sequencing were codon-optimized. DNAs were synthesized de-novo and inserted into expression vectors. Expi293 cells were transfected with these plasmids to express the designed monoclonal antibodies. Monoclonal antibodies were purified by affinity chromatography and further characterized for antibody binding and in competition assays. The neutralization potency of these antibodies was determined on HEp-2 cells. The RSV-specific monoclonal antibodies described herein exhibit potent neutralization of RSV (IC50as low as 0.4 ng / ml) that is superior to previously disclosed RSV neutralizing antibodies. The monoclonal antibodies of the present disclosure can be used, for example, to prevent, inhibit, treat, or detect RSV infection. The amino acid sequences of the F-specific monoclonal antibodies 309-004 and 309-018 and the G-specific monoclonal antibodies 309-020, 309-024, and 309-007 are provided below. The sequences of the heavy chain CDRs (HCDR1, HCDR2 and HCDR3) and the light chain CDRs (LCDR1, LCDR2 and LCDR3) for each antibody are provided in the tables following the VH / VL domain sequences. Unless otherwise indicated, the CDRs listed below were determined using Cell Ranger V(D)J (10X Genomics). However, a skilled person understands that other programs and numbering schemes, such as IMGT, Kabat and Chothia, can also be used to determine the boundaries of each CDR. 309-004 VH domain (SEQ ID NO: 1) YLQLVESGGGLVQPGGSLRLSCSASGFTFDSYSMNWIRQAPGKGLEWVAAITASGLITYFAD SVKGRFGISRDNARNSLFLHMNSLRAEDTAVYYCARDQDFAYGSGREVDTWGQGTQVTVSS 309-004 VL domain (SEQ ID NO: 2) DIRMTQSPSSLSASVGDRVTISCRASQGIGNDLGWYQQKPGKAPKRLIYSASSLESGVPSRFSG SGSGTEFILTISSLQPEDVATYYCLQGHAYPLTFGGGTKVERK 309-004 CDR sequences 309-018 VH domain (SEQ ID NO: 9) QVHLVQSGGEVKKPGASVKVSCRASGYTFTHFGISWVRQAPGQGLEWIGYISLYNGNTKFSH KVQDRVTVTTDTSTSTVYMELRRLTSDDTAVYYCAREPPSITAAALFDYWGQGTLVTVSS 309-018 VL domain (SEQ ID NO: 10) DVVMTQSPLSLSVTLGQPASISCRSSQSLVYTDGNTYLSWFQQRPGQSPRRLIYKISHRDSGVP DRFSGSGSGTDFTLKISRVEAEDVGVYYCMQAIDWPRTFGQGTKLEIK 309-018 CDR sequences 309-020 VH domain (SEQ ID NO: 17) QGHLVQSGTEVKKPGSSVRVSCKASGYTFANYGVIWARQAPGQGLEWVGWISAYNGNTYF AQKFQGRVTMTTDTSTSTAYVELRSLRSDDTAVYYCARDDSLSRTLPRGYFDLWGRGTLVT VSS 309-020 VL domain (SEQ ID NO: 18) DIQMTQSPSSVSASVGDRVTITCRASQDIANWLAWYQQKPGQAPKLLIYGASSLQSGVPSRFS GSGSGTDFTLTITSLQPEDFATYFCQQAHSFPYTFDQGTKVEIK 309-020 CDR sequences 309-024 VH domain (SEQ ID NO: 25) QVQLVESGGGVVQPGRSLRLSCAVSGLTMSHYGMHWVRQAPGKGLEWVAVISHDGERKY YADSVKGRFTISRDDSQSTLYLEMNGLRPEDTAMYNCALRFQVRWDGAFDTWGQGTGVTV SS 309-024 VL domain (SEQ ID NO: 26) DIQMTQSPSSLSASVGDRVTITCRASQGIGNFLAWYQQKPGKVPNLLIYSASTLHSGVPSRFSG SGSGTDFTLTISGLQPEDVATYYCQKY 309-024 CDR sequences 309-007 VH domain (SEQ ID NO: 33) QVQLVQSGGGVVQPGRSLRLSCVGSGFNFYSYGMHWVRQAPGKGLEWVAVIWHDASNIYY ADSVRGRFTISRDNFKDTVYLQMNSLRVEDTALYYCARDAIVEYPPIIPVDGMDVWGQGTR VTVSS 309-007 VL domain (SEQ ID NO: 34) SYELTQPPSVSVSPGQTARITCSGDALPDQYTYWYQQKPGQAPVMVIYKDKERPSGMPERFS GSSSGTIATLTIGGVQAEDEADYHCQSVDSSGTYWVFGGGTKLTVL 309-007 CDR sequences 309-007 CDR sequences (determined using IMGT) Provided herein are monoclonal antibodies that bind, such as specifically bind, RSV F or RSV G. The monoclonal antibodies include a variable heavy (VH) domain that includes a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, and a variable light (VL) domain that includes a light chain complementarity determining region (LCDR)1, a LCDR2, and a LCDR3. In some aspects herein, the monoclonal antibody includes the six CDR sequences of any one of antibodies 309-004, 309-018, 309-020, 309-024, and 309-007. In some aspects, the VH domain includes the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 1 and the VL domain includes the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 2. In some examples, the amino acid sequences of the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 respectively include SEQ ID NOs: 3, 4, 5, 6, 7 and 8. In some examples, the amino acid sequence of the VH domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 1 (and includes the CDR sequences of SEQ ID NO: 1) and the amino acid sequence of the VL domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 2 (and includes the CDR sequences of SEQ ID NO: 2). In specific non-limiting examples, the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 1 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 2. In some aspects, the VH domain includes the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 9 and the VL domain includes the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 10. In some examples, the amino acid sequences of the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 respectively include SEQ ID NOs: 11, 12, 13, 14, 15 and 16. In some examples, the amino acid sequence of the VH domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 9 (and includes the CDR sequences of SEQ ID NO: 9) and the amino acid sequence of the VL domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 10 (and includes the CDR sequences of SEQ ID NO: 10). In specific non-limiting examples, the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 9 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 10. In some aspects, the VH domain includes the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 17 and the VL domain includes the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 18. In some examples, the amino acid sequences of the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 respectively include SEQ ID NOs: 19, 20, 21, 22, 23 and 24. In some examples, the amino acid sequence of the VH domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 17 (and includes the CDR sequences of SEQ ID NO: 17) and the amino acid sequence of the VL domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 18 (and includes the CDR sequences of SEQ ID NO: 18). In specific non-limiting examples, the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 17 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 18. In some aspects, the VH domain includes the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 25 and the VL domain includes the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 26. In some examples, the amino acid sequences of the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 respectively include SEQ ID NOs: 27, 28, 29, 30, 31 and 32. In some examples, the amino acid sequence of the VH domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 25 (and includes the CDR sequences of SEQ ID NO: 25) and the amino acid sequence of the VL domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 26 (and includes the CDR sequences of SEQ ID NO: 26). In specific non-limiting examples, the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 25 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 26. In some aspects, the VH domain includes the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 33 and the VL domain includes the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 34. In some examples, the amino acid sequences of the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 respectively include SEQ ID NOs: 35, 36, 37, 38, 39 and 40. In other examples, the amino acid sequences of the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 respectively include SEQ ID NOs: 81, 82, 83, 84, 85 and 86. In some examples, the amino acid sequence of the VH domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 33 (and includes the CDR sequences of SEQ ID NO: 33) and the amino acid sequence of the VL domain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 34 (and includes the CDR sequences of SEQ ID NO: 34). In specific non-limiting examples, the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 33 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 34. In some aspects, the monoclonal antibody is a fully human antibody. In some aspects, the monoclonal antibody is an IgG, such as a human IgG. In some examples, the IgG is a human IgG1, an IgG2 or an IgG3. In other aspects, the monoclonal antibody is an IgA or an IgM. In some examples, the antibody is a human IgA. In particular examples, the antibody is a human dimeric IgA and includes a J chain. In specific instances, the dimeric IgA includes one monoclonal antibody specific for RSV F and one monoclonal antibody specific for RSV G. IgA and dimeric IgA can be administered by a mucosal route, such as intranasally. In some aspects, the monoclonal antibody further includes at least one heavy chain constant region (such as a CH1, CH2 and / or CH3 domain) and / or a light chain constant region. In some aspects, the heavy chain constant region of the monoclonal antibody includes one or more amino acid substitutions to optimize in vivo half-life of the antibody. The serum half-life of IgG antibodies is regulated by the neonatal Fc receptor (FcRn). Thus, in particular aspects, the antibody includes an amino acid substitution that increases binding to the FcRn. Several such substitutions are known, such as substitutions at IgG constant regions M252Y, S254T, and T256E (referred to herein as “YTE” substitutions; see, e.g., Oganesyan et al., Mol Immunol 46(8-9):1750-1755, 2009; Dall’Acqua et al., J. Biol. Chem., 281:23514-23524, 2006), T250Q and M428L (see, e.g., Hinton et al., J Immunol., 176:346-356, 2006); M428L and N434S (the “LS” mutation, see, e.g., Zalevsky, et al., Nature Biotechnology, 28:157-159, 2010); N434A (see, e.g., Petkova et al., Int. Immunol., 18:1759-1769, 2006); T307A, E380A, and N434A (see, e.g., Petkova et al., Int. Immunol., 18:1759- 1769, 2006); and an Arg to His substitution in IgG3 (referred to herein as “R511H” and described in Stapleton et al., Nat Commun 2:599, 2011). In some examples, the monoclonal antibody includes a human IgG1 constant region having the YTE substitutions. In other examples, the monoclonal antibody includes a human IgG3 constant region having the R511H substitution. The disclosed monoclonal antibodies can also be linked to a Fc polypeptide including any of the substitutions listed above, for example, the Fc polypeptide can include the YTE substitutions or the R511H substitution. In some aspects, the light chain is a kappa light chain. In other aspects, the light chain is a lambda light chain. In some aspects, the monoclonal antibody includes a hamster light chain constant region (such as a lambda light chain constant region) and / or a hamster heavy chain constant region (such as a hamster IgG2a heavy chain constant region). In some examples, the monoclonal antibody has a heavy chain sequence that includes or consists of SEQ ID NO: 91 (or is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 91) and / or a light chain sequence that includes or consists of SEQ ID NO: 90 (or is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 90). In some aspects, the monoclonal antibody is an antigen-binding fragment, which includes a heavy chain variable region and a light chain variable region, and specifically binds RSV F or RSV G. Non-limiting examples of antigen-binding fragments include: (1) Fab, the fragment which contains a monovalent antigen-binding fragment of an antibody molecule, can be produced by digestion of whole antibody with the enzyme papain to yield an intact light chain and a portion of one heavy chain. Fabs can also be generated by a plasmid encoding only the Fab region of an antibody; (2) Fab', the fragment of an antibody molecule can be obtained by treating whole antibody with pepsin, followed by reduction, to yield an intact light chain and a portion of the heavy chain; two Fab' fragments are obtained per antibody molecule; (3) (Fab')2, the fragment of the antibody that can be obtained by treating whole antibody with the enzyme pepsin without subsequent reduction; F(ab')2 is a dimer of two Fab' fragments held together by two disulfide bonds; (4) Fv, a genetically engineered fragment containing the VH and VL expressed as two chains; and (5) Single chain antibody (such as scFv), defined as a genetically engineered molecule containing the variable region of the light chain, the variable region of the heavy chain, linked by a suitable polypeptide linker as a genetically fused single chain molecule. A scFv is a fusion protein in which a VL of an immunoglobulin and a VH of an immunoglobulin are bound by a linker (see, for example, Ahmad et al., Clin. Dev. Immunol., 2012: 980250, 2012; Mabry and Snavely, IDrugs, 13:543-549, 2010). The intramolecular orientation of the VHdomain and the VLdomain in a scFv is not decisive for the provided antibodies. Thus, scFvs with both possible arrangements (VHdomain- linker domain-VL domain; VL domain-linker domain-VH domain) may be used. (6) A dimer of a single chain antibody (scFv2), defined as a dimer of a scFv. This has also been termed a “miniantibody.” Methods of making these fragments are known (see for example, Harlow and Lane, Antibodies: A Laboratory Manual, 2nd, Cold Spring Harbor Laboratory, New York, 2013). In some aspects, the antigen binding fragment is an Fv antibody, which is typically about 25 kDa and contains a complete antigen-binding site with three CDRs per each heavy chain and each light chain. To produce FV antibodies, the VH and the VL can be expressed from two individual nucleic acid constructs in a host cell. If the VH and the VL are expressed non-contiguously, the chains of the Fv antibody are typically held together by noncovalent interactions. However, these chains tend to dissociate upon dilution, so methods have been developed to crosslink the chains through glutaraldehyde, intermolecular disulfides, or a peptide linker. Thus, in one example, the Fv can be a disulfide stabilized Fv (dsFv), wherein the VH and the VL are chemically linked by disulfide bonds. In an additional example, the Fv fragments include VH and VL chains connected by a peptide linker. These single-chain antigen binding proteins (scFv) are prepared by constructing a nucleic acid molecule encoding the VHand VLdomains connected by an oligonucleotide. The nucleic acid molecule is inserted into an expression vector, which is subsequently introduced into a host cell such as a mammalian cell. The recombinant host cells synthesize a single polypeptide chain with a linker peptide bridging the two V domains. Methods for producing scFvs are known in the art (see Whitlow et al., Methods: a Companion to Methods in Enzymology, Vol.2, page 97, 1991; Bird et al., Science 242:423, 1988; U.S. Patent No.4,946,778; Pack et al., Bio / Technology 11:1271, 1993; Ahmad et al., Clin. Dev. Immunol., 2012: 980250, 2012; Mabry and Snavely, IDrugs, 13:543-549, 2010). Dimers of a single chain antibody (scFV2) are also contemplated. Antigen binding fragments can be prepared by proteolytic hydrolysis of the antibody or by expression in a host cell (such as an E. coli cell) of DNA encoding the fragment. Antigen binding fragments can also be obtained by pepsin or papain digestion of whole antibodies by conventional methods. For example, antigen binding fragments can be produced by enzymatic cleavage of antibodies with pepsin to provide a 5S fragment denoted F(ab')2. This fragment can be further cleaved using a thiol reducing agent, and optionally a blocking group for the sulfhydryl groups resulting from cleavage of disulfide linkages, to produce 3.5S Fab' monovalent fragments. Alternatively, an enzymatic cleavage using pepsin produces two monovalent Fab' fragments and an Fc fragment directly (see U.S. Patent No.4,036,945 and U.S. Patent No.4,331,647, and references contained therein; Nisonhoff et al., Arch. Biochem. Biophys.89:230, 1960; Porter, Biochem. J.73:119, 1959; Edelman et al., Methods in Enzymology, Vol.1, page 422, Academic Press, 1967; and Coligan et al. at sections 2.8.1-2.8.10 and 2.10.1-2.10.4). Other methods of cleaving antibodies, such as separation of heavy chains to form monovalent light-heavy chain fragments, further cleavage of fragments, or other enzymatic, chemical, or genetic techniques may also be used, so long as the fragments bind to the antigen that is recognized by the intact antibody. In other aspects, the monoclonal antibody is a nanobody (having a single chain, such as a VH single-domain antibody). In some examples, the nanobody includes the VH domain of any one of antibodies 309-004, 309-018, 309-020, 309-024, and 309-007. In some aspects, the monoclonal antibody (including antigen-binding fragments) neutralizes RSV. In some examples, the neutralization inhibitory concentration 50 (IC50) of the monoclonal antibody is less than 50 ng / ml, less than 40 ng / ml, less than 30 ng / ml, less than 20 ng / ml, less than 10 ng / ml, less than 5 ng / ml, or less than 1 ng / ml. In some aspects, the monoclonal antibody is linked to an effector molecule (such as a toxin or drug) or a detectable label. In some examples, the detectable label is a fluorescent, enzymatic, radioactive or nucleic