HPIV3-neutralizing antibodies and methods of use thereof

Abstract

The present disclosure relates to methods of using a human parainfluenza virus 3 (HPIV3) neutralizing antibody to prevent and / or treat HPIV infections.

Description

[0001] Docket No.10644-185WO1 HPIV3-NEUTRALIZING ANTIBODIES AND METHODS OF USE THEREOF CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority to, and the benefit of, U.S. Provisional Patent Application No.63 / 626,144, filed January 29, 2024, which is incorporated by reference herein in its entirety. STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH This invention was made with Government Support under Grant No. R01 AI175245 awarded by the National Institutes of Health. The Government has certain rights in the invention. REFERENCE TO SEQUENCE LISTING The sequence listing submitted on January 29, 2025, as an .XML file entitled “10644- 185WO1_ST26” created on January 24, 2025, and having a file size of 223,789 bytes is hereby incorporated by reference pursuant to 37 C.F.R. § 1.52(e)(5). FIELD The present disclosure relates to methods of using a human parainfluenza virus 3 (HPIV3) neutralizing antibody to prevent and / or treat HPIV infections. BACKGROUND Human parainfluenza virus 3 (HPIV3) is a widespread pathogen causing severe, lethal respiratory illness in at-risk populations. Effective countermeasures to prevent HPIV3 infections are in various stages of development; however, licensed therapeutic and prophylactic options are not available. The fusion glycoprotein (HPIV3 F), responsible for facilitating viral entry into host cells, is a major target of neutralizing antibodies that inhibit infection. While several neutralizing antibodies against a small number of HPIV3 F epitopes have been identified to date, relatively little is known about the antibody response to HPIV3, compared to other pathogens, such as influenza virus, and severe acute respiratory syndrome-related coronavirus (SARS-CoV-2). Docket No.10644-185WO1 Given the limitations described above, there is a need to identify and exploit antigenic sites on HPIV3 to help guide efforts for effective vaccine and therapeutic development. The compositions and methods disclosed herein address these needs and more. SUMMARY The present disclosure provides a human parainfluenza virus 3 (HPIV3) neutralizing antibody and compositions thereof. The present disclosure also provides methods of generating, identifying, isolating, detecting, and / or collecting an HPIV3 neutralizing antibody using a Linking B cell Receptor Sequence to Antigen Specificity through Sequencing (LIBRA- seq). The present disclosure also provides methods of preventing, treating, ameliorating, decreasing, and / or eliminating an HPIV3 infection in a subject. In some aspects, disclosed herein is a neutralizing antibody comprising a heavy chain region and a light chain region, wherein the heavy chain region comprises SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, or a variant thereof, and the light chain region comprises SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123, SEQ ID NO: 124, SEQ ID NO: 125, SEQ ID NO: 126, SEQ ID NO: 127, or a variant thereof. In some embodiments, the heavy chain region comprises a variable heavy chain comprising SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, or a variant thereof. In some embodiments, the light chain region comprises a variable light chain comprising SEQ ID NO: 90, SEQ ID NO: 91, SEQ ID NO: 92, SEQ ID NO: 93, SEQ ID NO: 94, SEQ ID NO: 95, SEQ ID NO: 96, SEQ ID NO: 97, SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101, SEQ ID NO: 102, SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107, or a variant thereof. In some embodiments, the neutralizing antibody comprises a first, a second, and a third heavy chain complementarity determining region (CDR) CDRH1, CDRH2, and CDRH3 selected from the group consisting of SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ Docket No.10644-185WO1 ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61, SEQ ID NO:62, SEQ ID NO: 63, SEQ ID NO: 64, SEQ ID NO: 65, SEQ ID NO: 66, SEQ ID NO: 67, SEQ ID NO:68, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 71, SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, SEQ ID NO: 78, SEQ ID NO: 79, SEQ ID NO: 80, SEQ ID NO: 81, SEQ ID NO: 82, SEQ ID NO: 83, SEQ ID NO: 84, SEQ ID NO:85, SEQ ID NO: 86, SEQ ID NO: 87, SEQ ID NO: 88, SEQ ID NO: 89, and SEQ ID NO: 163; and a first, a second, and a third light chain complementarity determining regions CDRL1, CDRL2, and CDRL3 selected from the group consisting of SEQ ID NO:128, SEQ ID NO: 129, SEQ ID NO: 130, SEQ ID NO:131, SEQ ID NO:132, SEQ ID NO: 133, SEQ ID NO: 134, SEQ ID NO: 135, SEQ ID NO:136, SEQ ID NO: 137, SEQ ID NO: 138, SEQ ID NO: 139, SEQ ID NO: 140, SEQ ID NO:141, SEQ ID NO:142, SEQ ID NO:143, SEQ ID NO: 144, SEQ ID NO: 145, SEQ ID NO: 146, SEQ ID NO: 147, SEQ ID NO: 148, SEQ ID NO: 149, SEQ ID NO: 150, SEQ ID NO: 151, SEQ ID NO: 152, SEQ ID NO: 153, SEQ ID NO: 154, SEQ ID NO: 155, SEQ ID NO: 156, SEQ ID NO: 157, SEQ ID NO: 158, SEQ ID NO: 159, SEQ ID NO:160, SEQ ID NO: 161, SEQ ID NO: 162, SEQ ID NO:164, SEQ ID NO: 165 and amino acid sequences selected from DVS, GVD, ANN, EDN, RND, DAS, ATS, KVS, EVS, RNS, MAS, AAS, and GTS. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 38, SEQ ID NO: 55, and SEQ ID NO: 72, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 128, amino acid sequence DVS, and SEQ ID NO: 145, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 39, SEQ ID NO: 56, and SEQ ID NO:73, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 129, amino acid sequence GVD, and SEQ ID NO: 146, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 40, SEQ ID NO:57, and SEQ ID NO:74, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 130, amino acid sequence ANN, and SEQ ID NO: 147, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 41, SEQ ID NO: 58, and SEQ ID NO:75, respectively; and Docket No.10644-185WO1 the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 131, amino acid sequence EDN, and SEQ ID NO: 148, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 42, SEQ ID NO:55, and SEQ ID NO: 76; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 132, amino acid sequence RND, and SEQ ID NO:149, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 43, SEQ ID NO: 59, and SEQ ID NO: 77; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 133, amino acid sequence DAS, and SEQ ID NO: 150, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 44, SEQ ID NO: 60, and SEQ ID NO: 78, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 134, amino acid sequence ATS, and SEQ ID NO: 151, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 45, SEQ ID NO: 61, and SEQ ID NO: 79, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 135, amino acid sequence DAS, and SEQ ID NO:152, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 46, SEQ ID NO: 62, and SEQ ID NO: 80, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 136, amino acid sequence KVS, and SEQ ID NO: 153, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 47, SEQ ID NO: 63, and SEQ ID NO:81, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 128, amino acid sequence EVS, SEQ ID NO: 154, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 48, SEQ ID NO: 64, and SEQ ID NO: 82, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 137, amino acid sequence RNS, and SEQ ID NO: 155, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 49, SEQ ID NO: 65, and SEQ ID NO: 83, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 138, amino acid sequence MAS, and SEQ ID NO: 156, respectively. Docket No.10644-185WO1 In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 50, SEQ ID NO: 66, and SEQ ID NO: 84, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 139, amino acid sequence MAS, and SEQ ID NO: 157, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 51, SEQ ID NO: 67, and SEQ ID NO: 85, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 140, amino acid sequence EVS, and SEQ ID NO: 158, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 52, SEQ ID NO: 68, and SEQ ID NO: 86, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 141, amino acid sequence DAS, and SEQ ID NO: 159, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 53, SEQ ID NO: 69, and SEQ ID NO: 87, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 142, amino acid sequence AAS, and SEQ ID NO: 160, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 54, SEQ ID NO: 70, and SEQ ID NO: 88, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 143, SEQ ID NO: 144, and SEQ ID NO: 161, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 42, SEQ ID NO: 71, and SEQ ID NO: 89, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 134, amino acid sequence GTS, and SEQ ID NO: 162, respectively. In some aspects, disclosed herein is a method of treating or preventing a human parainfluenza virus 3 (HPIV3) infection in a subject in need thereof, the method comprising administering to the subject a pharmaceutically effective amount of a composition comprising the HPIV3 neutralizing antibody of any preceding aspect, wherein the neutralizing antibody decreases one or more respiratory symptoms in the subject relative to an untreated subject. In some aspects, disclosed herein is a method of generating a human parainfluenza virus 3 (HPIV3) neutralizing antibody, the method comprising detecting a B cell using Linking B cell Receptor Sequence to Antigen Specificity through Sequencing (LIBRA-seq), wherein the B cell produces the HPIV3 neutralizing antibody of any preceding aspect, and wherein the HPIV3 neutralizing antibody targets an HPIV3 fusion (HPIV3 F) glycoprotein. Docket No.10644-185WO1 In some embodiments, the HPIV3 neutralizing antibody targets an HPIV3 fusion (HPIV3 F) glycoprotein. In some embodiments, the HPIV3 neutralizing antibody targets at least one epitope of the HPIV3 F glycoprotein. In some embodiments, the at least one epitope of the HPIV3 F glycoprotein comprises an Ø antigenic site. In some embodiments, the at least one epitope of the HPIV3 F glycoprotein comprises an X antigenic site. In some embodiments, the HPIV neutralizing antibody is encoded by an immunoglobulin heavy variable IGHV 5-51 gene. In some embodiments, the HPIV neutralizing antibody is encoded by an immunoglobulin light chain gene