acid label. In some instances, the antibody can be conjugated to a detectable marker capable of detection by ELISA, spectrophotometry, flow cytometry, microscopy or diagnostic imaging techniques (such as computed tomography (CT), computed axial tomography (CAT) scans, magnetic resonance imaging (MRI), nuclear magnetic resonance imaging NMRI), magnetic resonance tomography (MTR), ultrasound, fiberoptic examination, and laparoscopic examination). Specific, non-limiting examples of detectable markers include fluorophores, chemiluminescent agents, enzymatic linkages, radioactive isotopes and heavy metals or compounds (for example super paramagnetic iron oxide nanocrystals for detection by MRI). For example, useful detectable markers include fluorescent compounds, including fluorescein, fluorescein isothiocyanate, rhodamine, 5- dimethylamine-1-napthalenesulfonyl chloride, phycoerythrin, lanthanide phosphors and the like. Bioluminescent markers are also of use, such as luciferase, green fluorescent protein (GFP), and yellow fluorescent protein (YFP). An antibody can also be conjugated with enzymes that are useful for detection, such as horseradish peroxidase, β-galactosidase, luciferase, alkaline phosphatase, glucose oxidase and the like. When an antibody is conjugated with a detectable enzyme, it can be detected by adding additional reagents that the enzyme uses to produce a reaction product that can be discerned. For example, when the agent horseradish peroxidase is present, the addition of hydrogen peroxide and diaminobenzidine leads to a colored reaction product, which is visually detectable. An antibody may also be conjugated with biotin, and detected through indirect measurement of avidin or streptavidin binding. It should be noted that the avidin itself can be conjugated with an enzyme or a fluorescent label. The antibody can be conjugated with a paramagnetic agent, such as gadolinium. Paramagnetic agents such as superparamagnetic iron oxide are also of use as labels. Antibodies can also be conjugated with lanthanides (such as europium and dysprosium), and manganese. An antibody may also be labeled with predetermined polypeptide epitopes recognized by a secondary reporter (such as leucine zipper pair sequences, binding sites for secondary antibodies, metal binding domains, epitope tags). The antibody can also be conjugated with a radiolabeled amino acid. The radiolabel may be used for both diagnostic and therapeutic purposes. For instance, the radiolabel may be used to detect RSV G- or RSV F-expressing cells by x-ray, emission spectra, or other diagnostic techniques. Examples of labels for polypeptides include, but are not limited to, the following radioisotopes or radionucleotides:3H,14C,15N,35S,90Y,99Tc,111In,125I,131I. Means of detecting such detectable markers are well-known. Thus, for example, radiolabels may be detected using photographic film or scintillation counters, fluorescent markers may be detected using a photodetector to detect emitted illumination. Enzymatic labels are typically detected by providing the enzyme with a substrate and detecting the reaction product produced by the action of the enzyme on the substrate, and colorimetric labels are detected by simply visualizing the colored label. The average number of effector molecule or detectable marker moieties per antibody in a conjugate can range, for example, from 1 to 20 moieties per antibody. In certain aspects, the average number of effector molecules or detectable marker moieties per antibody in a conjugate range from about 1 to about 2, from about 1 to about 3, about 1 to about 8; from about 2 to about 6; from about 3 to about 5; or from about 3 to about 4. The loading (for example, effector molecule / antibody ratio) of an conjugate may be controlled in different ways, for example, by: (i) limiting the molar excess of effector molecule-linker intermediate or linker reagent relative to antibody, (ii) limiting the conjugation reaction time or temperature, (iii) partial or limiting reductive conditions for cysteine thiol modification, (iv) engineering by recombinant techniques the amino acid sequence of the antibody such that the number and position of cysteine residues is modified for control of the number or position of linker-effector molecule attachments. Further provided herein are monoclonal antibodies that bind to the same epitope as a monoclonal antibody disclosed herein, such as a monoclonal antibody that neutralizes RSV. Antibodies that bind to such an epitope can be identified based on their ability to cross-compete (for example, to competitively inhibit the binding of, in a statistically significant manner) with the 309- 004, 309-018, 309-020, 309-024, and 309-007 antibodies provided herein in RSV binding assays. An antibody “competes” for binding when the competing antibody inhibits RSV G or F binding of the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody by more than 50%, in the presence of competing antibody concentrations higher than 106x KDof the competing antibody. In a certain aspects, the antibody that binds to the same epitope on RSV F or G as the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody is a human monoclonal antibody. Human antibodies that bind to the same epitope on RSV F or RSV G to which the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody binds can be produced using various techniques known in the art. Human antibodies are described generally in van Dijk and van de Winkel, Curr. Opin. Pharmacol.5: 368-74 (2001) and Lonberg, Curr. Opin. Immunol.20:450-459 (2008). Such antibodies may be prepared, for example, by administering an immunogen to a transgenic animal that has been modified to produce intact human antibodies or intact antibodies with human variable regions in response to antigenic challenge. Such animals typically contain all or a portion of the human immunoglobulin loci, which replace the endogenous immunoglobulin loci, or which are present extrachromosomally or integrated randomly into the animal’s chromosomes. In such transgenic mice, the endogenous immunoglobulin loci have generally been inactivated. For review of methods for obtaining human antibodies from transgenic animals, see Lonberg, Nat. Biotech.23:1117-1125 (2005) (see also, for example, U.S. Pat. Nos. 6,075,181 and 6,150,584 describing XENOMOUSE™ technology; U.S. Pat. No.5,770,429 describing HUMAB® technology; U.S. Pat. No.7,041,870 describing K-M MOUSE® technology, and U.S. Patent Application Publication No. US 2007 / 0061900, describing VELOCIMOUSE® technology). Human variable regions from intact antibodies generated by such animals may be further modified, for example, by combining with a different human constant region. Human antibodies that bind to the same epitope on RSV F or RSV G to which the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody binds can also be made by hybridoma-based methods. Human myeloma and mouse-human heteromyeloma cell lines for the production of human monoclonal antibodies have been described (see, for example, Kozbor J. Immunol., 133: 3001 (1984); Brodeur et al., Monoclonal Antibody Production Techniques and Applications, pp.51-63 (Marcel Dekker, Inc., New York, 1987); and Boerner et al., J. Immunol., 147: 86 (1991).) Human antibodies generated via human B-cell hybridoma technology are also described in Li et al., Proc. Natl. Acad. Sci. USA, 103:3557-3562 (2006). Additional methods include those described, for example, in U.S. Pat. No.7,189,826 (describing production of monoclonal human IgM antibodies from hybridoma cell lines) and Ni, Xiandai Mianyixue, 26(4):265-268 (2006) (describing human-human hybridomas). Human hybridoma technology (Trioma technology) is also described in Vollmers and Brandlein, Histology and Histopathology, 20(3):927-937 (2005) and Vollmers and Brandlein, Methods and Findings in Experimental and Clinical Pharmacology, 27(3): 185-91 (2005). Human antibodies may also be generated by isolating Fv clone variable domain sequences selected from human-derived phage display libraries. Such variable domain sequences may then be combined with a desired human constant domain. Antibodies that specifically bind to the same epitope on RSV F or RSV G as the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody can also be isolated by screening combinatorial libraries for antibodies with the desired binding characteristics. For example, a variety of methods are known for generating phage display libraries and screening such libraries for antibodies possessing the desired binding characteristics. Such methods are reviewed, for example, in Hoogenboom et al. in Methods in Molecular Biology 178:1-37 (O'Brien et al., ed., Human Press, Totowa, N.J., 2001) and further described, for example, in the McCafferty et al., Nature 348:552-554; Clackson et al., Nature 352: 624-628 (1991); Marks et al., J. Mol. Biol.222: 581-597 (1992); Marks and Bradbury, in Methods in Molecular Biology 248:161-175 (Lo, ed., Human Press, Totowa, N.J., 2003); Sidhu et al., J. Mol. Biol.338(2): 299-310 (2004); Lee et al., J. Mol. Biol.340(5): 1073-1093 (2004); Fellouse, Proc. Natl. Acad. Sci. USA 101(34): 12467-12472 (2004); and Lee et al., J. Immunol. Methods 284(1- 2): 119-132 (2004). In certain phage display methods, repertoires of VH and VL genes are separately cloned by polymerase chain reaction (PCR) and recombined randomly in phage libraries, which can then be screened for antigen-binding phage as described in Winter et al., Ann. Rev. Immunol., 12: 433-455 (1994). Phage typically display antibody fragments, either as single-chain Fv (scFv) fragments or as Fab fragments. Libraries from immunized sources provide high-affinity antibodies to the immunogen without the requirement of constructing hybridomas. Alternatively, the naïve repertoire can be cloned (for example, from humans) to provide a single source of antibodies to a wide range of non-self and also self-antigens without any immunization as described by Griffiths et al., EMBO J, 12: 725-734 (1993). Finally, naïve libraries can also be made synthetically by cloning unrearranged V-gene segments from stem cells, and using PCR primers containing random sequence to encode the highly variable CDR3 regions and to accomplish rearrangement in vitro, as described by Hoogenboom and Winter, J. Mol. Biol., 227: 381-388 (1992). Patent publications describing human antibody phage libraries include, for example: U.S. Pat. No.5,750,373, and US Patent Publication Nos. 2005 / 0079574, 2005 / 0119455, 2005 / 0266000, 2007 / 0117126, 2007 / 0160598, 2007 / 0237764, 2007 / 0292936, and 2009 / 0002360. In certain aspects, amino acid sequence variants of the monoclonal antibodies provided herein are contemplated. For example, it may be desirable to improve the binding affinity and / or other biological properties of the antibody. Amino acid sequence variants of an antibody may be prepared by introducing appropriate modifications into the nucleotide sequence encoding the antibody, or by peptide synthesis. Such modifications include, for example, deletions from, and / or insertions into and / or substitutions of residues within the amino acid sequences of the antibody. Any combination of deletion, insertion, and substitution can be made to arrive at the final construct, provided that the final construct possesses the desired characteristics, for example, antigen-binding. In certain aspects, antibody variants having one or more amino acid substitutions are provided. Sites of interest for substitutional mutagenesis include the CDRs and the framework regions. Amino acid substitutions may be introduced into an antibody of interest and the products screened for a desired activity, for example, retained / improved antigen binding, decreased immunogenicity, or improved ADCC or CDC. The variants typically retain amino acid residues necessary for correct folding and stabilizing between the VH and the VL regions, and will retain the charge characteristics of the residues in order to preserve the low pI and low toxicity of the molecules. Amino acid substitutions can be made in the VHand the VLregions to increase yield. In some aspects, the heavy chain of the antibody includes up to 10 (such as up to 1, up to 2, up to 3, up to 4, up to 5, up to 6, up to 7, up to 8, or up to 9) amino acid substitutions (such as conservative amino acid substitutions) compared to the amino acid sequence of an antibody heavy chain (or VH domain) disclosed herein. In some aspects, the light chain of the antibody includes up to 10 (such as up to 1, up to 2, up to 3, up to 4, up to 5, up to 6, up to 7, up to 8, or up to 9) amino acid substitutions (such as conservative amino acid substitutions) compared to the amino acid sequence of an antibody light chain (or VL domain) disclosed herein. In some aspects, the antibody can include up to 10 (such as up to 1, up to 2, up to 3, up to 4, up to 5, up to 6, up to 7, up to 8, or up to 9) amino acid substitutions (such as conservative amino acid substitutions) in the framework regions of the heavy chain of the antibody, or the light chain of the antibody, or the heavy and light chains of the antibody, compared to a known framework region, or compared to the framework regions of the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody, and maintain the specific binding activity for RSV F or RSV G. Also provided herein are multi-specific antibodies, such as bispecific antibodies, that include a monoclonal antibody disclosed herein and a second monoclonal antibody (such as an antigen binding fragment). In some aspects, the second monoclonal antibody binds a different antigen (e.g., an antigen other than RSV F or RSV G). In other aspects, the second monoclonal antibody binds a different epitope on RSV F or RSV G as an antibody disclosed herein. In some examples, the bispecific antibody includes an F-specific antibody disclosed herein (such as 309-004 or 309-018) and a G-specific antibody disclosed herein (such as 309-020, 309-024 or 309-007). Further provided herein are compositions that include a pharmaceutically acceptable carrier and a monoclonal antibody or multi-specific (such as bispecific) antibody disclosed herein. In some aspects, the composition is sterile an / or is in unit dosage form or a multiple thereof. In some aspects, the composition includes at least two monoclonal antibodies disclosed herein, such as 2, 3, 4 or 5 monoclonal antibodies disclosed herein. In specific examples, the composition includes at least one monoclonal antibody that specifically binds RSV F (e.g., 309-004 and / or 309-018) and at least one monoclonal antibody that specifically binds RSV G (e.g., 309-020, 309-024, and / or 309-007). In some instances, the composition includes 1 or 2 antibodies (309-004 and / or 309-018) that specifically bind RSV F and 1, 2 or 3 antibodies that specifically bind RSV G (309-020, 309-024, and / or 309- 007). In particular examples, the composition includes a dimeric IgA that includes one antibody that specifically binds RSV F and one antibody that specifically binds RSV G. Pharmaceutical compositions are further described in section VI. V. Nucleic Acids, Vectors and Host Cells Isolated nucleic acid molecules and vectors encoding the monoclonal antibodies disclosed herein are also provided. Further provided are isolated cells that include a nucleic acid molecule or vector disclosed herein. Nucleic acid molecules (for example, DNA, cDNA and RNA molecules) encoding the amino acid sequences of the disclosed monoclonal antibodies that specifically bind RSV F or RSV G can readily be produced by one of skill in the art, using the amino acid sequences provided herein (such as the CDR sequences and VH and VL sequences), sequences available in the art (such as framework or constant region sequences), and the genetic code. In several aspects, a nucleic acid molecules can encode the VH, the VL, or both the VHand VL(for example in a bicistronic expression vector) of a disclosed antibody. In several aspects, the nucleic acid molecules can be expressed in a host cell (such as a mammalian cell) to produce a disclosed antibody or antigen binding fragment. In some aspects, the isolated nucleic acid molecule encodes a VH domain, a VL domain, or both a VH domain and a VL domain, of a monoclonal antibody disclosed herein. In some examples, the nucleic acid sequences of the VH domain and / or the VL domain of the monoclonal antibody includes the nucleic acid sequences set forth as SEQ ID NOs: 41 and 42, respectively, or degenerate variants thereof; SEQ ID NOs: 43 and 44, respectively, or degenerate variants thereof; SEQ ID NOs: 45 and 46, respectively, or degenerate variants thereof; SEQ ID NOs: 47 and 48, respectively, or degenerate variants thereof; or SEQ ID NOs: 49 and 50, respectively, or degenerate variants thereof.