comprising IGLV 2- 23, IGLV 2-11, IGLV 1-51, IGLV 1-44, IGLV 2-23, IGLV 1-40, IGKV 1-33, IGKV 3-20, IGKV 1-5, or IGKV 4-69. In some embodiments, the composition further comprises a pharmaceutically acceptable carrier selected from an excipient, diluent, buffer, stabilizer, solubilizer, lipid, nanoparticle, or any variant thereof. In some embodiments, the composition is further administered with a pharmaceutical composition selected from an analgesic, an antibody, an antibiotic, a decongestant, a cough suppressant, or any combinations thereof. In some embodiments, the one or more respiratory symptoms comprise fever, coughing, congested sinuses, respiratory inflammation, wheezing, sneezing, or any combinations thereof. BRIEF DESCRIPTION OF FIGURES The accompanying figures, which are incorporated in and constitute a part of this specification, illustrate several aspects described below. FIGS. 1A and 1B show the epitope mapping of HPIV3 F-specific antibodies. Figure 1A shows the ELISA binding of 19 recombinantly produced antibodies against HPIV3 prefusion F trimer, calculated as absorbance at 450 nm. ELISA area under the curve (AUC) shown as a heatmap from minimum (white) to maximum binding (blue). Experiments were performed in technical and biological duplicate. Figure 1B shows the antibody-antibody competition binding against published HPIV3 site specific antibodies. Percentage of binding of biotinylated antibody is shown as a heatmap from 0% (black) to 100% (white). Non- biotinylated competitor antibodies were coated first, and then biotinylated PI3-E12, PIA174, and 3X1 were added to detect competition. Strong (≤ 40%), intermediate (41-70%) and weak / non-competing (≥71%) is calculated as the signal obtained for binding of the biotin- labelled reference antibody in the presence of the unlabeled antibody, expressed as a percentage of the binding of the reference antibody alone. Experiments were performed in technical and biological duplicate Antigenic sites are depicted on PyMOL rendered 3D constructed Docket No.10644-185WO1 representation of the HPIV3 prefusion trimer from PDB ID 6MJZ. Site Ø is shown in red based on PIA174’s structural epitope residues from its complex with F (PDB ID 6MJZ), site X is depicted in yellow as 3x1’s epitope residues from PDB ID 8DG8. FIG. 2 shows the antibody neutralization against HPIV3 C243 via PRNT. IC50values, expressed as a heatmap with strong neutralization (<0.1 ug / ml) shown in blue and weak / non neutralizing (>10 ug / ml) shown in white, are calculated by non-linear regression analysis by GraphPad Prism software. Neutralization assays were performed in technical triplicate; data are represented as mean ± SD. FIGS. 3A and 3B show the public clonotype analysis of HPIV3-specific antibody neutralizing antibodies. Figure 3A shows the count of similar antibodies found in Jaffe et al. (Jaffe, D.B., Shahi, P., Adams, B.A., Chrisman, A.M., Finnegan, P.M., Raman, N., Royall, A.E., Tsai, F., Vollbrecht, T., Reyes, D.S., et al (2022) [https: / / rdcu.be / ds9OS]). Each antibody is represented as a point, with its x-axis coordinate reflecting the number of antibodies sharing both heavy and light variable genes and having a CDRH3 with ≥50% amino acid sequence identity. The y-axis coordinate corresponds to the number of antibodies with the same heavy and light variable genes and a CDRL3 sequence ≥50% identical. Figure 3B shows the frequency of our HPIV3-specific antibody sequence features in public databases. The plots compare all antibodies from Jaffe et al. (each as a dot) against a reference HPIV3-directed antibody, indicated above each plot. The dot's position reflects the CDRH3 (x-axis) and CDRL3 (y-axis) amino acid identity to the PIV3-specific antibody, with color coding indicating shared V gene usage. Inclusion criteria for dots are at least one matching V gene or ≥50% CDR3 sequence identity with the reference HPIV3-specific antibody. FIG. 4 shows the competitive binding of antibodies that do not map to site Ø or site X. Antibody-antibody competition binding of HPIV3 specific antibodies that do not compete with site Ø or site X. Percentage of binding biotinylated antibody is shown as a heatmap from 0% (black) to 100% (white). Non-biotinylated competitor antibodies were coated first, and then biotinylated antibodies were added to detect competition. Strong (≤40%), intermediate (41- 70%), and weak / non-competing (≥71%) in calculated as the signal obtained for binding of the biotin-labeled reference antibody in the presence of the unlabeled antibody, expressed as a percentage of the binding of the reference antibody alone. FIGS. 5A and 5B show the HPIV PRNT and RTCA HPIV3 neutralization. Figure 5A shows the antibody neutralization against HPIV C35 via PRNT. Neutralization assays were performed in technical triplicate; data are represented as mean ± SD. Figure 5B shows the real Docket No.10644-185WO1 time cell analysis (RTCA) HPIV3 JS neutralization by 75163-6. Neutralization assays were performed in technical duplicate; data are represented as mean ± SD. FIG. 6 shows the CDRH3 sequence identity of IGHV 5-51 antibodies targeting site Ø. Pairwise identities calculated at the amino acid level are shown as a heatmap with minimum values shown in blue and maximum values shown in red. DETAILED DESCRIPTION The following description of the disclosure is provided as an enabling teaching of the disclosure in its best, currently known embodiment(s). To this end, those skilled in the relevant art will recognize and appreciate that many changes can be made to the various embodiments of the invention described herein, while still obtaining the beneficial results of the present disclosure. It will also be apparent that some of the desired benefits of the present disclosure can be obtained by selecting some of the features of the present disclosure without utilizing other features. Accordingly, those who work in the art will recognize that many modifications and adaptations to the present disclosure are possible and can even be desirable in certain circumstances and are a part of the present disclosure. Thus, the following description is provided as illustrative of the principles of the present disclosure and not in limitation thereof. Reference will now be made in detail to the embodiments of the invention, examples of which are illustrated in the drawings and the examples. This invention may, however, be embodied in many different forms and should not be construed as limited to the embodiments set forth herein. Terminology Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood to one of ordinary skill in the art to which this disclosure belongs. The term “comprising” and variations thereof as used herein is used synonymously with the term “including” and variations thereof and are open, non-limiting terms. Although the terms “comprising” and “including” have been used herein to describe various embodiments, the terms “consisting essentially of” and “consisting of” can be used in place of “comprising” and “including” to provide for more specific embodiments and are also disclosed. As used in this disclosure and in the appended claims, the singular forms “a”, “an”, “the”, include plural referents unless the context clearly dictates otherwise. The following definitions are provided for the full understanding of terms used in this specification. Docket No.10644-185WO1 The terms "about" and "approximately" are defined as being “close to” as understood by one of ordinary skill in the art. In one non-limiting embodiment the terms are defined to be within 10%. In another non-limiting embodiment, the terms are defined to be within 5%. In still another non-limiting embodiment, the terms are defined to be within 1%. As used herein, the terms "may," "optionally," and "may optionally" are used interchangeably and are meant to include cases in which the condition occurs as well as cases in which the condition does not occur. Thus, for example, the statement that a formulation "may include an excipient" is meant to include cases in which the formulation includes an excipient as well as cases in which the formulation does not include an excipient. “Composition” refers to any agent that has a beneficial biological effect. Beneficial biological effects include both therapeutic effects, e.g., treatment of a disorder or other undesirable physiological condition, and prophylactic effects, e.g., prevention of a disorder or other undesirable physiological condition. The terms also encompass pharmaceutically acceptable, pharmacologically active derivatives of beneficial agents specifically mentioned herein, including, but not limited to, a vector, polynucleotide, cells, salts, esters, amides, proagents, active metabolites, isomers, fragments, analogs, and the like. When the term “composition” is used, then, or when a particular composition is specifically identified, it is to be understood that the term includes the composition per se as well as pharmaceutically acceptable, pharmacologically active vector, polynucleotide, salts, esters, amides, proagents, conjugates, active metabolites, isomers, fragments, analogs, etc. "Comprising" is intended to mean that the compositions, methods, etc. include the recited elements, but do not exclude others. "Consisting essentially of'' when used to define compositions and methods, shall mean including the recited elements, but excluding other elements of any essential significance to the combination. Thus, a composition consisting essentially of the elements as defined herein would not exclude trace contaminants from the isolation and purification method and pharmaceutically acceptable carriers, such as phosphate buffered saline, preservatives, and the like. "Consisting of'' shall mean excluding more than trace elements of other ingredients and substantial method steps for administering the compositions provided and / or claimed in this disclosure. Embodiments defined by each of these transition terms are within the scope of this disclosure. An "increase" can refer to any change that results in a greater amount of a symptom, disease, composition, condition, or activity. An increase can be any individual, median, or average increase in a condition, symptom, activity, composition in a statistically significant amount. Thus, the increase can be a 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, Docket