[0002] In other aspects, the nucleic acid molecule encoding the VH domain and / or the VL domain is codon-optimized for expression in mammalian cells, such as human cells. In some examples, the nucleic acid sequences of the VH domain and / or the VL domain of the monoclonal antibody includes the nucleic acid sequences set forth as SEQ ID NOs: 51 and 52, respectively, or degenerate variants thereof; SEQ ID NOs: 53 and 54, respectively, or degenerate variants thereof; SEQ ID NOs: 55 and 56, respectively, or degenerate variants thereof; SEQ ID NOs: 57 and 58, respectively, or degenerate variants thereof; or SEQ ID NOs: 59 and 60, respectively, or degenerate variants thereof. In some aspects, the nucleic acid molecule is operably linked to a promoter. Further provided herein are vectors that include a nucleic acid molecule disclosed herein. In some aspects, the vector is a viral vector, such as a lentiviral vector, an adenovirus vector or an adeno- associated virus vector. In some aspects, the vector is an expression vector, such as a pFUSE vector (InvivoGen, San Diego, CA) or a pTRIOZ vector (InvivoGen, San Diego, CA). In some examples, the vector includes a coding sequence for a signal sequence, such as an IL-2 signal sequence. In particular examples, the nucleotide sequence of the IL-2 signal sequence is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 61. In some aspects disclosed herein, the nucleic acid molecule further includes a heavy chain constant region coding sequence. In some examples, the heavy chain constant region is an IgG3 constant region or an IgG1 constant region. In specific examples, the nucleotide sequence encoding the IgG3 heavy chain constant region is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 62. In other specific examples, the nucleotide sequence encoding the IgG1 heavy chain constant region is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 63. In specific non-limiting examples, the heavy chain constant region includes one or more amino acid substitutions that increase half-life of the antibody, such as an R511H substitution in an IgG3 constant region or YTE (M252Y, S254T and T256E) substitutions in an IgG1 constant region. Modified codons for the exemplary amino acid substitutions in the constant region are indicated in bold underline in the sequences below.