No.10644-185WO1 55, 60, 65, 70, 75, 80, 85, 90, 95, 100% or more increase so long as the increase is statistically significant. A "decrease" can refer to any change that results in a smaller amount of a symptom, disease, composition, condition, or activity. A substance is also understood to decrease the genetic output of a gene when the genetic output of the gene product with the substance is less relative to the output of the gene product without the substance. Also, for example, a decrease can be a change in the symptoms of a disorder such that the symptoms are less than previously observed. A decrease can be any individual, median, or average decrease in a condition, symptom, activity, composition in a statistically significant amount. Thus, the decrease can be a 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% decrease so long as the decrease is statistically significant. "Inhibit," "inhibiting," and "inhibition" mean to decrease an activity, response, condition, disease, or other biological parameter. This can include but is not limited to the complete ablation of the activity, response, condition, or disease. This may also include, for example, a 10% reduction in the activity, response, condition, or disease as compared to the native or control level. Thus, the reduction can be a 10, 20, 30, 40, 50, 60, 70, 80, 90, 100%, or any amount of reduction below, above, or in between the given ranges as compared to native or control levels. By “reduce” or other forms of the word, such as “reducing” or “reduction,” means lowering of an event or characteristic (e.g., tumor growth). It is understood that this is typically in relation to some standard or expected value, in other words it is relative, but that it is not always necessary for the standard or relative value to be referred to. For example, “reduces tumor growth” means reducing the rate of growth of a tumor relative to a standard or a control. By “prevent” or other forms of the word, such as “preventing” or “prevention,” is meant to stop a particular event or characteristic, to stabilize or delay the development or progression of a particular event or characteristic, or to minimize the chances that a particular event or characteristic will occur. Prevent does not require comparison to a control as it is typically more absolute than, for example, reduce. As used herein, something could be reduced but not prevented, but something that is reduced could also be prevented. Likewise, something could be prevented but not reduced, but something that is prevented could also be reduced. It is understood that where reduce or prevent are used, unless specifically indicated otherwise, the use of the other word is also expressly disclosed. The term “subject” refers to any individual who is the target of administration or treatment. The subject can be a vertebrate, for example, a mammal. In one aspect, the subject Docket No.10644-185WO1 can be human, non-human primate, bovine, equine, porcine, canine, or feline. The subject can also be a guinea pig, rat, hamster, rabbit, mouse, or mole. Thus, the subject can be a human or veterinary patient. The term “patient” refers to a subject under the treatment of a clinician, e.g., physician. The term “therapeutically effective amount” refers to the amount of the composition used is of sufficient quantity to ameliorate one or more causes or symptoms of a disease or disorder. Such amelioration only requires a reduction or alteration, not necessarily elimination. A “pharmaceutically effective amount” of a drug necessary to achieve a therapeutic effect may vary according to factors such as the age, sex, and weight of the subject. Dosage regimens can be adjusted to provide the optimum therapeutic response. For example, several divided doses may be administered daily, or the dose may be proportionally reduced as indicated by the exigencies of the therapeutic situation. The term “amino acid,” includes but is not limited to amino acids contained in the group consisting of alanine (Ala or A), cysteine (Cys or C), aspartic acid (Asp or D), glutamic acid (Glu or E), phenylalanine (Phe or F), glycine (Gly or G), histidine (His or H), isoleucine (Ile or I), lysine (Lys or K), leucine (Leu or L), methionine (Met or M), asparagine (Asn or N), proline (Pro or P), glutamine (Gln or Q), arginine (Arg or R), serine (Ser or S), threonine (Thr or T), valine (Val or V), tryptophan (Trp or W), and tyrosine (Tyr or Y) residues. The term “amino acid residue” also may include amino acid residues contained in the group consisting of homocysteine, 2-Aminoadipic acid, N-Ethylasparagine, 3-Aminoadipic acid, Hydroxylysine, β-alanine, β-Amino-propionic acid, allo-Hydroxylysine acid, 2-Aminobutyric acid, 3-Hydroxyproline, 4-Aminobutyric acid, 4-Hydroxyproline, piperidinic acid, 6- Aminocaproic acid, Isodesmosine, 2-Aminoheptanoic acid, allo-Isoleucine, 2- Aminoisobutyric acid, N-Methylglycine, sarcosine, 3-Aminoisobutyric acid, N- Methylisoleucine, 2-Aminopimelic acid, 6-N-Methyllysine, 2,4-Diaminobutyric acid, N- Methylvaline, Desmosine, Norvaline, 2,2′-Diaminopimelic acid, Norleucine, 2,3- Diaminopropionic acid, Ornithine, and N-Ethylglycine. Typically, the amide linkages of the peptides are formed from an amino group of the backbone of one amino acid and a carboxyl group of the backbone of another amino acid. Reference also is made herein to peptides, polypeptides, proteins, and compositions comprising peptides, polypeptides, and proteins. As used herein, a polypeptide and / or protein is defined as a polymer of amino acids, typically of length≥100 amino acids (Garrett & Grisham, Biochemistry, 2nd edition, 1999, Brooks / Cole, 110). A peptide is defined as a short polymer of amino acids, of a length typically of 20 or less amino acids, and more typically of Docket No.10644-185WO1 a length of 12 or less amino acids (Garrett & Grisham, Biochemistry, 2nd edition, 1999, Brooks / Cole, 110). The peptides, polypeptides, and proteins disclosed herein may be modified to include non-amino acid moieties. Modifications may include but are not limited to carboxylation (e.g., N-terminal carboxylation via addition of a di-carboxylic acid having 4-7 straight-chain or branched carbon atoms, such as glutaric acid, succinic acid, adipic acid, and 4,4- dimethylglutaric acid), amidation (e.g., C-terminal amidation via addition of an amide or substituted amide such as alkylamide or dialkylamide), PEGylation (e.g., N-terminal or C- terminal PEGylation via additional of polyethylene glycol), acylation (e.g., O-acylation (esters), N-acylation (amides), S-acylation (thioesters)), acetylation (e.g., the addition of an acetyl group, either at the N-terminus of the protein or at lysine residues), formylation lipoylation (e.g., attachment of a lipoate, a C8 functional group), myristoylation (e.g., attachment of myristate, a C14 saturated acid), palmitoylation (e.g., attachment of palmitate, a C16 saturated acid), alkylation (e.g., the addition of an alkyl group, such as an methyl at a lysine or arginine residue), isoprenylation or prenylation (e.g., the addition of an isoprenoid group such as farnesol or geranylgeraniol), amidation at C-terminus, glycosylation (e.g., the addition of a glycosyl group to either asparagine, hydroxylysine, serine, or threonine, resulting in a glycoprotein). Distinct from glycation, which is regarded as a nonenzymatic attachment of sugars, polysialylation (e.g., the addition of polysialic acid), glypiation (e.g., glycosylphosphatidylinositol (GPI) anchor formation, hydroxylation, iodination (e.g., of thyroid hormones), and phosphorylation (e.g., the addition of a phosphate group, usually to serine, tyrosine, threonine, or histidine). The phrases “percent identity” and “% identity,” as applied to polypeptide sequences, refer to the percentage of residue matches between at least two polypeptide sequences aligned using a standardized algorithm. Methods of polypeptide sequence alignment are well-known. Some alignment methods consider conservative amino acid substitutions. Such conservative substitutions, explained in more detail above, generally preserve the charge and hydrophobicity at the site of substitution, thus preserving the structure (and therefore function) of the polypeptide. Percent identity for amino acid sequences may be determined as understood in the art. (See, e.g., U.S. Pat. No.7,396,664, which is incorporated herein by reference in its entirety). A suite of commonly used and freely available sequence comparison algorithms is provided by the National Center for Biotechnology Information (NCBI) Basic Local Alignment Search Tool (BLAST) (Altschul, S. F. et al. (1990) J. Mol. Biol.215:403410), which is available from several sources, including the NCBI, Bethesda, Md., at its website. The BLAST software suite Docket No.10644-185WO1 includes various sequence analysis programs including “blastp,” that is used to align a known amino acid sequence with other amino acids sequences from a variety of databases. The term “variant” means a polypeptide derived from a parent polypeptide by one or more (several) alteration(s), i.e., a substitution, insertion, and / or deletion, at one or more (several) positions. A substitution means a replacement of an amino acid occupying a position with a different amino acid; a deletion means removal of an amino acid occupying a position; and an insertion means adding 1 or more, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10, preferably 1-3 amino acids immediately adjacent an amino acid occupying a position. In relation to substitutions, ‘immediately adjacent’ may be to the N-side (‘upstream’) or C-side (‘downstream’) of the amino acid occupying a position (‘the named amino acid’). Therefore, for an amino acid named / numbered ‘X,’ the insertion may be at position ‘X+1’ (‘downstream’) or at position ‘X−1’ (‘upstream’). A “variant” of a particular polypeptide sequence may be defined as a polypeptide sequence having at least 50% sequence identity to the particular polypeptide sequence over a certain length of one of the polypeptide sequences using blastp with the “BLAST 2 Sequences” tool available at the National Center for Biotechnology Information's website. (See Tatiana A. Tatusova, Thomas L. Madden (1999), “Blast 2 sequences—a new tool for comparing protein and nucleotide sequences”, FEMS Microbiol Lett. 