[0003] In some aspects herein, the nucleic acid molecule further includes a coding sequence for a light chain constant region, such as a kappa light chain or a lambda light chain. In some examples, the kappa light chain coding sequence is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 64. In some aspects, the nucleic acid molecule encodes a hamster light chain, such as a hamster lambda light chain. In some examples, the nucleic acid sequence encoding the hamster lambda light chain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 88. In specific examples, the nucleic acid sequence encoding the hamster light chain includes or consists of SEQ ID NO: 88. In some aspects, the nucleic acid molecule encodes a hamster heavy chain, such as a hamster IgG2a heavy chain. In some examples, the nucleic acid sequence encoding the hamster heavy chain is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identical to SEQ ID NO: 89. In specific examples, the nucleic acid sequence encoding the hamster heavy chain includes or consists of SEQ ID NO: 89. Also provided are isolated host cells that include a disclosed nucleic acid molecule or vector are also provided. In some examples, the host cell is a bacterial cell, a yeast cell, an insect cell or a mammalian cell (such as a human cell). A skilled person can readily use the genetic code to construct a variety of functionally equivalent nucleic acids, such as nucleic acids which differ in sequence but which encode the same antibody sequence. Nucleic acid sequences encoding antibodies, bispecific antibodies and conjugates that specifically bind RSV F or RSV G can be prepared by any suitable method including, for example, cloning of appropriate sequences, direct chemical synthesis, and nucleic acid amplification methods. VI. Compositions and Administration Provided herein are compositions that include a pharmaceutically acceptable carrier and an RSV F- or RSV G-specific monoclonal antibody, bispecific antibody, nucleic acid molecule or vector disclosed herein. In some aspects, the composition is sterile an / or is in unit dosage form or a multiple thereof. The compositions are useful, for example, for the treatment or detection of an RSV infection. The compositions can be prepared in unit dosage forms for administration to a subject. The amount and timing of administration are at the discretion of the treating physician to achieve the desired purposes. The RSV F- or RSV G-specific antibody, bispecific antibody, or nucleic acid molecules / vectors encoding such molecules can be formulated for systemic or local administration. In one example, the RSV F- or RSV G-specific monoclonal antibody, bispecific antibody or nucleic acid molecule or vector encoding such molecules, is formulated for parenteral administration, such as intravenous administration. In some aspects, the compositions comprise a monoclonal antibody, bispecific antibody, or conjugate thereof, in at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% purity. In certain aspects, the compositions contain less than 10%, less than 5%, less than 4%, less than 3%, less than 2%, less than 1% or less than 0.5% of macromolecular contaminants, such as other mammalian (for example, human) proteins. The compositions for administration can include a solution of the RSV F- or RSV G-specific antibody, bispecific antibody, conjugate, or nucleic acid molecule (such as a vector) encoding such molecules, dissolved in a pharmaceutically acceptable carrier, such as an aqueous carrier. A variety of aqueous carriers can be used, for example, buffered saline and the like. These solutions are sterile and generally free of undesirable matter. These compositions may be sterilized by conventional, well known sterilization techniques. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions such as pH adjusting and buffering agents, toxicity adjusting agents and the like, for example, sodium acetate, sodium chloride, potassium chloride, calcium chloride, sodium lactate and the like. The concentration of antibody in these formulations can vary widely, and will be selected primarily based on fluid volumes, viscosities, body weight and the like in accordance with the particular mode of administration selected and the subject’s needs. A typical composition for intravenous administration includes about 0.01 to about 30 mg / kg of monoclonal antibody or bispecific antibody per subject per day (or the corresponding dose of a conjugate including the antibody or antigen binding fragment). Actual methods for preparing administrable compositions will be known or apparent to those skilled in the art and are described in more detail in such publications as Remington's Pharmaceutical Science, 22th ed., Pharmaceutical Press, London, UK (2012). In some aspects, the composition can be a liquid formulation including one or more antibodies or bispecific antibodies, in a concentration range from about 0.1 mg / ml to about 20 mg / ml, or from about 0.5 mg / ml to about 20 mg / ml, or from about 1 mg / ml to about 20 mg / ml, or from about 0.1 mg / ml to about 10 mg / ml, or from about 0.5 mg / ml to about 10 mg / ml, or from about 1 mg / ml to about 10 mg / ml. The disclosed monoclonal antibodies, bispecific antibodies, and nucleic acids (including vectors) encoding such molecules, can be provided in lyophilized form and rehydrated with sterile water before administration, although they are also provided in sterile solutions of known concentration. The antibody solution can then be added to an infusion bag containing 0.9% sodium chloride, USP, and administered according to standard protocols. Considerable experience is available in the art in the administration of antibody drugs, which have been marketed in the U.S. since the approval of RITUXAN® in 1997. Monoclonal antibodies, bispecific antibodies, or a nucleic acids / vectors encoding such molecules, can be administered by slow infusion, rather than in an intravenous push or bolus. In one example, a higher loading dose is administered, with subsequent, maintenance doses being administered at a lower level. For example, an initial loading dose of 4 mg / kg may be infused over a period of some 90 minutes, followed by weekly maintenance doses for 4-8 weeks of 2 mg / kg infused over a 30 minute period if the previous dose was well tolerated. Controlled-release parenteral formulations can be made as implants, oily injections, or as particulate systems. For a broad overview of protein delivery systems see, Banga, A.J., Therapeutic Peptides and Proteins: Formulation, Processing, and Delivery Systems, Technomic Publishing Company, Inc., Lancaster, PA, (1995). Particulate systems include microspheres, microparticles, microcapsules, nanocapsules, nanospheres, and nanoparticles. Microcapsules contain the therapeutic protein, such as a cytotoxin or a drug, as a central core. In microspheres the therapeutic is dispersed throughout the particle. Particles, microspheres, and microcapsules smaller than about 1 µm are generally referred to as nanoparticles, nanospheres, and nanocapsules, respectively. Capillaries have a diameter of approximately 5 µm so that only nanoparticles are administered intravenously. Microparticles are typically around 100 µm in diameter and are administered subcutaneously or intramuscularly (see, for example, Kreuter, Colloidal Drug Delivery Systems, J. Kreuter, ed., Marcel Dekker, Inc., New York, NY, pp.219-342 (1994); and Tice & Tabibi, Treatise on Controlled Drug Delivery, A. Kydonieus, ed., Marcel Dekker, Inc. New York, NY, pp.315-339, (1992). Polymers can be used for ion-controlled release of the antibody compositions disclosed herein. Various degradable and nondegradable polymeric matrices for use in controlled drug delivery are known (Langer, Accounts Chem. Res.26:537-542, 1993). For example, the block copolymer, polaxamer 407, exists as a viscous yet mobile liquid at low temperatures but forms a semisolid gel at body temperature. It has been shown to be an effective vehicle for formulation and sustained delivery of recombinant interleukin-2 and urease (Johnston et al., Pharm. Res.9:425-434, 1992; and Pec et al., J. Parent. Sci. Tech.44(2):58-65, 1990). Alternatively, hydroxyapatite has been used as a microcarrier for controlled release of proteins (Ijntema et al., Int. J. Pharm.112:215-224, 1994). In yet another aspect, liposomes are used for controlled release as well as drug targeting of the lipid-capsulated drug (Betageri et al., Liposome Drug Delivery Systems, Technomic Publishing Co., Inc., Lancaster, PA (1993)). Numerous additional systems for controlled delivery of therapeutic proteins are known (see U.S. Patent No.5,055,303; U.S. Patent No.5,188,837; U.S. Patent No.4,235,871; U.S. Patent No. 4,501,728; U.S. Patent No.4,837,028; U.S. Patent No.4,957,735; U.S. Patent No.5,019,369; U.S. Patent No.5,055,303; U.S. Patent No.5,514,670; U.S. Patent No.5,413,797; U.S. Patent No. 5,268,164; U.S. Patent No.5,004,697; U.S. Patent No.4,902,505; U.S. Patent No.5,506,206; U.S. Patent No.5,271,961; U.S. Patent No.5,254,342 and U.S. Patent No.5,534,496). A therapeutically effective amount of an RSV F- or RSV G-specific monoclonal antibody, bispecific antibody, or nucleic acid molecule / vector encoding such molecules, will depend upon the severity of the disease and / or infection and the general state of the patient's health. A therapeutically effective amount is that which provides either subjective relief of a symptom(s) or an objectively identifiable improvement as noted by the clinician or other qualified observer. The RSV F or RSV G- specific monoclonal antibody, bispecific antibody, or nucleic acid molecule / vector encoding such molecules, can be administered in conjunction with another therapeutic agent, either simultaneously or sequentially. Single or multiple administrations of a composition including a disclosed RSV F or RSV G- specific antibody, bispecific antibody, or nucleic acid molecule / vector encoding such molecules, can be administered depending on the dosage and frequency as required and tolerated by the patient. Compositions including the RSV F or RSV G-specific antibody, bispecific antibody, or nucleic acid molecule / vector encoding such molecules, should provide a sufficient quantity of at least one of the RSV F or RSV G-specific-specific antibodies, bispecific antibodies, or nucleic acid molecules / vectors to effectively treat the patient. The dosage can be administered once, but may be applied periodically until either a therapeutic result is achieved or until side effects warrant discontinuation of therapy. In one example, a dose of the monoclonal antibody is infused for thirty minutes every other day. In this example, about one to about ten doses can be administered, such as three or six doses can be administered every other day. In a further example, a continuous infusion is administered for about five to about ten days. The subject can be treated at regular intervals, such as daily, weekly, or monthly, until a desired therapeutic result is achieved. Generally, the dose is sufficient to treat or ameliorate symptoms or signs of disease without producing unacceptable toxicity to the patient. Data obtained from cell culture assays and animal studies can be used to formulate a range of dosage for use in humans. The dosage normally lies within a range of circulating concentrations that include the ED50, with little or minimal toxicity. The dosage can vary within this range depending upon the dosage form employed and the route of administration utilized. The therapeutically effective dose can be determined from cell culture assays and animal studies. In certain aspects, the monoclonal antibody that specifically binds RSV F or RSV G, or a nucleic acid molecule or vector encoding such a molecule, can be administered at a dose in the range of from about 1 to about 100 mg / kg, such as about 5-50 mg / kg, about 25-75 mg / kg, or about 40-60 mg / kg. In some aspects, the dosage can be administered at about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 150, 200, or 300 mg / kg, or other dose deemed appropriate by the treating physician. Further, the doses described herein can be administered according to the dosing frequency or frequency of administration described herein, including without limitation daily, every other day, 2 or 3 times per week, weekly, every 2 weeks, every 3 weeks, monthly, etc. In some aspects, the dosage is administered daily beginning at the time of diagnosis with RSV and until RSV symptoms are alleviated. Additional treatments, including additional courses of therapy with a disclosed agent can be performed as needed. The RSV F or RSV G-specific antibody, bispecific antibody, nucleic acid molecule, or composition, as well as additional agents, can be administered to subjects in various ways, including local and systemic administration, such as, for example, by injection subcutaneously, intravenously, intra-arterially, intraperitoneally, intramuscularly, intradermally, or intrathecally. In an aspect, a therapeutic agent is administered by a single subcutaneous, intravenous, intra-arterial, intraperitoneal, intramuscular, intradermal or intrathecal injection once a day. The therapeutic agent can also be administered by direct injection at or near the site of disease. The therapeutic agent may also be administered orally in the form of microspheres, microcapsules, liposomes (uncharged or charged (such as cationic)), polymeric microparticles (such as polyamides, polylactide, polyglycolide, poly(lactide-glycolide)), microemulsions, and the like. A further method of administration is by osmotic pump (for example, an Alzet pump) or mini-pump (for example, an Alzet mini-osmotic pump), which allows for controlled, continuous and / or slow-release delivery of the therapeutic agent or pharmaceutical composition over a pre- determined period. The osmotic pump or mini-pump can be implanted subcutaneously, or near a target site. It will be apparent to a skilled person that the therapeutic agent or compositions thereof can also be administered by other modes. The therapeutic agent can be administered as pharmaceutical formulations suitable for, for example, oral (including buccal and sub-lingual), rectal, nasal, topical, pulmonary, vaginal or parenteral (including intramuscular, intraarterial, intrathecal, subcutaneous and intravenous) administration, or in a form suitable for administration by inhalation or insufflation. Depending on the intended mode of administration, the pharmaceutical formulations can be in the form of solid, semi-solid or liquid dosage forms, such as tablets, suppositories, pills, capsules, powders, liquids, suspensions, emulsions, creams, ointments, lotions, and the like. The formulations can be provided in unit dosage form suitable for single administration of a precise dosage. The formulations include an effective amount of a therapeutic agent, and one or more pharmaceutically acceptable excipients, carriers and / or diluents, and optionally one or more other biologically active agents. VII. Methods of Inhibiting, Treating and Preventing RSV Infection and Illness Methods of inhibiting, treating, or preventing an RSV infection are described. The methods include administering to a subject with or at risk of an RSV infection a therapeutically effective amount of a monoclonal antibody, bispecific monoclonal antibody, nucleic acid molecule, vector, or composition disclosed herein. In some aspects, the subject has been exposed to RSV but has not been diagnosed as having an RSV infection and / or does not yet have any symptoms of an RSV infection (post-exposure prophylaxis). In some example, the monoclonal antibody, bispecific monoclonal antibody, nucleic acid molecule, vector or composition is administered no more than 2, no more than 3, no more than 4, no more than 5, no more than 6, no more than 7, no more than 8, no more than 9, no more than 10, no more than 15 or no more than 20 days following exposure to RSV. In other aspects, the subject has been diagnosed with an RSV infection and / or has symptoms of an RSV infection (post-exposure treatment). In some examples, the monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition is administered no more than 2, no more than 3, no more than 4, no more than 5, no more than 6, no more than 7, no more than 8, no more than 9, no more than 10, no more than 15 or no more than 20 days following diagnosis of an RSV infection or following development of symptoms of an RSV infection. In some aspects of the disclosed methods, the monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition is administered in multiple doses, such as but not limited to, two, three, four or five doses. In other aspects, the monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition is administered in a single dose. Methods are disclosed herein for the inhibition (such as prevention) or treatment of an RSV infection or RSV illness, in a subject. Prevention can include inhibition of infection with RSV. The method can include administering to a subject a therapeutically effective amount of a disclosed monoclonal antibody, bispecific antibody, or conjugate (for example, an antibody conjugated to a toxin, drug, or other effector molecule) that specifically binds RSV F or RSV G, or a nucleic acid encoding such an antibody, bispecific antibody, or conjugate. In some examples, the monoclonal antibody, bispecific antibody, conjugate, or nucleic acid molecule can be used pre-exposure (for example, to prevent or inhibit RSV infection). In some examples, the antibody, bispecific antibody, conjugate, or nucleic acid molecule, can be used in post-exposure prophylaxis. In some examples, the antibody, bispecific antibody, conjugate, or nucleic acid molecule, can be used to eliminate or reduce the viral load of RSV in a subject infected with RSV. For example, a therapeutically effective amount of an antibody, bispecific antibody, conjugate, or nucleic acid molecule, can be administered to a subject with an RSV infection. In some examples, the antibody, bispecific antibody, conjugate, or nucleic acid molecule is modified such that it is directly cytotoxic to infected cells (for example, by conjugation to a toxin), or uses natural defenses such as complement, antibody dependent cellular cytotoxicity (ADCC), or phagocytosis by macrophages, or can be modified to increase the natural defenses. The RSV infection in the subject does not need to be completely eliminated for the method to be effective. For example, the method can reduce or ameliorate RSV illness or RSV infection by a desired amount, for example by at least 10%, at least 20%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, or even at least 100% (elimination of detectable RSV infection or RSV illness), as compared to RSV infection or RSV illness in the absence of the treatment. In one non-limiting example, the method reduces viral titer in a subject with an RSV infection. For example, administration of a therapeutically effective amount of a disclosed monoclonal antibody or bispecific antibody can reduce viral titer by at least 10%, at least 20%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, or even at least 100% (elimination of detectable RSV) in the subject. Methods of determining the RSV viral titer in the subject are known, and include, for example, obtaining a blood sample from the subject and assaying the sample for RSV activity. In several aspects, administration of a therapeutically effective amount of a disclosed antibody, bispecific antibody, conjugate, or nucleic acid molecule / vector, results in a reduction in the establishment of RSV infection and / or reducing subsequent RSV illness progression in a subject. A reduction in the establishment of RSV infection and / or a reduction in subsequent RSV illness progression encompass any statistically significant reduction in RSV activity. In several aspects, the subject can be selected for treatment, for example, a subject at risk of RSV infection, or known to have an RSV infection. In several aspects, a method of preventing or inhibiting RSV infection of a cell is provided. The method includes contacting the cell with an effective amount of an antibody as disclosed herein. For example, the cell can be incubated with the effective amount of the antibody prior to or contemporaneous with incubation with the RSV. RSV infection of the cell does not need to be completely eliminated for the method to be effective. For example, a method can reduce RSV infection by a desired amount, for example by at least 10%, at least 20%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, at least 98%, or even at least 100% (elimination of detectable RSV infected cells), as compared to RSV infection in the absence of the treatment. In some aspects, the cell is also contacted with an effective amount of an additional agent, such as anti- viral agent. The cell can be in vivo or in vitro. In some aspects, a subject is further administered one or more additional antibodies that bind RSV and that can neutralize RSV infection. For example, the subject can be administered a therapeutically effective amount of a set of antibodies including two or more (such as 2, 3, 4 or 5) of the 309-004, 309-018, 309-020, 309-024, and 309-007 antibodies disclosed herein. The antibodies can be administered as a cocktail (that is, as a single composition including the two or more antibodies), or can be administered sequentially. In some aspects, the subject is administered a monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition disclosed herein as a prime treatment and the subject is later boosted with a RSV vaccine or a chimeric attenuated respiratory virus vaccine. For example, the subject can be treated with at least one antibody that specifically binds RSV G (e.g., 309-020, 309- 024, or 309-007) and at least one antibody that specifically RSV F (e.g., 309-004 or 309-018, nirsevimab-alip, or palivizumab) as a prime dose, and then the subject can be boosted with any licensed RSV vaccine (such as AREXVY, BRYSVO, or mRESVIA), or a chimeric respiratory virus vaccine. In some examples of the disclosed methods, the monoclonal antibody administered is an IgA or dimeric IgA (such as a human IgA or human dimeric IgA) and the monoclonal antibody is administered via a mucosal route, such as intranasally. In some examples, a subject is administered the DNA encoding the antibody to provide in vivo antibody production, for example using the cellular machinery of the subject. Immunization by nucleic acid constructs is well known and taught, for example, in U.S. Patent Nos.5,643,578, 5,593,972 and 5,817,637. U.S. Patent No.5,880,103 describes several methods of delivery of nucleic acids encoding to an organism. One approach to administration of nucleic acids is direct administration with plasmid DNA, such as with a mammalian expression plasmid. The nucleotide sequence encoding the disclosed antibody can be placed under the control of a promoter to increase expression. The methods include liposomal delivery of the nucleic acids. Such methods can be applied to the production of an antibody. In some aspects, a disclosed antibody is expressed in a subject using the pVRC8400 vector (described in Barouch et al., J. Virol, 79:8828-8834, 2005). The nucleic acid molecules encoding the disclosed antibodies or bispecific antibodies can be included in a viral vector (or multiple vectors, particularly for bispecific antibodies), for example for expression of the antibody or bispecific antibody in a host cell, or a subject (such as a subject with or at risk of RSV infection). A number of viral vectors have been constructed that can be used to express the disclosed antibodies or bispecific antibodies, such as a retroviral vector, an adenoviral vector, or an adeno-associated virus (AAV) vector. In several examples, the viral vector can be replication-competent. For example, the viral vector can have a mutation in the viral genome that does not inhibit viral replication in host cells. The viral vector also can be conditionally replication- competent. In other examples, the viral vector is replication-deficient in host cells. In one aspect, a nucleic acid encoding a disclosed antibody is introduced directly into cells. For example, the nucleic acid can be loaded onto gold microspheres by standard methods and introduced into the skin by a device such as Bio-Rad’s HELIOS^ Gene Gun. The nucleic acids can be “naked,” consisting of plasmids under control of a strong promoter. Typically, the DNA is injected into muscle, although it can also be injected directly into other sites. Dosages for injection are usually around 0.5 µg / kg to about 50 mg / kg, and typically are about 0.005 mg / kg to about 5 mg / kg (see, e.g., U.S. Patent No.5,589,466). VIII. Diagnostic Methods for Detection of RSV Also provided herein are methods of detecting an RSV infection in a subject. The methods include contacting a biological sample from the subject with a disclosed monoclonal antibody under conditions sufficient to form an immune complex; and detecting the presence of the immune complex in the sample. The presence of the immune complex in the sample indicates that the subject has an RSV infection. Similarly, provided are methods of diagnosing an RSV infection in a subject by contacting a biological sample from the subject with a disclosed monoclonal antibody under conditions sufficient to form an immune complex, and detecting the presence of the immune complex in the sample. The disclosed methods can be used for the detection of RSV F or RSV G in vitro or in vivo. In one example, expression of RSV F or RSV G is detected in a biological sample, and can be used to detect an RSV infection based on the presence of RSV F or RSV G in a sample. The sample can be any sample, including, but not limited to, tissue from biopsies, autopsies and pathology specimens. Biological samples also include sections of tissues, for example, frozen sections taken for histological purposes. Biological samples further include body fluids, such as blood, serum, plasma, sputum, spinal fluid or urine. The method of detection can include contacting a cell or sample, or administering to a subject, an antibody that specifically binds to RSV F or RSV G, or a conjugate thereof (such as a conjugate including a detectable marker) under conditions sufficient to form an immune complex, and detecting the immune complex (for example, by detecting a detectable marker conjugated to the antibody. In some aspects, the disclosed antibodies are used to test vaccines. For example, to test if a vaccine composition including RSV F or RSV G assumes a conformation including the RSV F or RSV G epitope to which the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody binds. Thus, provided herein is a method for testing a vaccine, wherein the method includes contacting a sample containing the vaccine, such as an RSV F or RSV G immunogen, with a disclosed antibody under conditions sufficient for formation of an immune complex, and detecting the immune complex. Detection of the immune complex confirms that the RSV F or RSV G vaccine includes the epitope to which the 309-004, 309-018, 309-020, 309-024, or 309-007 antibody binds. In one example, the detection of the immune complex in the sample indicates that a vaccine component, such as an RSV F or RSV G immunogen, assumes a conformation capable of binding the antibody. In one aspect, the antibody is directly labeled with a detectable marker. In another aspect, the antibody that binds RSV F or RSV G (the first antibody) is unlabeled and a second antibody or other molecule that can bind the antibody that binds the first antibody is utilized for detection. As is well known to a skilled person, a second antibody is chosen that is able to specifically bind the species and class of the first antibody. For example, if the first antibody is a human IgG, then the secondary antibody may be an anti-human-IgG. Other molecules that can bind to antibodies include, without limitation, Protein A and Protein G, both of which are available commercially. Suitable labels for the monoclonal antibody or secondary antibody are described above, and include various enzymes, prosthetic groups, fluorescent materials, luminescent materials, magnetic agents and radioactive materials. Non-limiting examples of suitable enzymes include horseradish peroxidase, alkaline phosphatase, beta-galactosidase, or acetylcholinesterase. Non-limiting examples of suitable prosthetic group complexes include streptavidin / biotin and avidin / biotin. Non-limiting examples of suitable fluorescent materials include umbelliferone, fluorescein, fluorescein isothiocyanate, rhodamine, dichlorotriazinylamine fluorescein, dansyl chloride or phycoerythrin. A non-limiting exemplary luminescent material is luminol; a non-limiting exemplary a magnetic agent is gadolinium, and non-limiting exemplary radioactive labels include125I,131I,35S or3H. IX. Kits Kits are also provided. For example, kits for treating a subject with an RSV infection, or for detecting RSV F or RSV G in a sample or in a subject. The kits will typically include a disclosed RSV F- or RSV G-specific antibody, bispecific antibody, or a nucleic acid molecule(s) or vector(s) encoding such molecules, or compositions including such molecules. More than one of the disclosed RSV F- or RSV G-specific antibody, bispecific antibody, conjugate, or nucleic acid molecule or vector encoding such molecules, or compositions including such molecules can be included in the kit. In one aspect, the kit is a diagnostic kit and includes an immunoassay. Although the details of the immunoassays may vary with the particular format employed, the method of detecting RSV F or RSV G in a biological sample generally includes the steps of contacting the biological sample with an antibody which specifically reacts, under conditions sufficient to form an immune complex, to RSV F or RSV G. The antibody is allowed to specifically bind under immunologically reactive conditions to form an immune complex, and the presence of the immune complex (bound antibody) is detected directly or indirectly. The kit can include a container and a label or package insert on or associated with the container. Suitable containers include, for example, bottles, vials, syringes, etc. The containers may be formed from a variety of materials such as glass or plastic. The container typically holds a composition including one or more of the disclosed antibodies, bispecific antibodies, conjugates, nucleic acid molecules, vectors, or compositions. In several aspects, the container may have a sterile access port (for example the container may be an intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). A label or package insert indicates that the composition is used for treating the particular condition. The label or package insert typically will further include instructions for use of the antibodies, bispecific antibodies, conjugates, nucleic acid molecules / vectors, or compositions included in the kit. The package insert typically includes instructions customarily included in commercial packages of therapeutic products that contain information about the indications, usage, dosage, administration, contraindications and / or warnings concerning the use of such therapeutic products. The instructional materials may be written, in an electronic form or may be visual. The kits may also include additional components to facilitate the particular application for which the kit is designed. Thus, for example, the kit may additionally contain means of detecting a label (such as enzyme substrates for enzymatic labels, filter sets to detect fluorescent labels, appropriate secondary labels such as a secondary antibody, or the like). The kits may additionally include buffers and other reagents routinely used for the practice of a particular method. Such kits and appropriate contents are well known to a skilled person. EXAMPLES The following examples are provided to illustrate particular features of certain aspects of the disclosure, but the scope of the claims should not be limited to those features exemplified. Example 1: Methods This example describes the materials and methods used for the studies described in Examples 2-4. RSV challenge of adult human participants The described RSV challenge studies (NCT02484417 and NCT03388645) were phase I studies in healthy adult male and non-pregnant female participants 18 years to 50 years of age. Participants were intranasally challenged with one of three doses (105PFU, 106.3PFU, or 107PFU) of RSV A2 and monitored for shedding of RSV and respiratory symptoms. PBMCs were collected before challenge and on days 7 and 28 post-challenge to evaluate the B cell recall response following RSV challenge. Antigen expression, purification, and labeling RSV antigens for immunoassays were expressed from cDNAs in Expi293 cells. Briefly, previously described DNA constructs for the expression of RSV preF (DS-CAV1, A2 strain) (Stewart-Jones et al., PLOS One 10(6):e0128779, 2015) and postF (A2 strain) (McLellan et al., J Virol 85(15):7788-7796, 2011) contained C-terminal His and Avi tags. The sequence encoding the ectodomain of RSV G (A2 strain) was codon-optimized for expression in human cells (Genscript) and cloned under the control of the CMV promoter in the pcDNA3.1(-) vector between the XbaI and KpnI sites. The construct encodes from the 5’-end to the 3’-end (i) the prolactin signal sequence, (ii) aa 65- 298 (234 aa) of RSV G A2, (iii) the Avi tag sequence, (iv) the human rhinovirus 3C protease cleavage site, (v) an 8X His tag and (vi) the Strep-tag II. Constructs were transfected into Expi293 cells using Expifectamine (Gibco A14525) following manufacturer recommendations. On day 5-6 post transfection, clarified supernatant was loaded onto a HisTrap HP column (Cytiva 17524802) overnight at 4°C using an Atka Go FPLC