174:247-250). In some embodiments a variant polypeptide may show, for example, at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or greater sequence identity over a certain defined length relative to a reference polypeptide. A variant polypeptide may have substantially the same functional activity as a reference polypeptide. For example, a variant polypeptide may exhibit or more biological activities associated with binding a ligand and / or binding DNA at a specific binding site. Variants comprising a fragment of a reference amino acid sequence or nucleotide sequence are contemplated herein. A “fragment” is a portion of an amino acid sequence or a nucleotide sequence which is identical in sequence to but shorter in length than the reference sequence. A fragment may comprise up to the entire length of the reference sequence, minus at least one nucleotide / amino acid residue. For example, a fragment may comprise from 5 to 1000 contiguous nucleotides or contiguous amino acid residues of a reference polynucleotide or reference polypeptide, respectively. In some embodiments, a fragment may comprise at least 5, 10, 15, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 40, 50, 60, 70, 80, 90, 100, 150, 250, or 500 contiguous nucleotides or contiguous amino acid residues of a reference polynucleotide or Docket No.10644-185WO1 reference polypeptide, respectively. Fragments may be preferentially selected from certain regions of a molecule, for example the N-terminal region and / or the C-terminal region of a polypeptide or the 5′-terminal region and / or the 3′ terminal region of a polynucleotide. The term “at least a fragment” encompasses the full length polynucleotide or full length polypeptide. The term “administer,” “administering”, or derivatives thereof refer to delivering a composition, substance, inhibitor, or medication to a subject or object by one or more the following routes: oral, topical, intravenous, subcutaneous, transcutaneous, transdermal, intramuscular, intra-joint, parenteral, intra-arteriole, intradermal, intraventricular, intracranial, intraperitoneal, intralesional, intranasal, rectal, vaginal, by inhalation or via an implanted reservoir. The term “parenteral” includes subcutaneous, intravenous, intramuscular, intra- articular, intra-synovial, intrasternal, intrathecal, intrahepatic, intralesional, and intracranial injections or infusion techniques. An “epitope” or “antigenic determinant” refer to the part of an antigen, a molecular structure, or foreign particulate that can bind to a specific antibody or T-cell receptor. The presence of antigens or epitopes of antigens within a host can illicit an immune response. An “antigen” refers to a molecule, moiety, foreign particulate matter, or an allergen that can bind to a specific antibody or T cell receptor. The presence of antigens within a host can illicit an immune response against said molecule, moiety, foreign particulate matter, or allergen. An “adjuvant” refers to a drug, molecule, substance, or a combination thereof that is used to increase the efficacy or potency of certain therapeutic agents, such as for example vaccines and / or antibodies. “Adjuvant(s)” are often at least one ingredient used in some vaccines that help create a stronger immune response in the host receiving said vaccine. A “vaccine” refers to a biological preparation that provides active acquired immunity to a particular infectious diseases caused by a virus, bacteria, parasite, or any other microorganisms. Vaccines typically comprise an agent or several agents, also referred to as antigens, resembling the disease-causing microorganism and is often made from weakened or killed forms of the microbe, its toxins, or its surface proteins / peptides. Vaccines are also made to comprise additional components, such as adjuvants, preservatives, and / or stabilizers to boost the immune response, improve safety, and improve vaccine storage. “Composition” refers to any agent that has a beneficial biological effect. Beneficial biological effects include both therapeutic effects, e.g., treatment of a disorder or other undesirable physiological condition (such as, for example, treatment of an HPIV infection), Docket No.10644-185WO1 and prophylactic effects, e.g., prevention of a disorder or other undesirable physiological condition (such as, for example prevention of an HPIV infection). The terms also encompass pharmaceutically acceptable, pharmacologically active derivatives of beneficial agents specifically mentioned herein, including, but not limited to, a vector, polynucleotide, cells, salts, esters, amides, proagents, active metabolites, isomers, fragments, analogs, and the like. When the term “composition” is used, then, or when a particular composition is specifically identified, it is to be understood that the term includes the composition per se as well as pharmaceutically acceptable, pharmacologically active vector, polynucleotide, salts, esters, amides, proagents, conjugates, active metabolites, isomers, fragments, analogs, etc. In some aspects, the composition disclosed herein comprises the neutralizing HPIV3 antibody of any aspect disclosed herein. The terms “treat,” “treating,” and grammatical variations thereof as used herein, include partially or completely delaying, alleviating, mitigating or reducing the intensity of one or more attendant symptoms of a disorder or condition and / or alleviating, mitigating or impeding one or more causes of a disorder or condition. Treatments according to the disclosure may be applied preventively, prophylactically, palliatively or remedially. Treatments are administered to a subject prior to onset (e.g., before obvious signs of infection), during early onset (e.g., upon initial signs and symptoms of infection), or after an established development of infection. Neutralizing Antibodies An "antibody" is used in the broadest sense, and specifically covers monoclonal antibodies (including full length monoclonal antibodies), polyclonal antibodies, and multispecific antibodies (e.g., bispecific antibodies). Antibodies (Abs) and immunoglobulins (Igs) are glycoproteins having the same structural characteristics. While antibodies exhibit binding specificity to a specific target, immunoglobulins include both antibodies and other antibody-like molecules which lack target specificity. Native antibodies and immunoglobulins are usually heterotetrameric glycoproteins of about 150,000 daltons, composed of two identical light (L) chains and two identical heavy (H) chains. Each heavy chain has at one end a variable domain (VH) followed by a number of constant domains. Each light chain has a variable domain at one end (VL) and a constant domain at its other end. A neutralizing antibody is an antibody comprising peptide sequences that protect cells from pathogens, including but not limited to viruses and bacteria, and other infectious particles by neutralizing their biological effects, thus preventing said pathogen or particles from causing disease. Neutralizing antibodies prevent infections by affecting how surface pathogenic Docket No.10644-185WO1 antigens from entering a subject’s cells. Non-limiting examples of neutralizing antibodies mechanisms of action are blocking the attachment and entry of a virus into a cell, or preventing infection by binding to a viral capsid protein. In some embodiments, the neutralizing antibody prevent infection by preventing pathogens from inducing conformational changes to enter and replicate within a cell. The term "antibody fragment" refers to a portion of a full-length antibody, generally the target binding or variable region. Examples of antibody fragments include Fab, Fab', F(ab')2and Fv fragments. The phrase "functional fragment or analog" of an antibody is a compound having qualitative biological activity in common with a full-length antibody. For example, a functional fragment or analog of an anti-IgE antibody is one which can bind to an IgE immunoglobulin in such a manner so as to prevent or substantially reduce the ability of such molecule from having the ability to bind to the high affinity receptor, FcεRI. As used herein, "functional fragment" with respect to antibodies, refers to Fv, F(ab) and F(ab')2 fragments. An "Fv" fragment is the minimum antibody fragment which contains a complete target recognition and binding site. This region consists of a dimer of one heavy and one light chain variable domain in a tight, non-covalent association (VH-VL dimer). It is in this configuration that the three CDRs of each variable domain interact to define a target binding site on the surface of the VH-VL dimer. Collectively, the six CDRs confer target binding specificity to the antibody. However, even a single variable domain (or half of an Fv comprising only three CDRs specific for a target) has the ability to recognize and bind target, although at a lower affinity than the entire binding site. "Single-chain Fv" or "sFv" antibody fragments comprise the VHand VLdomains of an antibody, wherein these domains are present in a single polypeptide chain. Generally, the Fv polypeptide further comprises a polypeptide linker between the VH and VL domains which enables the sFv to form the desired structure for target binding. The term “monoclonal antibody” as used herein refers to an antibody obtained from a substantially homogeneous population of antibodies, i.e., the individual antibodies within the population are identical except for possible naturally occurring mutations that may be present in a small subset of the antibody molecules. The present disclosure provides neutralizing antibodies targeted against a human parainfluenza virus (HPIV). HPIVs are single-stranded RNA viruses within the Paramyxoviridae family that cause upper and lower respiratory illness in infants, young children, elderly, and immunocompromised individuals. There are four major serotypes of HPIV, including HPIV1, HPIV2, HPIV3, and HPIV4. The HPIVs generally comprise6 structural genes including hemagglutinin-neuraminidase (HN), fusion (F) protein, matrix (M) Docket No.10644-185WO1 protein, nucleoprotein (NP), phosphoprotein (P), and large (L) protein. Herein, the neutralizing proteins target the F protein of a HPIV3 to prevent viral fusion and entry into a cell. The present disclosure provides a human parainfluenza virus 3 (HPIV3) neutralizing antibody and compositions