system. For both preF and postF antigens, the column was washed with 50 mM tris-HCl, pH 8.0 + 400 mM NaCl, and antigens were eluted with 50 mM tris-HCl, pH 8.0 + 400 mM NaCl + 300 mM imidazole. To purify RSV G antigen, the column was washed with 20 mM tris-HCL pH 8.0, 300 mM NaCl buffer and eluted with 20 mM tris-HCL pH 8.0, 300 mM NaCl, 75 mM imidazole buffer. The resulting product was concentrated on a 30K centrifugal filter (Amicon Ultra 4 #UFC803096). Proteins were further purified by size-exclusion chromatography (Superdex 200 Increase; 10 / 300 GL). Purified proteins were aliquoted, flash frozen in liquid nitrogen, and stored at -80°C. Purified antigens were labeled with biotin (Avidity BirA500), following manufacturer instructions and further purified by size-exclusion chromatography in PBS to remove excess biotin. Each antigen was then labeled with tetramers containing streptavidin, a PE or APC fluorophore, and a unique oligonucleotide barcode (BioLegend #405283, 405261, 405282, 405263, 405293, 405265) at a 3 to 1 molar ratio. (Phung et al., Sci Transl Med 14(650):eabo5032, 2022). Labeling and sorting of human B cells from PBMC PBMC from human donors were thawed at 37°C for 1 minute, resuspended in RPMI medium + 10% FBS prewarmed to 37°C, washed twice in PBS, blocked with Fc Receptor Blocking Solution (BioLegend 422301) for 10 minutes on ice, and labeled 1:1 with a cocktail of antibodies (Table 1) and labeled antigens for 30 minutes on ice. The cocktail included antibodies for flow cytometry and sorting (CD3, CD14, CD16, CD19), antibodies with oligonucleotide barcodes (CD138, CD20, CD27, CD24, CD21, CD71, CD38, CD56, CD45, IgM, IgG, and IgD; Table 1), and the labeled RSV G, preF, and postF probes (two versions of each, labelled with APC or PE, respectively; 25 ng of each probe per ~5 million PBMC). Following labeling, PBMC were washed four times with Cell Staining Buffer (BioLegend 420201) in FACS tubes before a final resuspension in PBS with live / dead Helix NP Blue diluted 1:1000 (BioLegend 425305). PE and APC labelled versions of each probe were included in the B cell panel to increase the confidence of detection of true antigen-specific cells obtained by the cell sorting (described in the next paragraph). Optimal concentrations of each BioLegend antibody and labelled RSV G and F antigens for flow cytometry and cell sorting were determined with PBMC from the NIH donor blood bank. PBMC were sorted into Cell Staining Buffer on a BD Arya to collect the population of live single B cells (CD3- CD14- CD16- CD19+) that were double-positive for both APC and PE, indicating binding of two or more of the RSV antigen probes. Table 1. Antibodies with oligonucleotide barcodes for B cell characterization by sequencing Table 2. Antibodies and dyes for flow cytometry Single cell sequencing Sorted cells were filtered using a 40 µm FlowMi cell strainer (136800040), counted, and loaded into the 10X Chromium Controller following instructions in 10X Genomics User Guide CG000330. Single cell emulsions were made using the 5’ single cell kit from 10X Genomics (PN- 1000263). DNA libraries of expressed B cell receptors were generated with the Chromium Single Cell Human BCR Amplification Kit (PN-1000253), deviating from the User Guide at V(D)J Amplification 1 and 2 to increase to 10 PCR cycles. The feature barcode libraries were constructed with the 5’ Features Barcode Library Kit (PN-1000256), adding an additional final purification with SPRI beads (1.0X concentration) to remove the adapter dimer prior to sequencing. Final data was analyzed using Cell Ranger with Ensembl reference library and SeqGeq. Antibody analysis, expression, and purification Cell phenotypes were analyzed with FlowJo and SeqGeq. FlowJo was used to gate on live single CD3- CD14- CD16- CD19+ B cells. B cells that were double-positive for APC and PE were sorted and used for single-cell sequencing. Based on single-cell sequencing results, cells double- positive for two probes of a single antigen (e.g., preF-APC+ and preF PE+) were identified by SeqGeq, and B cell receptor sequences were analyzed to determine VL, VH, and CDR regions. The amino acid coding sequence of the variable region of the expressed B cell receptor of a specific B cell was codon-optimized for expression in human cells (GenScript) and cloned into pTRIOZ or pFUSE / pFUSE2 vectors (InvivoGen) to match the native subclass of the antibody. Antibodies were expressed by transfecting plasmids into Expi293 cells using Expifectamine (Gibco A14525) and purified from the supernatants by affinity chromatography. IgG1 and IgG2 antibodies were purified using HiTrap Protein A HP columns (Cytiva # 17040303) and IgG3 antibodies were purified using HiTrap Protein G HP columns (Cytiva # 17040503). Columns were washed using 20 mM sodium phosphate binding buffer and antibodies were eluted using Pierce IgG Elution Buffer (Thermo Fisher 21004). Eluted fractions were collected in tubes preloaded with 200 µL of 1 M tris-HCl, pH 9.0, per mL eluent. IgA1 and IgA2 antibodies were purified using Peptide M agarose beads (Invitrogen gel- pdm-5) at 4°C. Beads were washed with PBS, and antibodies were eluted using 0.1 M glycine into tubes preloaded with 200 µL of 1 M tris-HCl, pH 9.0, per mL eluent. Antibody purity was checked on 4-12% bis-tris gels in both reducing and non-reducing conditions, visualized with Coomassie blue (abcam 119211). Antibodies with improved half-life were engineered by site-directed mutagenesis to introduce specific substitutions. The IgG1 subclass antibodies were mutagenized to contain the YTE mutation (M252Y, S254T and T256E), as described in Oganesyan et al. (Mol Immunol 46(8-9):1750-1755, 2009). The IgG3 subclass antibodies were mutagenized to substitute His for Arg, as described in Stapleton et al. (Nat Commun 2:599, 2011). For 309-007, this residue is R511H. Mutagenesis was completed at GenScript. Fabs were made by digestion of full-length IgG using papain (Thermo Fisher Fab Preparation Kit 44985) and purifying on Protein A spin columns (Thermo Fisher 89952). Products were verified with Coomassie blue on a 4-12% bis-tris gel. Expression and purification of a peptide corresponding to the central conserved domain (CCD) of RSV G A mammalian suspension cell line that constitutively expressed a 35-amino acid peptide (HFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKKT; SEQ ID NO: 66), corresponding to the central conserved domain (CCD) of the G protein of RSV strain A2 (aa 164-198), was generated. The sequence encoding the CCD was synthetized de novo by a commercial company and cloned into a lentivirus pJG expression vector as described in Yost et al. (Methods Mol Biol 1911:305-316, 2019). The expressed sequence consisted of (i) a prolactin signal sequence, followed by (ii) aa 164-198 of RSV G, corresponding to the CCD; (iii) the human rhinovirus (HRV) 3C protease cleavage site; (iv) a protein A tag used for purification; and (v) a 3X Flag tag (SEQ ID NO: 68), separated by short T / G / S / linker sequences (underlined): The lentivirus containing the pJG-CCD vector was produced in HEK293T cells that were maintained in Dulbecco’s Modified Eagle Medium (DMEM) supplemented with 10% fetal bovine serum (FBS). HEK293 T cells were co-transfected with the pJG-CCD expressing vector and the viral packaging vectors pPAX-2 and pPMD2-G and incubated at 37°C and 5% CO2. Four hours later, the medium was removed and replaced with fresh medium, and cells were further incubated at 37°C for 3 days. The supernatant containing the lentivirus was harvested, and cell debris was removed by centrifugation at 3,800 g for 10 minutes. The clarified supernatant was then centrifuged at 112,000 g for 90 minutes to pellet the lentivirus. The lentivirus pellet was resuspended in 600 µl of Expi293 expression medium and 200 µl of lentivirus suspension was used to infect 4x105Expi293 cells in 24- well plate, followed by incubation at 37°C and 5% CO2. The following day, cells were washed once with fresh Expi293 medium and moved to a shaking incubator at 37°C and 8% CO2. Three days later, medium was replaced, and cells were expanded until they reached 6 million cells per ml in 3L final volume. The medium containing the expressed CCD-containing protein (SEQ ID NO: 68) was clarified from cell debris by centrifugation and filtered using a 0.2 µm aPES filter unit. The entire 3L of filtered medium was loaded onto an IgG Sepharose column (Cytiva). The column was next extensively washed with binding buffer (20 mM Tris-HCl and 300 mM NaCl). The CCD was cleaved from the protein A tag on the column for 16-18 hours at 4°C using the PreScission Protease diluted in binding buffer. The PreScission Protease that contained a GST tag was removed from the CCD preparation using a GSTrap column (Cytiva). The CCD was concentrated using an Amicon 3 kDa molecular weight cut-off membrane (Millipore) and further purified by size exclusion chromatography in binding buffer using a Superdex 200 increase 10 / 300 GL column (Cytiva). The purity and identity of the CCD was confirmed by SDS-PAGE on a 4-12% bis-tris gel, followed by Coomassie staining, as well as by Western blotting using the anti-G CB017.5 antibody, and aliquots were snap-frozen in liquid nitrogen and stored at -80°C. Expression and purification of 309-007 fragment antigen-binding (Fab) domain The 309-007 Fab was expressed from the pTRIOZ vector expressing both the light and heavy chains. A histidine tag (6X His) followed by a stop codon was introduced after the “EPKSC” motif (SEQ ID NO: 75) in the hinge region of the heavy chain. In addition, to help with crystallization, the human kappa constant domain FG loop (“HQGLSSP” motif; SEQ ID NO: 76) in the light chain was replaced with the shorter rabbit kappa loop (“QGTTS” motif; SEQ ID NO: 74) as described in Lieu et al. (PLOS One, 5(9):e0232311, 2020) and Rosen et al (Cell, 187(25):7196-7213.e26, 2024). The 309- 007 Fab encoding cDNA was transfected into 500 mL of Expi293 cells following the manufacturer’s recommendations. Transfected Expi293 cells were incubated at 37°C, 8% CO2for 6 days. On day 6, medium was harvested, and cell debris were pelleted by centrifugation at 6,000 x g for 30 minutes. The clarified medium was filtered using a 0.2 µm aPES filter and incubated with nickel beads following the manufacturer’s recommendations. After a 2-3 hour incubation at 4°C, beads were washed with PBS and the 309-007 Fab was eluted with PBS containing 500 mM imidazole, followed by dialysis into PBS overnight. The purity of the Fab was confirmed by SDS-PAGE using a 4-12% bis-tris gel, followed by Coomassie staining, and aliquots were snap-frozen in liquid nitrogen and stored at -80°C. Nucleic acid sequence encoding the kappa loop (SEQ ID NO: 73) CAGGGCACCACATCT Amino acid sequence of the kappa loop (SEQ ID NO: 74) QGTTS Confirmation of the binding of the 309-007 Fab to the CCD by biolayer interferometry The binding of the 309-007 Fab to the purified soluble CCD was confirmed by biolayer interferometry using the Octet RED384 (ForteBio). Assays were performed at 30°C in black 96-well plates (Greiner Bio-One #655209) with shaking using 10x Kinetics buffer (ForteBio #18-1105). NTA biosensors (ForteBio) were hydrated in 10x Kinetics buffer for at least 10 minutes prior to beginning of the assays. The soluble CCD was serially diluted using seven three-fold dilutions from a starting concentration of 0.5 µg / ml. NTA biosensors were first loaded with the His-tagged 309-007 Fab (2 µg / ml) for 5 minutes. Biosensors were next washed for 3 minutes in 10x Kinetics buffer, and then dipped into CCD dilutions for 5 minutes. After CCD binding, biosensors were moved to buffer for 20 minutes to monitor dissociation. The background binding observed from a 309-007 Fab-loaded sensor dipped into a control well with no soluble CCD was subtracted from the test wells. BLI data confirmed that the soluble CCD efficiently bound to 309-007 Fab (KD < 1.0x10-12M). Crystallization of the 309-007 Fab in complex with the CCD The 309-007 Fab and soluble CCD were mixed with a 1.5 molar excess of CCD and incubated at 4°C for 16-18 hours. The complex was then concentrated using an Amicon 3 kDa molecular weight cut-off membrane (Millipore) and purified by SEC on the Superdex 200 increase 10 / 300 GL column (Cytiva) in binding buffer (20 mM Tris-HCl and 300 mM NaCl). The formation of the complex was confirmed by SDS-PAGE using a 4-12% bis-tris gel, followed by Coomassie staining. The 309-007 Fab / CCD complex was concentrated to around 10 mg / mL using an Amicon 10 kDa molecular weight cut-off membrane (Millipore).100 nL were dropped into each well on a CrystalQuick 96-well plate (Greiner) using the Mosquito LV liquid handler (SPT Labtech) and mixed with 100 nL of pre-mixed crystallization screening buffers from Hampton Research Crystal Screens. Plates were sealed, incubated at either 4°C or 20°C and formation of crystals was evaluated 2 days later. Evaluation of the prophylactic efficacy of antibodies against RSV in hamsters Seventy-two 5- to 6-week-old male golden Syrian hamsters (Envigo Laboratories, Frederick, MD) were included in the study. On days -2 or -3, serum was collected from all animals, and their body weight was determined. Cages of three hamsters were rearranged to form six groups of 12 hamsters with comparable average body weight. On day -1, hamsters in groups of 12 were immunized by intraperitoneal injection at a dose of 12 mg / kg with each of four versions of the 309-007 antibodies, the RSV G specific reference antibody CB017.5, included as a positive control, or the anti- SARS-CoV-2 antibody CR3022 which was included as a negative control. One day later (day 0), hamsters were challenged intranasally under isoflurane anesthesia with recombinant RSV A2 (6 log10 PFU / hamster). The body weight of each hamster was determined from day 0 to day 3 post-challenge (pc). On day 3 pc, serum was collected from each hamster to confirm the presence of the injected antibody by ELISA, and hamsters were euthanized by CO2inhalation; nasal turbinates (NT) and lungs harvested. Lungs from three hamsters per group were inflated and fixed with a 10% neutral-buffered formaldehyde solution for histological analysis. NT and lungs from 12 or 9 animals per group, respectively, were homogenized. Clarified tissue homogenates were snap frozen, and RSV titers were determined later by immunoplaque assay on Vero cells. Example 2: Serology of study participants Adults challenged with RSV A2 were monitored for symptoms of RSV illness and RSV shedding. The results are shown in FIG.1. RSV-associated upper respiratory illness was defined as the presence of at least one major symptom or two minor symptoms that lasted two or more consecutive days, with evidence of viral shedding detectable over two or more days in nasal wash specimens collected on day 2 post-challenge or later. Major symptoms included nasal congestion or rhinorrhea, ear pain, sinus congestion or pain, and sore throat (Hall et al., Clin Infect Dis 33(6):792- 796, 2001). Minor symptoms included fever, with temperature ranging from 38°C (100.4°F) to 39.4°C (103°F), headache, cough, and hoarseness. Sub-clinical illness was defined by the presence of RSV shedding for two or more days, but no clinical symptoms. Patient 309, who was inoculated with 106.3PFU of RSV A2, exhibited signs of RSV illness. Serum specimens were collected to evaluate serum neutralization titers and ELISA titers to the major antigens preF, postF, and G. As shown in FIG.2, at 28 and 56 days post-inoculation (dpi) there was little increase in serum neutralization titers or ELISA titers to preF, postF, and G antigens, with the exception of serum anti-G IgA, when compared to specimens collected at -1 dpi. Example 3: Synthesis of F-specific and G-specific antibodies from sequences of B cell receptors determined by single-cell sequencing of RSV antigen-positive B cells For single-cell sequencing analysis, at least two donors from each of the dose cohorts were selected (n=3 dosed with 105PFU, n=2 with 106.3PFU, and n=2 with 107PFU). Five donors with RSV illness (103, 210, 309, 501, and 701) were selected because these subjects were assumed to have a strong B cell response. In addition, one donor with shedding and symptoms below the threshold for RSV illness (201), and one donor with sub-clinical illness (301) were included. PBMC from these participants were labeled with a cocktail of (i) fluorescent antibodies for FACS, (ii) oligonucleotide-tagged antibodies to provide “feature barcodes” for single-cell sequencing, and (iii) pairs of RSV antigens tagged with PE or APC as fluorophores, each with an oligonucleotide feature barcode. FACS was used to sort for CD19 immunostaining to identify B cells. The population of CD19+ cells that were double-positive for RSV antigen (PE+ / APC+) was collected. For comparison, the complementary population of CD19+ cells that were double-negative for antigen (PE- / APC-) was also collected. Both the B cell receptor (BCR) and feature barcode sequencing libraries were prepared to identify the V(D)J sequences of the expressed B cell receptor and, by analyzing the feature barcode sequences, the protein phenotype of the B cells. Cell phenotypic data was determined by combining analysis with flow cytometry fluorophores and the single-cell sequencing feature barcodes for protein expression. The gating strategy for donor 309 is shown in FIG.3. The final cell population identified live cells that were CD3- / CD14- / CD16- / CD19+ / PE+ / APC+ by flow cytometry and CD14- / CD3- / CD56- / CD45+ / IgD- / CD27+ by CITE-seq. B cell receptors with paired heavy and light chains were analyzed, focusing on IgG and IgA isotypes. Result confirmed that the heavy chain usage of IGHV1-18 was enriched in RSV-reactive antibodies, compared to the reference database, which is consistent with previous observations by others (Gilman et al., Sci Immunol 1(6):eaaj1879, 2016). Heavy chain and light chain sequences were determined, cDNAs from each sequenced antigen-positive B cell were synthesized and cloned into an expression vector matching the native immunoglobulin isotype and subclass identified by sequencing. The antibodies were expressed with Expi293 cells, purified as described in Example 1, and tested for reactivity by ELISA to preF, postF, and G antigens. A total of 90 antibodies were generated and tested by RSV G, preF, or postF ELISA: 31 of 50 (62%) mAbs derived from B cells collected on 28 dpi were found to bind RSV G or F antigen by ELISA. Only 1 of 19 (5%) and 5 of 21 (24%) mAbs derived from B cells collected on days 0 and 7 dpi were found to bind RSV G or F antigen by ELISA (FIG.4B). The results of this study for donor 309 are shown in FIG.4A. Five antibodies from donor 309 were selected for further analysis – two RSV F-specific antibodies (309-004 and 309-018) and three RSV G-specific antibodies (309-020, 309-024, and 309- 007). The VH domain and VL domain sequences of these five antibodies are set forth herein as SEQ ID NOs: 1 and 2 (309-004), SEQ ID NOs: 9 and 10 (309-018), SEQ ID NOs: 17 and 18 (309-020), SEQ ID NOs: 25 and 26 (309-024), and SEQ ID NOs: 33 and 34 (309-007). Example 4: Antibody characterization The selected mAbs that were reactive to RSV antigens were further tested to determine their half-maximal effective concentrations (EC50) in ELISAs. ELISAs were performed using RSV preF and postF antigen of RSV A2. Many of the antibodies had log10 EC50 value below 2 ng / mL, exceeding the potency of known reference antibodies. A comparison of the potency of binding to preF and postF of two F-specific antibodies (309-004 and 309-018) with RSV F-specific reference antibodies (D25, ADI-15614, MPE8, Motavizumab, and 101F) is shown in Table 3. In addition, ELISA antigens were generated to evaluate reactivity of the antibodies with RSV G proteins from RSV A2 and different RSV subgroups. While RSV A2 (reference strain, representative of subgroup A) is widely used in laboratories and represented the challenge virus, RSV of subgroups A or B are in circulation in communities. Recent RSV isolates of subgroups A and B contain a duplication in the C-terminal domain of the G protein that increases the length of the G protein. For example, the ON1 lineage of RSV subgroup A has acquired a duplication that lengthens the G protein by 24 amino acids (Eshaghi et al., PLoS One 7(3):e32807, 2012), and the BA lineage of subgroup B contains a duplication that lengthens the G protein by 20 amino acids (Trento et al., J Gen Virol 84(Pt 11):3115-3120, 2003). Thus, the mAbs described here were tested to determine their reactivity with G proteins of currently circulating lineages containing amino acid duplications. To generate antigen for ELISA assays, G protein from two recent isolates of subgroups A (isolate Seattle A) and B (isolate Seattle B), both containing amino acid duplications in the G protein, was generated in Expi293 cells and purified as described for A2 G probes above. In addition, G antigen of a subgroup B variant without amino acid duplication (Little Rock B) was generated for ELISA assays. A comparison of the potency of binding to RSV G of three G-specific antibodies (309-020, 309-024, and 309-007) with RSV G-specific reference antibodies (CB017.5, 3G12, CB002.5 and 3D3; Jones et al., PLoS Pathog 14(3): e1006935, 2018; Collarini et al., J Immunol 183(10:6338-6345, 2009) to G proteins derived from subgroups A (A2 and Seattle A) and B (Little Rock B and Seattle B) is shown in Table 4. These results show that the EC50values of 309-007 and 309-024 for all RSV G antigens exceed those of the reference antibodies (CB017.5, 3G12, CB002.5 and 3D3), and the EC50 values of 309-020 is similar to those of these reference antibodies. Table 3. Binding efficacy of F-specific antibodies to preF and postF Table 4. Binding efficacy of G-specific antibodies to G from subgroups A and B In addition, the ability of RSV F-specific mAbs was tested to neutralize RSV A2 using a plaque-reduction neutralization assay on Hep2 cells in the presence of complement. F-specific mAbs 309-004 (IgG isotype) and 309-018 (IgA1isotype) were strongly RSV-neutralizing, as shown in Table 5. Table 5. Neutralization potency of F-specific antibodies to RSV A2 RSV G-specific mAbs were also tested for their ability to neutralize RSV in a plaque- reduction neutralization assay on Hep2 cells in the presence of complement. G-specific mAbs 309- 020 (IgG1), 309-024 (IgG1) and 309-007 (IgG3) were found to neutralize RSV A2, RSV B1, or both, as shown in Table 6. Table 6. Neutralization potency of G-specific antibodies to RSV of subgroups A and B A 3 3 3 C C These results demonstrated that the RSV G-specific antibodies 309-007 and 309-024 bound all 4 tested versions of RSV G proteins, derived from RSV subgroups A and B, and with and without the duplication. Both of these antibodies also neutralized RSV of both subgroups. This finding suggests that these antibodies may bind the central conserved domain (CCD) of G, which is conserved between all variants of G. In addition, the results from the RSV neutralization assays show that the G-specific antibody 309-007 was 25- to 80-fold more potent than the reference antibodies CB017.5, CB002.5, and 3D3 (16.2, 8.2, and 24.3 ng / mL, respectively; see FIG.5). Moreover, antibody 309-007 is 7- to 9-fold more potent than the best reference antibody to date, D25 (FIG.6), the precursor to Nirsevimab / BEYFORTUS. It was found that the same variable region of 309-007, expressed as an IgG1 subclass of IgG, is 6 times less potent than the native IgG3 subclass (FIG.7). Thus, the ultrapotent RSV neutralization potency of antibody 309-007 appears to be, at least in part, based on the IgG3 subclass of IgG. Antibody 309-007 only reaches 100% RSV-neutralization when in the IgG3 subclass, and neutralization is achieved in the presence of complement (FIG.8), but not in the absence of complement. To determine the affinity of each antibody, the dissociation constant (KD) of each antibody was determined using biolayer interferometry (BLI) by Octet. Streptavidin-coated biosensors were loaded with biotinylated preF or G at 0.5 µg / mL. Affinity of the antibody for its cognate ligand was measured by an increase in binding signal. KD was calculated using the dissociation rate into buffer only, compared to the association rate of the antibody for the antigen. The limit of detection of the instrument is 1.0 x 10-12M, so values lower than this threshold cannot be distinguished from each other. BLI was completed using an OctetRED 384. Octet Kinetics Buffer (Sartorius 18-1105) was used at 1X for biosensor hydration and at 10X for baseline measurements and as diluent for ligands and analytes. Antigens were loaded at 0.5 µg / mL onto streptavidin (SA) biosensors (Sartorius 18- 5019) by affinity with the biotin tag at the C-terminus. Full-length immunoglobulins were serially diluted for affinity measurements with RSV antigen. Kinetics were observed with the following protocol: Baseline 180 s, loading 300 s, baseline 180 s, association 300 s, dissociation 1200 s. At least 4 analyte curves were used for interpolation of the KD by global fit. F-specific KD values (Table 7) are from one technical experiment, and G-specific KD values (Table 8) are the mean of at least 2 technical replicates. Table 7. Dissociation constants (KD) of F-specific antibodies to RSV pre-F Table 8. Dissociation constants (KD) of G-specific antibodies to RSV G To determine the general epitope of each antibody, epitope binning was performed by biolayer interferometry (BLI). Streptavidin-coated biosensors were loaded with biotinylated preF or G at 0.5 µg / mL. For each RSV antigen tested, binning was observed with the following protocol: Baseline 30 s, loading 300 s, baseline 30 s, “blocking” mAb1600 s, baseline 30 s, “test” mAb2300 s. Blocking was calculated as a percentage of reduced binding during association with mAb2, compared to samples where mAb1 was replaced with buffer. Each antibody was tested for its ability to block the epitope of other antibodies, comparing the antibodies described herein to reference antibodies characterized in the literature (FIG.9 and FIG. 10). The results demonstrated that F-specific antibody 309-018 shares an epitope with D25, motavizumab, and AM14, suggesting that its antigenic site may be broader, overlapping with at least two previously-described sites, 0 and II (shown in FIG.9). Additionally, the highly potent G-specific antibody 309-007 binds to the CCD of G, and appears to partially share an epitope with the CCD- specific reference antibodies CB017.5 and CD3 (shown in FIG.10). The RSV G specific antibody 309-020 shares an epitope with another CCD specific antibody, CB002.5, but its antigenic site does not seem to overlap with that of antibody 309-007. Example 5: Crystal structure of the 309-007 Fab bound to the CCD of RSV G To determine the precise binding site of antibody 309-007 on the CCD of RSV G, a soluble 35 aa peptide (SEQ ID NO: 66) corresponding to the CCD of the RSV G protein (aa 164-198) and the Fab domain of antibody 309-007 (modified to contain a shorter Kappa loop, as described in Example 1) were expressed individually in mammalian Expi293 cells as described in Example 1, and purified by affinity chromatography. The 309-007 Fab and the purified CCD peptide were mixed for complex formation, concentrated, purified, and concentrated again to around 10 mg / mL, and used for crystallization (see Example 1). The crystal structure of the 309-007 Fab in complex with the peptide corresponding to the CCD of the RSV G protein (aa 164-198) was solved by X-ray crystallography at a 2.47 Å resolution (FIG.11). The asymmetric unit is comprised of two copies of the 309-007 Fab and two copies of the CCD, with each Fab interacting with its own CCD (FIGS.11A-11B). The interactions of the 309-007 Fabs with the CCD molecules were analyzed using PDBsum (FIG.11). The protein interactions between a single Fab and a single CCD were mediated by residues in the first, second and third complementarity-determining regions (CDRs) of the heavy and light chain of the 309-007 Fab (FIG.12). Residues from the 309-007 heavy chain interact with residues of conformational epitopes of the RSV G protein [aa 171-175 (VPCSI; SEQ ID NO: 77) of the strictly conserved central domain and aa S177 and W183 in the CX3C motif], as well as with aa 188-194 (RIPNKKP; SEQ ID NO: 87) of its heparin binding domain (FIG.11C). Residues of the 309-007 light chain interact with aa 192-193 (KK) and aa 195-197 (GKK) of the heparin binding domain of the RSV G protein. The footprint of the interaction of the 309-007 Fab on the CCD was close to but slightly offset from that of reference antibody CB017.5, and appeared different from those of 3D3 and CB002.5 (Nunez Castrejon, et al., J. Virol,, 96(7):e0220121, 2022). Interestingly, further analysis of the interactions between two 309-007 Fabs / CCD heterodimers revealed the presence of non-bonded cross-contacts of a CCD molecule from one of the Fab / CCD heterodimers with the heavy chain of the 309-007 Fab from the other heterodimer, and reciprocally (FIG.11B, diagonal lines between the two boxes). This cross-interaction occurs through the proline residue 106 in the CDR3 of the 309-007 heavy chain that seems to interact with the residues I175, C176 and N178 of the RSV G CCD (FIG.11D and FIG.12). This suggested that one 309-007 Fab could possibly interact with two CCDs. The sequence alignment between the heavy chains of 309-007 and reference antibody CB017.5 revealed a 4 aa insertion in 309-007. The P106 residue with the putative ability to mediate this inter-heterodimer interaction with the CCD is located within this 4-aa insertion that is present in the CDR3 of the 309-007 heavy chain, but not in that of CB017.5 (FIG.12). Thus, the molecular interactions deduced from the crystal structure of the 309- 007 Fab with the CCD peptide of RSV G provide a rationale for the strong interaction of antibody 309-007 with the RSV G protein. Example 6: Prophylactic protection of 309-007 against RSV challenge in hamsters The prophylactic efficacy of antibody 309-007 against RSV challenge was evaluated in 5-6- week-old golden Syrian hamsters (FIG.13). Four versions of 309-007 were evaluated: (i) the original unmodified 309-007 IgG3, (ii) a 309-007 IgG3 version further engineered by the introduction of the R491H mutation in the fragment crystallizable (Fc) region of the heavy chain to increase its half-life (309-007 IgG3 stab) (Stapleton NM, et al., Nat Commun 20:2:599, 2011), (iii) the IgG1 version of 309-007 and (iv) the IgG1 version of 309-007 further engineered by the introduction of the “YTE” motif mutations in the Fc region of the heavy chain to also increase its half-life (309-007 IgG1 stab) (Oganesyan V., et al., Mol Immunol 46(8-9):1750-5, 2009). FIG.13A shows the timeline of the hamster experiment. On day -1, four groups of hamsters (n=12 per group) received the indicated version of the 309-007 antibody (12 mg / kg, administered intraperitoneally). One group received the RSV G specific reference antibody CB017.5, included as a positive control, and another group received the anti-SARS-CoV-2 antibody CR3022, included as a negative control, delivered at the same dose and by the same route. One day later (day 0), all hamsters were challenged intranasally with recombinant RSV A2 (6 log10 PFU / hamster). The body weight of the hamsters increased from day -2 to day 3 post-challenge (pc), suggesting no major effect of the injected antibody or the RSV challenge (FIG.13B). On day 3 pc, serum was collected from each hamster to confirm the presence of the injected antibody by ELISA (FIG.14A). Of the 72 hamsters in each group, one animal in the group immunized with CB017.5 and one in the group immunized with 309-007 IgG3 had low levels of the injected antibody in their serum, suggesting incomplete uptake, and thus data from these two animals were removed from the data analysis (FIG.14A). Hamsters were euthanized by CO2 inhalation, nasal turbinates (NT) and lungs were harvested, and RSV titers in NT and lungs were determined. As expected, RSV replicated efficiently in the lungs of hamsters immunized with the negative control antibody CR3022 (geometric mean titer (GMT) of 4.2 log10PFU / g, FIG.13C). RSV GMTs in lungs from hamsters that had received the reference antibody CB017.5 were 8-fold lower compared to those in CR3022 immunized hamsters, but the difference between these groups did not reach statistical significance. Challenge virus GMTs in each of the groups of animals that had received versions of 309-007 were significantly lower compared to the CR3022 control group (20- to 79-fold reduction in GMTs; p=0.0016 to p<0.0001). The IgG1 version of 309-007 was the most protective (p<0.0001 compared to CR3022, and p= 0.0115 compared to CB017.5) (FIG.13C). None of the antibodies provided protection in the upper airways against RSV replication (FIG.14B). Example 7: Antibody 309-007 with hamster constant regions A hamster version of the 309-007 antibody was generated to evaluate the contribution of the Fc domain of 309-007 in its RSV neutralization potency in a hamster model. The hamster 309-007 light chain includes the 309-007 VL domain and a hamster lambda light chain constant region, while the hamster 309-007 heavy chain includes the 309-007 VH domain and the hamster IgG2a heavy chain constant region. The nucleotide and amino acid sequences of the hamster heavy and light chains are provided below. In each sequence, the constant regions are underlined. CMITGFFPADVHVEWEKNGQPEQNYKNTSPVLDTDGSYFMYSKLNVPKSSWEQGNIYVCSV LHEALRNHHTTKAISRSLGN It will be apparent that the precise details of the methods or compositions described may be varied or modified without departing from the spirit of the described aspects of the disclosure. We claim all such modifications and variations that fall within the scope and spirit of the claims below.