thereof. Herein, the present disclosure aims to characterize a set of HPIV3-specific antibodies identified in multiple individuals for genetic signatures, epitope specificity, neutralization potential, and publicness. Twelve potently neutralizing antibodies targeting three non-overlapping epitopes on HPIV3 F were identified. Among these, six antibodies identified from two different individuals utilized immunoglobulin heavy variable gene IGHV 5-51, with five of the six antibodies targeting the same epitope. However, despite the use of the same heavy chain variable (VH) gene, these antibodies utilized multiple different light chain variable genes (VL) and diverse heavy chain complementarity determining region 3 (CDRH3) sequences. Together, these results provide further information about the genetic and functional characteristics of HPIV3-neutralizing antibodies and show the existence of a reproducible VH-dependent antibody response associated with VLand CDRH3 promiscuity. Understanding sites of HPIV3 F vulnerability, and the genetic and molecular characteristics of antibodies targeting these sites, will help guide efforts for effective vaccine and therapeutic development. In some aspects, disclosed herein is a neutralizing antibody comprising a heavy chain region and a light chain region, wherein the heavy chain region comprises SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, or a variant thereof, and the light chain region comprises SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123, SEQ ID NO: 124, SEQ ID NO: 125, SEQ ID NO: 126, SEQ ID NO: 127, or a variant thereof. In some embodiments, the heavy chain comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, or SEQ ID NO: 37. In some embodiments, the light chain comprises 70%, 71%, 72%, 73%, 74%, 75%, Docket No.10644-185WO1 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123, SEQ ID NO: 124, SEQ ID NO: 125, SEQ ID NO: 126, or SEQ ID NO: 127. In some embodiments, the heavy chain region comprises a variable heavy chain comprising SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, or a variant thereof. In some embodiments, the variable heavy chain comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, or SEQ ID NO: 18. In some embodiments, the light chain region comprises a variable light chain comprising SEQ ID NO: 90, SEQ ID NO: 91, SEQ ID NO: 92, SEQ ID NO: 93, SEQ ID NO: 94, SEQ ID NO: 95, SEQ ID NO: 96, SEQ ID NO: 97, SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101, SEQ ID NO: 102, SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107, or a variant thereof. In some embodiments, the variable light chain comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 90, SEQ ID NO: 91, SEQ ID NO: 92, SEQ ID NO: 93, SEQ ID NO: 94, SEQ ID NO: 95, SEQ ID NO: 96, SEQ ID NO: 97, SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101, SEQ ID NO: 102, SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, or SEQ ID NO: 107. The term "variable" in the context of variable domain of antibodies, refers to the fact that certain portions of the variable domains differ extensively in sequence among antibodies and are used in the binding and specificity of each particular antibody for its particular target. However, the variability is not evenly distributed through the variable domains of antibodies. It is concentrated in three segments called complementarity determining regions (CDRs) also known as hypervariable regions both in the light chain and the heavy chain variable domains. Docket No.10644-185WO1 The more highly conserved portions of variable domains are called the framework (FR). The variable domains of native heavy and light chains each comprise four FR regions, largely an adopting a .beta.-sheet configuration, connected by three CDRs, which form loops connecting, and in some cases forming part of, the .beta.-sheet structure. The CDRs in each chain are held together in close proximity by the FR regions and, with the CDRs from the other chain, contribute to the formation of the target binding site of antibodies (see Kabat et al.) As used herein, numbering of immunoglobulin amino acid residues is done according to the immunoglobulin amino acid residue numbering system of Kabat et al., (Sequences of Proteins of Immunological Interest, National Institute of Health, Bethesda, Md.1987), unless otherwise indicated. In some embodiments, the neutralizing antibody comprises a first, a second, and a third heavy chain complementarity determining region (CDR) CDRH1, CDRH2, and CDRH3; and a light CDRL1, CDRL2, and CDRL3. In some embodiments, the heavy chain CDRH1 comprises SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, or a variant thereof. In some embodiments, the heavy chain CDRH1 comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52, SEQ ID NO: 53, or SEQ ID NO: 54. In some embodiments, the heavy chain CDRH2 comprises SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO:61, SEQ ID NO: 62, SEQ ID NO: 63, SEQ ID NO: 64, SEQ ID NO: 65, SEQ ID NO: 66, SEQ ID NO: 67, SEQ ID NO: 68, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 71, or a variant thereof. In some embodiments, the heavy chain CDRH2 comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO:61, SEQ ID NO: 62, SEQ ID NO: 63, SEQ ID NO: 64, SEQ ID NO: 65, SEQ Docket No.10644-185WO1 ID NO: 66, SEQ ID NO: 67, SEQ ID NO: 68, SEQ ID NO: 69, SEQ ID NO: 70, or SEQ ID NO: 71. In some embodiments, the heavy chain CDRH3 comprises SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, SEQ ID NO: 78, SEQ ID NO: 79, SEQ ID NO: 80, SEQ ID NO: 81, SEQ ID NO: 82, SEQ ID NO: 83, SEQ ID NO: 84, SEQ ID NO: 85, SEQ ID NO: 86, SEQ ID NO: 87, SEQ ID NO: 88, SEQ ID NO: 89, SEQ ID NO: 163, or a variant thereof. In some embodiments, the heavy chain CDRH3 comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, SEQ ID NO: 78, SEQ ID NO: 79, SEQ ID NO: 80, SEQ ID NO: 81, SEQ ID NO: 82, SEQ ID NO: 83, SEQ ID NO: 84, SEQ ID NO: 85, SEQ ID NO: 86, SEQ ID NO: 87, SEQ ID NO: 88, SEQ ID NO: 89, or SEQ ID NO: 163. In some embodiments, the light chain CDRL1 comprises SEQ ID NO: 128, SEQ ID NO: 129, SEQ ID NO: 130, SEQ ID NO: 131, SEQ ID NO: 132, SEQ ID NO: 133, SEQ ID NO: 134, SEQ ID NO: 135, SEQ ID NO: 136, SEQ ID NO: 137, SEQ ID NO: 138, SEQ ID NO: 139, SEQ ID NO: 140, SEQ ID NO: 141, SEQ ID NO: 142, SEQ ID NO: 143, or a variant thereof. In some embodiments, the light chain CDRL1 comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 128, SEQ ID NO: 129, SEQ ID NO: 130, SEQ ID NO: 131, SEQ ID NO: 132, SEQ ID NO: 133, SEQ ID NO: 134, SEQ ID NO: 135, SEQ ID NO: 136, SEQ ID NO: 137, SEQ ID NO: 138, SEQ ID NO: 139, SEQ ID NO: 140, SEQ ID NO: 141, SEQ ID NO: 142, or SEQ ID NO: 143. In some embodiments, the light chain CDRL2 comprises SEQ ID NO: 144, or a variant thereof; or an amino acid sequence selected from DVS, GVD, ANN, EDN, RND, DAS, ATS, KVS, EVS, RNS, MAS, DAS, AAS, or GTS. In some embodiments, the light chain CDRL2 comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 144. In some embodiments, the light chain CDRL3 comprises SEQ ID NO: 145, SEQ ID NO: 146, SEQ ID NO: 147, SEQ ID NO: 148, SEQ ID NO: 149, SEQ ID NO: 150, SEQ ID NO: 151, SEQ ID NO: 152, SEQ ID NO: 153, SEQ ID NO: 154, SEQ ID NO: 155, SEQ ID NO: 156, SEQ ID NO: 157, SEQ ID NO: 158, SEQ ID NO: 159, SEQ ID NO: 160, SEQ ID Docket No.10644-185WO1 NO: 161, SEQ ID NO: 162, SEQ ID NO: 164, SEQ ID NO: 165, or a variant thereof. In some embodiments, the light chain CDRL3 comprises 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 145, SEQ ID NO: 146, SEQ ID NO: 147, SEQ ID NO: 148, SEQ ID NO: 149, SEQ ID NO: 150, SEQ ID NO: 151, SEQ ID NO: 152, SEQ ID NO: 153, SEQ ID NO: 154, SEQ ID NO: 155, SEQ ID NO: 156, SEQ ID NO: 157, SEQ ID NO: 158, SEQ ID NO: 159, SEQ ID NO: 160, SEQ ID NO: 161, SEQ ID NO: 162, SEQ ID NO: 164, or SEQ ID NO: 165. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 38, SEQ ID NO: 55, and SEQ ID NO: 72, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 128, amino acid sequence DVS, and SEQ ID NO: 145, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 38, SEQ ID NO: 55, and SEQ ID NO: 72, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 128 and SEQ ID NO: 145. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 39, SEQ ID NO: 56, and SEQ ID NO:73, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 129, amino acid sequence GVD, and SEQ ID NO: 146, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 39, SEQ ID NO: 56, and SEQ ID NO:73, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 129 and SEQ ID NO: 146. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 40, SEQ ID NO:57, and SEQ ID NO:74, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 130, amino acid sequence ANN, and SEQ ID NO: 147, respectively. In some embodiments, the neutralizing antibody comprises Docket No.10644-185WO1 the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 40, SEQ ID NO:57, and SEQ ID NO:74, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 130 and SEQ ID NO: 147. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 41, SEQ ID NO: 58, and SEQ ID NO:75, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 131, amino acid sequence EDN, and SEQ ID NO: 148, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 41, SEQ ID NO: 58, and SEQ ID NO:75, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 131 and SEQ ID NO: 148. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 42, SEQ ID NO:55, and SEQ ID NO: 76; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 132, amino acid sequence RND, and SEQ ID NO:149, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 42, SEQ ID NO:55, and SEQ ID NO: 76, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 132 and SEQ ID NO: 149. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 43, SEQ ID NO: 59, and SEQ ID NO: 77; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 133, amino acid sequence DAS, and SEQ ID NO: 150, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, Docket No.10644-185WO1 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 43, SEQ ID NO: 59, and SEQ ID NO: 77, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 133 and SEQ ID NO: 150. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 44, SEQ ID NO: 60, and SEQ ID NO: 78, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 134, amino acid sequence ATS, and SEQ ID NO: 151, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 44, SEQ ID NO: 60, and SEQ ID NO: 78, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 134 and SEQ ID NO: 151. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 45, SEQ ID NO: 61, and SEQ ID NO: 79, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 135, amino acid sequence DAS, and SEQ ID NO:152, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 45, SEQ ID NO: 61, and SEQ ID NO: 79, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 135 and SEQ ID NO: 152. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 46, SEQ ID NO: 62, and SEQ ID NO: 80, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 136, amino acid sequence KVS, and SEQ ID NO: 153, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, Docket No.10644-185WO1 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 46, SEQ ID NO: 62, and SEQ ID NO: 80, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 136 and SEQ ID NO: 153. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 47, SEQ ID NO: 63, and SEQ ID NO:81, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 128, amino acid sequence EVS, SEQ ID NO: 154, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 47, SEQ ID NO: 63, and SEQ ID NO:81, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 128 and SEQ ID NO: 154. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 48, SEQ ID NO: 64, and SEQ ID NO: 82, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 137, amino acid sequence RNS, and SEQ ID NO: 155, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 48, SEQ ID NO: 64, and SEQ ID NO: 82, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 137 and SEQ ID NO: 155. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 49, SEQ ID NO: 65, and SEQ ID NO: 83, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 138, amino acid sequence MAS, and SEQ ID NO: 156, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: Docket No.10644-185WO1 49, SEQ ID NO: 65, and SEQ ID NO: 83, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 138 and SEQ ID NO: 156. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 50, SEQ ID NO: 66, and SEQ ID NO: 84, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 139, amino acid sequence MAS, and SEQ ID NO: 157, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 50, SEQ ID NO: 66, and SEQ ID NO: 84, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 139 and SEQ ID NO: 157. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 51, SEQ ID NO: 67, and SEQ ID NO: 85, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 140, amino acid sequence EVS, and SEQ ID NO: 158, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 51, SEQ ID NO: 67, and SEQ ID NO: 85, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 140 and SEQ ID NO: 158. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 52, SEQ ID NO: 68, and SEQ ID NO: 86, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 141, amino acid sequence DAS, and SEQ ID NO: 159, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 52, SEQ ID NO: 68, and SEQ ID NO: 86, respectively; and comprises CDRL1, CDRL2, and Docket No.10644-185WO1 CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 141 and SEQ ID NO: 159. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 53, SEQ ID NO: 69, and SEQ ID NO: 87, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 142, amino acid sequence AAS, and SEQ ID NO: 160, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 53, SEQ ID NO: 69, and SEQ ID NO: 87, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 142 and SEQ ID NO: 160. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 54, SEQ ID NO: 70, and SEQ ID NO: 88, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 143, SEQ ID NO: 144, and SEQ ID NO: 161, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 54, SEQ ID NO: 70, and SEQ ID NO: 88, respectively; and comprises CDRL1, CDRL2, and CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 143, SEQ ID NO: 144, and SEQ ID NO: 161, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 42, SEQ ID NO: 71, and SEQ ID NO: 89, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 134, amino acid sequence GTS, and SEQ ID NO: 162, respectively. In some embodiments, the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 42, SEQ ID NO: 71, and SEQ ID NO: 89, respectively; and comprises CDRL1, CDRL2, and Docket No.10644-185WO1 CDRL3 further comprising 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity to SEQ ID NO: 134 and SEQ ID NO: 162. Methods of treating and / preventing HPIV3 infections The present disclosure also provides methods of preventing, treating, ameliorating, decreasing, and / or eliminating an HPIV3 infection in a subject. In some aspects, disclosed herein is a method of preventing, treating, ameliorating, decreasing, and / or eliminating an HPIV3 infection in a subject, the method comprising administering to the subject a pharmaceutically effective amount of a composition comprising the HPIV3 neutralizing antibody of any preceding aspect, wherein the neutralizing antibody decreases one or more respiratory symptoms in the subject relative to an untreated subject. In some aspects, disclosed herein is a method of preventing, treating, ameliorating, decreasing, and / or eliminating an HPIV3 infection in a subject, the method comprising detecting a B cell using LIBRA-seq, wherein the B cell produces a HPIV3 neutralizing antibody; isolating the HPIV3 neutralizing antibody from the B cell; and administering to the subject a pharmaceutically effective amount of a composition comprising the HPIV3 neutralizing antibody, wherein one or more respiratory symptoms are decreased in the subject relative to an untreated subject. In some embodiments, the HPIV3 neutralizing antibody comprises a heavy chain sequence of any preceding aspect. In some embodiments, the HPIV3 neutralizing antibody comprises a light chain sequence of any preceding aspect. In some embodiments, the heavy chain region comprises a variable heavy chain sequence of any preceding aspect. In some embodiments, the heavy chain region comprises a CDRH1, CDRH2, and CDRH3 of any preceding aspect. In some embodiments, the light chain region comprises a variable light chain sequence of any preceding aspect. In some embodiments, the light chain region comprises a CDRL1, CDRL2, and CDRL3 of any preceding aspect. In some embodiments, the HPIV3 neutralizing antibody targets at least one epitope of the HPIV3 F glycoprotein. In some embodiments, the at least one epitope of the HPIV3 F glycoprotein includes, but is not limited to an Ø antigenic site, an X antigenic site, and any unknown antigenic sites disclosed herein. In some embodiments, the HPIV neutralizing antibody is encoded by an immunoglobulin heavy variable IGHV 5-51 gene. In some embodiments, the HPIV neutralizing antibody is encoded by an immunoglobulin light chain gene comprising IGLV 2- Docket No.10644-185WO1 23, IGLV 2-11, IGLV 1-51, IGLV 1-44, IGLV 2-23, IGLV 1-40, IGKV 1-33, IGKV 3-20, IGKV 1-5, or IGKV 4-69. "Pharmaceutically acceptable" component can refer to a component that is not biologically or otherwise undesirable, i.e., the component may be incorporated into a pharmaceutical formulation of the invention and administered to a subject as described herein without causing significant undesirable biological effects or interacting in a deleterious manner with any of the other components of the formulation in which it is contained. When used in reference to administration to a human, the term generally implies the component has met the required standards of toxicological and manufacturing testing or that it is included on the Inactive Ingredient Guide prepared by the U.S. Food and Drug Administration. As used herein, the term “carrier” encompasses any excipient, diluent, filler, salt, buffer, stabilizer, solubilizer, lipid, stabilizer, or other material well known in the art for use in pharmaceutical formulations. The choice of a carrier for use in a composition will depend upon the intended route of administration for the composition. The preparation of pharmaceutically acceptable carriers and formulations containing these materials is described in, e.g., Remington's Pharmaceutical Sciences, 21st Edition, ed. University of the Sciences in Philadelphia, Lippincott, Williams & Wilkins, Philadelphia, PA, 2005. Examples of physiologically acceptable carriers include saline, glycerol, DMSO, buffers such as phosphate buffers, citrate buffer, and buffers with other organic acids; antioxidants including ascorbic acid; low molecular weight (less than about 10 residues) polypeptides; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, arginine or lysine; monosaccharides, disaccharides, and other carbohydrates including glucose, mannose, or dextrins; chelating agents such as EDTA; sugar alcohols such as mannitol or sorbitol; salt-forming counterions such as sodium; and / or nonionic surfactants such as TWEENTM(ICI, Inc.; Bridgewater, New Jersey), polyethylene glycol (PEG), and PLURONICSTM(BASF; Florham Park, NJ). To provide for the administration of such dosages for the desired therapeutic treatment, compositions disclosed herein can advantageously comprise between about 0.1% and 99% by weight of the total of one or more of the subject compounds based on the weight of the total composition including carrier or diluent. In some embodiments, the composition further comprises a pharmaceutically acceptable carrier selected from an excipient, diluent, buffer, stabilizer, solubilizer, lipid, nanoparticle, or any variant thereof. In some embodiments, the composition is further administered with a pharmaceutical composition selected from an analgesic, an antibody, an Docket No.10644-185WO1 antibiotic (including, but not limited to penicillins (including, but not limited to amoxicillin, clavulanate and amoxicillin, ampicillin, dicloxacillin, oxacillin, and penicillin V potassium), tetracyclins (including, but not limited to demeclocycline, doxycycline, eravacycline, minocycline, omadacycline, sarecycline, and tetracycline), cephalosporins (cefaclor, cefadroxil, cefdinir, cephalexin, cefprozil, cefepime, cefiderocol, cefotaxime, cefotetan, ceftaroline, cefazidme, ceftriaxone, and cefuroxime), quinolones (also referred to as fluoroquinolones include, but are not limited to ciprofloxacin, delafloxacin, levofloxacin, moxifloxacin, and gemifloxacin), lincomycins (including clindamycin and lincomycin), macrolides (including, but not limited to azithromycin, clarithromycin, erythromycin, and fidaxomicin (ketolide)), sulfonamides (including sulfamethoxazole and trimethoprim, and sulfasalazine), glycopeptides (including, but not limited to dalbavancin, oritavancin, telavancin, and vancomycin), aminoglycosides (including, but not limited to gentamicin, tobramycin, and amikacin), carbapenems (including, but not limited to imipenem and cilastatin, meropenem, and ertapenem), and topical antibiotics (including, but not limited to neomycin, bacitracin, polymyxin B, and praxomine) used alone or in combination), a decongestant, a cough suppressant, an anti-inflammatory compound (including, but is not limited to aspirin, ibuprofen, ketoprofen, naproxen, steroids, glucocorticoids (including, but not limited to betamethasone, budesonide, dexamethasone, hydrocortisone, hydrocortisone acetate, methylprednisolone, prednisolone, prednisone, and triamcinolone), methotrexate, sulfasalazine, lefunomide, anti-Tumor Necrosis Factor (TNF) medications, cyclophosphamide, and mycophenolate), or any combinations thereof. In some embodiments, the one or more respiratory symptoms comprise fever, coughing, congested sinuses, respiratory inflammation, wheezing, sneezing, or any combinations thereof. The composition of any preceding aspect may be administered in such amounts, time, and route deemed necessary in order to achieve the desired result. The exact amount of the composition of any preceding aspect will vary from subject to subject, depending on the species, age, and general condition of the subject, the severity of the HPIV3 infection, the particular composition of any preceding aspect, its mode of administration, its mode of activity, and the like. The composition of any preceding aspect is preferably formulated in dosage unit form for ease of administration and uniformity of dosage. It will be understood, however, that the total daily usage of the composition of any preceding aspect will be decided by the attending physician within the scope of sound medical judgment. The specific therapeutically effective dose level for any particular subject will depend upon a variety of factors including the HPIV3 Docket No.10644-185WO1 infection being treated and the severity of the HPIV3 infection; the activity of the composition of any preceding aspect employed; the specific composition of any preceding aspect employed; the age, body weight, general health, sex and diet of the patient; the time of administration, route of administration, and rate of excretion of the specific composition of any preceding aspect employed; the duration of the treatment; drugs used in combination or coincidental with the specific composition of any preceding aspect employed; and like factors well known in the medical arts. The composition of any preceding aspect may be administered by any route. In some embodiments, the composition of any preceding aspect is administered via a variety of routes, including oral, intravenous, intramuscular, intra-arterial, intramedullary, intrathecal, subcutaneous, intraventricular, transdermal, interdermal, rectal, intravaginal, intraperitoneal, topical (as by powders, ointments, creams, and / or drops), mucosal, nasal, buccal, enteral, sublingual; by intratracheal instillation, bronchial instillation, and / or inhalation; and / or as an oral spray, nasal spray, and / or aerosol. In general, the most appropriate route of administration will depend upon a variety of factors including the nature of the composition of any preceding aspect (e.g., its stability in the environment of the gastrointestinal tract), the condition of the subject (e.g., whether the subject is able to tolerate oral administration), etc. The exact amount of the composition of any preceding aspect required to achieve a therapeutically and / or prophylactically effective amount will vary from subject to subject, depending on species, age, and general condition of a subject, severity of the side effects, identity of the particular compound(s), mode of administration, and the like. The amount to be administered to, for example, a child or an adolescent can be determined by a medical practitioner or person skilled in the art and can be lower or the same as that administered to an adult. Methods of generating neutralizing antibodies The present disclosure also provides methods of generating, identifying, isolating, detecting, and / or collecting an HPIV3 neutralizing antibody using a Linking B cell Receptor Sequence to Antigen Specificity through Sequencing (LIBRA-seq). In some aspects, disclosed herein is a method of generating a human parainfluenza virus 3 (HPIV3) neutralizing antibody, the method comprising detecting a B cell using Linking B cell Receptor Sequence to Antigen Specificity through Sequencing (LIBRA-seq), wherein the B cell produces the HPIV3 neutralizing antibody of any preceding aspect, and wherein the HPIV3 neutralizing antibody targets an HPIV3 fusion (HPIV3 F) glycoprotein. Docket No.10644-185WO1 LIBRA-seq (Linking B Cell Receptor to Antigen specificity through sequencing) is developed to simultaneously recover both antigen specificity and paired heavy and light chain BCR sequence. LIBRA-seq is a next-generation sequencing-based readout for BCR-antigen binding interactions that utilizes oligonucleotides (oligos) conjugated to recombinant antigens. Antigen barcodes are recovered during paired-chain BCR sequencing experiments and bioinformatically mapped to single cells. The LIBRA-seq method was applied to PBMC samples from two HIV-infected subjects, and from these, HIV- and influenza-specific antibodies were successfully identified, including both known and novel broadly neutralizing antibody (bNAb) lineages. LIBRA-seq is high-throughput, scalable, and applicable to many targets. This single, integrated assay enables the mapping of monoclonal antibody sequences to panels of diverse antigens theoretically unlimited in number and facilitates the rapid identification of cross-reactive antibodies that serves as therapeutics or vaccine templates. Following a LIBRA-seq experiment, there are 2 resulting pairs of FASTQ files: (1) B cell receptor libraries (containing heavy and light chain contigs), and (2) antigen barcode libraries (containing antigen-identifying DNA barcode sequences from the antigen screening library). In some embodiments, it should be understood that the methods described herein are for uniting the information from these two sequencing libraries. Accordingly, in some embodiments, the above noted step of removing a sequence lacking the cell barcode, the UMI, or the antigen barcode is for removing a sequence from the antigen barcode library lacking the cell barcode, the UMI, or the antigen barcode. The processing serves two purposes: (1) quality control and annotation of sequenced reads, and (2) identification of binding signal from the annotated sequenced reads. Before the following steps are carried out, the BCR libraries are processed in order to determine the list of cell barcodes that have a VDJ sequence. The present disclosure incorporates by reference Georgiev et al (PCT / US20 / 49330) for its teaching of using LIBRA-seq to identify antigen binding specificity of antibodies. The present disclosure also incorporates by reference Georgiev et al (63 / 588,443) for its teaching of using LIBRA-seq systems and methods for simultaneous detection of antigens and ligands. In some embodiments, the method of any preceding aspect further comprises training a machine learning algorithm on sequence features, sequence motifs, or encoded sequence properties (such as via Kidera factors), associated with any particular combination of antigen specificities for subsequent application to sequenced antibodies lacking antigen specificity information due to not using LIBRA-seq or otherwise. In some embodiments, the HPIV3 neutralizing antibody comprises a heavy chain sequence of any preceding aspect. In some embodiments, the HPIV3 neutralizing antibody Docket No.10644-185WO1 comprises a light chain sequence of any preceding aspect. In some embodiments, the heavy chain region comprises a variable heavy chain sequence of any preceding aspect. In some embodiments, the heavy chain region comprises a CDRH1, CDRH2, and CDRH3 of any preceding aspect. In some embodiments, the light chain region comprises a variable light chain sequence of any preceding aspect. In some embodiments, the light chain region comprises a CDRL1, CDRL2, and CDRL3 of any preceding aspect. In some embodiments, the HPIV3 neutralizing antibody targets at least one epitope of the HPIV3 F glycoprotein. In some embodiments, the at least one epitope of the HPIV3 F glycoprotein includes, but is not limited to an Ø antigenic site, an X antigenic site, and any unknown antigenic sites disclosed herein. In some embodiments, the HPIV neutralizing antibody is encoded by an immunoglobulin heavy variable IGHV 5-51 gene. In some embodiments, the HPIV neutralizing antibody is encoded by an immunoglobulin light chain gene comprising IGLV 2- 23, IGLV 2-11, IGLV 1-51, IGLV 1-44, IGLV 2-23, IGLV 1-40, IGKV 1-33, IGKV 3-20, IGKV 1-5, or IGKV 4-69. A number of embodiments of the disclosure have been described. Nevertheless, it will be understood that various modifications may be made without departing from the spirit and scope of the invention. Accordingly, other embodiments are within the scope of the following claims. By way of non-limiting illustration, examples of certain embodiments of the present disclosure are given below. EXAMPLES The following examples are set forth below to illustrate the compositions, devices, methods, and results according to the disclosed subject matter. These examples are not intended to be inclusive of all aspects of the subject matter disclosed herein, but rather to illustrate representative methods and results. These examples are not intended to exclude equivalents and variations of the present invention which are apparent to one skilled in the art. Example 1: Potent HPIV3-neutralizing IGHV5-51 antibodies identified from multiple individuals show light chain and CDRH3 promiscuity. INTRODUCTION Docket No.10644-185WO1 Human parainfluenza virus 3 (HPIV3) is an endemic respiratory pathogen belonging to the Paramyxoviridae viral