Claims

CLAIMS 1. A monoclonal antibody that specifically binds respiratory syncytial virus (RSV) glycoprotein (G) or fusion protein (F), comprising a variable heavy (VH) domain comprising a heavy chain complementarity determining region (HCDR) 1, a HCDR2 and a HCDR3, and a variable light (VL) domain comprising a light chain complementarity determining region (LCDR)1, a LCDR2, and a LCDR3, wherein: the VH domain comprises the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 33 and the VL domain comprises the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 34; the VH domain comprises the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 1 and the VL domain comprises the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 2; the VH domain comprises the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 9 and the VL domain comprises the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 10; the VH domain comprises the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 17 and the VL domain comprises the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO: 18; or the VH domain comprises the HCDR1, HCDR2 and HCDR3 sequences of SEQ ID NO: 25 and the VL domain comprises the LCDR1, LCDR2 and LCDR3 sequences of SEQ ID NO:

26.

2. The monoclonal antibody of claim 1, wherein the amino acid sequences of the HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 respectively comprise: SEQ ID NOs: 35, 36, 37, 38, 39, and 40; SEQ ID NOs: 81, 82, 83, 84, 85, and 86; SEQ ID NOs: 3, 4, 5, 6, 7, and 8; SEQ ID NOs: 11, 12, 13, 14, 15, and 16; SEQ ID NOs: 19, 20, 21, 22, 23, and 24; or SEQ ID NOs: 27, 28, 29, 30, 31, and 32.

3. The monoclonal antibody of claim 1 or claim 2, wherein: the amino acid sequence of the VH domain is at least 90% identical to SEQ ID NO: 33 and the amino acid sequence of the VL domain is at least 90% identical to SEQ ID NO: 34; the amino acid sequence of the VH domain is at least 90% identical to SEQ ID NO: 1 and the amino acid sequence of the VL domain is at least 90% identical to SEQ ID NO: 2; the amino acid sequence of the VH domain is at least 90% identical to SEQ ID NO: 9 and the amino acid sequence of the VL domain is at least 90% identical to SEQ ID NO: 10; the amino acid sequence of the VH domain is at least 90% identical to SEQ ID NO: 17 and the amino acid sequence of the VL domain is at least 90% identical to SEQ ID NO: 18; orthe amino acid sequence of the VH domain is at least 90% identical to SEQ ID NO: 25 and the amino acid sequence of the VL domain is at least 90% identical to SEQ ID NO:

26.

4. The monoclonal antibody of any one of claims 1-3, wherein: the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 33 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 34; the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 1 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 2; the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 9 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 10; the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 17 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO: 18; or the amino acid sequence of the VH domain comprises or consists of SEQ ID NO: 25 and the amino acid sequence of the VL domain comprises or consists of SEQ ID NO:

26.

5. The monoclonal antibody of any one of claims 1-4, which is a fully human antibody.

6. The monoclonal antibody of any one of claims 1-5, further comprising at least one heavy chain constant region and / or a light chain constant region.

7. The monoclonal antibody of any one of claims 1-6, wherein the monoclonal antibody is an IgG.

8. The monoclonal antibody of claim 7, wherein the IgG is IgG1 or IgG3.

9. The monoclonal antibody of any one of claims 1-6, wherein the monoclonal antibody is an IgA.

10. The monoclonal antibody of claim 9, wherein the IgA is dimeric and comprises a J chain.

11. The monoclonal antibody of any one of claims 6-10, wherein the at least one heavy chain constant region is a recombinant constant region comprising a modification that increases half- life of the antibody.

12. The monoclonal antibody of claim 11, wherein the monoclonal antibody is a human IgG1 antibody and comprises M252Y, S254T and T256E amino acid substitutions.

13. The monoclonal antibody of claim 11, wherein the monoclonal antibody is a human IgG3 antibody and comprises a R511H amino acid substitution.

14. The monoclonal antibody of any one of claims 1-5, wherein the monoclonal antibody is an antigen binding fragment selected from a Fab fragment, a Fab’ fragment, a F(ab’)2fragment, a single chain variable fragment (scFv) or a disulfide stabilized variable fragment (dsFv).

15. The monoclonal antibody of any one of claims 1-14, wherein the monoclonal antibody neutralizes RSV.

16. The monoclonal antibody of claim 15, wherein the neutralization inhibitory concentration 50 (IC50) of the monoclonal antibody is less than 50 ng / ml, less than 40 ng / ml, less than 30 ng / ml, less than 20 ng / ml, less than 10 ng / ml, less than 5 ng / ml, or less than 1 ng / ml.

17. The monoclonal antibody of any one of claims 1-16, further comprising an effector molecule or a detectable label.

18. The monoclonal antibody of claim 17, wherein the detectable label is a fluorescent, enzymatic, radioactive or nucleic acid label.

19. A bispecific antibody, comprising the monoclonal antibody of any one of claims 1-16 and a second monoclonal antibody.

20. An isolated nucleic acid molecule encoding the VH domain, the VL domain, or both the VH domain and the VL domain of the monoclonal antibody of any one of claims 1-16.

21. The isolated nucleic acid molecule of claim 20, wherein the VH domain and / or the VL domain of the monoclonal antibody comprise the nucleic acid sequences set forth as: SEQ ID NOs: 49 and 50, respectively, or degenerate variants thereof; SEQ ID NOs: 41 and 42, respectively, or degenerate variants thereof; SEQ ID NOs: 43 and 44, respectively, or degenerate variants thereof; SEQ ID NOs: 45 and 46, respectively, or degenerate variants thereof; or SEQ ID NOs: 47 and 48, respectively, or degenerate variants thereof.

22. The isolated nucleic acid molecule of claim 20, wherein the nucleotide sequence encoding the VH domain, the VL domain, or both the VH domain and the VL domain is codon- optimized.

23. The isolated nucleic acid molecule of claim 22, wherein VH domain and / or the VL domain of the monoclonal antibody comprise the nucleic acid sequences set forth as: SEQ ID NOs: 59 and 60, respectively, or degenerate variants thereof; SEQ ID NOs: 51 and 52, respectively, or degenerate variants thereof; SEQ ID NOs: 53 and 54, respectively, or degenerate variants thereof; SEQ ID NOs: 55 and 56, respectively, or degenerate variants thereof; or SEQ ID NOs: 57 and 58, respectively, or degenerate variants thereof.

24. The isolated nucleic acid molecule of any one of claims 20-23, operably linked to a promoter.

25. A vector comprising the nucleic acid molecule of any one of claims 20-24.

26. An isolated host cell comprising the vector of claim 25.

27. A composition, comprising a pharmaceutically acceptable carrier and the monoclonal antibody of any one of claims 1-18, the bispecific antibody of claim 19, the nucleic acid molecule of any one of claims 20-24, or the vector of claim 25.

28. A composition, comprising two or more monoclonal antibodies of any one of claims 1-18, wherein at least one antibody specifically binds RSV G and at least one antibody specifically binds RSV F.

29. The composition of claim 28, comprising a dimeric IgA comprising one antibody that specifically binds RSV F and one antibody that specifically binds RSV G.

30. The composition of claim 28 or claim 29, further comprising a pharmaceutically acceptable carrier.

31. The composition of any one of claims 27-30, wherein the composition is sterile and / or is in unit dosage form or a multiple thereof.

32. A method of detecting an RSV infection in a subject, comprising: contacting a biological sample from the subject with the monoclonal antibody of any one of claims 1-18 under conditions sufficient to form an immune complex; and detecting the presence of the immune complex in the sample, wherein the presence of the immune complex in the sample indicates that the subject has an RSV infection.

33. A method of preventing, inhibiting or treating an RSV infection, comprising administering to a subject with or at risk of an RSV infection a therapeutically effective amount of the monoclonal antibody of any one of claims 1-18, the bispecific monoclonal antibody of claim 19, the nucleic acid molecule of any one of claims 20-24, the vector of claim 25, or the composition of any one of claims 27-31, thereby preventing, inhibiting or treating an RSV infection.

34. The method of claim 33, wherein the subject has been exposed to RSV but has not been diagnosed as having an RSV infection and / or does not yet have any symptoms of an RSV infection.

35. The method of claim 33, wherein the subject has been diagnosed with an RSV infection and / or has symptoms of an RSV infection.

36. The method of any one of claims 33-35, wherein the monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition is administered in multiple doses.

37. The method of any one of claims 33-36, wherein the monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition is administered in two, three, four or five doses.

38. The method of any one of claims 33-35, wherein the monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition is administered in a single dose.

39. The method of any one of claims 33-38, wherein the subject is administered the monoclonal antibody, bispecific antibody, nucleic acid molecule, vector or composition as a prime treatment and the subject is later boosted with an RSV vaccine or a chimeric attenuated respiratory virus vaccine.

40. The method of any one of claims 33-39, wherein the monoclonal antibody is an IgA or dimeric IgA and the monoclonal antibody is administered intranasally.

41. Use of the monoclonal antibody of any one of claims 1-18, the bispecific monoclonal antibody of claim 19, the nucleic acid molecule of any one of claims 20-24, the vector of claim 25, or the composition of any one of claims 27-31 to prevent, inhibit, treat, or diagnose an RSV infection in a subject.

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