family. Primary infections occur early in life and can cause severe lower respiratory tract illness, while recurrent infections throughout life are limited to milder disease primarily in the upper respiratory tract. Of the four parainfluenza viruses known to infect humans (HPIVs), HPIV3 is responsible for half of all parainfluenza-induced fever and / or acute respiratory illness (ARI)-associated hospitalizations in the United States in children under 5. Among particularly susceptible adult populations, most notably geriatric and the immune compromised, HPIV3 is a leading cause of serious and lethal respiratory viral illness. To date, there are no approved prophylactic or therapeutic options for HPIV3 infection. Several HPIV3 vaccine candidates that leverage modalities such as mRNA delivery of viral genes or attenuation of live viruses, however, are being evaluated in phase I and II clinical trials. A major target of neutralizing antibodies against HPIV3 is the fusion (F) glycoprotein on the surface of the virion, responsible for facilitating viral entry into epithelial cells of the respiratory tract. HPIV3 F is a class I fusion protein that exists in a metastable prefusion and a stable post fusion state. Stabilization of HPIV3 F in the prefusion conformation has been shown to allow engineering of an F antigen that elicits high neutralizing titers in experimentally inoculated animals, making it an attractive vaccine candidate immunogen. Analysis of antigen- specific B cells directed against HPIV3 F in the prefusion conformation are limited, yet still have enabled definition of the antigenic landscape to some degree. Among the sites with distinct classifications are site Ø at the apex of the prefusion trimer and site X near the equator and apex on the vertices of the prefusion trimer. A more extensive mapping of HPIV3 F is needed to uncover neutralization sensitive sites of vulnerability and understand how these sites affect antibody responses in the general population. Public antibodies, clonotypes sharing highly similar (or in some cases identical) sequences found in more than one individual, have been described in several disease settings and in healthy donors. Although the human antibody gene repertoire exhibits exceptional baseline diversity, the existence of public antibody clonotypes indicates a selective pressure towards convergent evolution of variable genes used by B cells responding to an antigen, likely driven by low affinity interactions mediated by germline-encoded genes. Understanding this phenomenon as it relates to HPIV3 immunity has implications in therapeutic and vaccine development, as the identification of public clonotypes may help identify common immune responses that can be reproducibly elicited in a broad population. The propensity of prefusion HPIV3 F epitopes towards the elicitation of public antibodies, however, remains obscure. Docket No.10644-185WO1 Through analysis of LIBRA-seq (Linking B cell Receptor Sequence to Antigen Specificity through Sequencing) datasets leveraging HPIV3 F as an antigen bait, a set of HPIV3 F-reactive B cells were identified and characterized for genetic signatures, epitope specificity, neutralization potential, and publicness. Analysis revealed several potently neutralizing monoclonal antibodies, primarily targeting the two previously defined major antigenic sites, designated Ø and X, as well as a third, unclassified epitope. Notably, a reproducible variable heavy (VH)-dependent signature was observed for HPIV3-neutralizing antibodies that was observed in multiple individuals, but that was associated with variable light (VL) and CDRH3 promiscuity. Further, although a number of B cells from a database of published antibody sequences utilized the same combination of germline heavy and light chain genes as some of the HPIV3-neutralizing antibodies reported here, the overall frequency of public clonotypes was low when considering conventional public antibody definitions requiring high identity in the CDR3 regions and matching variable genes. Together, these results provide several ultra-potent neutralizing antibody candidates for further pre-clinical validation and show the existence of a reproducible VH-dependent HPIV3-neutralizing antibody response associated with VL and CDRH3 promiscuity. MATERIALS AND METHODS Data mining LIBRA-seq datasets generated from 2020-2023 that included prefusion HPIV3 F in the antigen screening library were mined for B cells displaying a minimum LIBRA-seq score of one for HPIV3 F while also displaying a score below one for a control antigen, in this case, recombinant HIV-1 envelope protein. LIBRA-seq experiments were performed on peripheral blood mononuclear cells (PBMCs) samples obtained from otherwise healthy adult individuals. The established LIBRA-seq pipeline was used for score generation. Antibody expression and purification For each antibody, variable genes were synthesized as cDNA and were inserted into bi- cistronic plasmids encoding for the constant regions of the heavy chain and either the kappa or lambda light chain (Twist BioScience). Antibodies were transiently expressed with Expifectamine transfection reagent (Thermo Fisher Scientific) in Expi293F cells in FreeStyle F17 expression media (Thermo Fisher) (0.1% Pluronic Acid F-68 and 20% 4 mM L- glutamine). Cells were cultured for 5 days at 8% CO2 saturation and 37°C with shaking. Five days post transfection, cells were collected and centrifuged at a minimum of 6000 rpm for Docket No.10644-185WO1 20 minutes. Supernatant was filtered with Nalgene Rapid Flow Disposable Filter Units with PES membrane (0.45 or 0.22 μm) and purified over protein A equilibrated with PBS. Antibodies were eluted with 100 mM glycine HCl at pH 2.7 directly into a 1:10 volume of 1 M Tris-HCl pH 8 and then exchanged into PBS for storage at 4°C. Prefusion HPIV3 F expression and purification Human parainfluenza virus type 3 prefusion stabilized F ectodomain (PDB: 6MJZ) was expressed in Expi293F cells by transient transfection using Expifectamine transfection reagent (Thermo Fisher Scientific) in FreeStyle F17 expression media (Thermo Fisher) (0.1% Pluronic Acid F-68 and 20% 4 mM L-glutamine). Cultures were grown with shaking at 37°C and 8% CO2saturation. Six days post transfection, cultures were centrifuged at 6000 rpm for 20 minutes and then filtered with Nalgene Rapid Flow Disposable Filter Units with PES membrane (0.45 or 0.22 μm). Protein was purified by nickel affinity chromatography using an equilibrated, 1 mL pre-packed HisTrap HP column (GE Healthcare, IL, USA). The column was equilibrated with 15 mL of binding buffer (20 mM sodium phosphate, 0.5 M NaCl, 0.3 M imidazole, pH 7.4), and purified protein was eluted from the column with 15 mL of binding buffer supplemented with 0.5 M imidazole. Concentrated protein was buffer exchanged into PBS and further purified by size exclusion on Superose 6 Increase 10 / 300 GL on the AKTA FPLC system. Fractions containing pure HPIV3 F were identified based on confirmation of molecular mass by sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Antigenicity was confirmed with binding to PIA174. Protein was concentrated and then quantified using UV / vis spectroscopy and frozen at -80°C until use. Enzyme linked immunosorbent assay (ELISA) HPIV3 F was plated at 2 ug / mL overnight at 4°C. The next day, plates were washed three times with PBS supplemented with 0.05% Tween20 (PBS-T) and coated with 1% bovine serum albumin (BSA) in PBS-T. Plates were incubated for one hour at room temperature and then washed three times with PBS-T. Primary antibodies were diluted in 1% BSA in PBS-T, starting at 10 μg / mL with a serial 1:5 dilution, plated, and then incubated at room temperature for one hour before washing three times in PBS-T. The secondary antibody, goat anti-human IgG conjugated to peroxidase, was added at 1:10,000 dilution in 1% BSA in PBS-T to the plates, which were incubated for one hour at room temperature. Plates were washed three times with PBS-T and then developed by adding TMB substrate to each well. The plates were incubated at room temperature for five minutes, and then 1 N sulfuric acid was added to stop Docket No.10644-185WO1 the reaction. Plates were read at 450 nm. ELISAs were performed in technical and biological duplicate. Competitive binding of mAbs with site-specific antibodies in the literature Wells of 384-well microtiter plates were coated with 25ul of 2 μg / mL purified HPIV3 pre-fusion F protein at 4°C overnight. Plates were blocked with 50 μl of 1% BSA in PBS-T for 1 h before washing three times with PBS-T. Primary antibodies at 10 μg / mL were added to wells (20 μL per well) in duplicate and incubated for 1 h at room temperature. A biotinylated preparation of recombinantly produced site-specific monoclonal antibodies (PIA174, PI3-E12, 3X1) were added to wells of each primary antibody at a concentration of 10μg / mL in a volume of 5 μL per well, without washing of unlabeled antibody, and then incubated for 1 h at room temperature. Plates were washed three times with PBS-T and bound antibodies were detected using horseradish peroxidase (HRP) -conjugated anti-biotin 1:1000 (ThermoFischer Scientific) and a TMB substrate. The signal obtained for binding of the biotin-labelled reference antibody in the presence of the unlabeled tested antibody was expressed as a percentage of the binding of the reference antibody alone after subtracting the background signal. Tested mAbs were considered competing if their presence reduced the reference antibody binding to less than 40% of its maximal binding and non-competing if the signal was greater than 71%. A level of 41 to 70% was considered intermediate competition. Cells and virus LLC-MK2 cells were obtained from ATCC (CCL-7) and grown in growth media (Opti- MEM with 2% FBS) at 37ºC, 5% CO2. HPIV3 strain C243 was obtained from IRR (VR-93). HPIV1 strain C35 was obtained from IRR (VR-94). Propagated virus was grown in viral growth media (Opti-MEM with 5 µg / mL trypsin-EDTA and 1% antibiotic-antimycotic) in LLC-MK2 cells at a multiplicity of infection (MOI) of 0.01 for 3-5 days at 37ºC, 5% CO2 until CPE was observed. Virus was harvested using the freeze-thaw method into 25% sucrose solution and stored at -80ºC until use. Plaque reduction neutralization test with HPIV3 and HPIV1 Twenty-four hours prior to viral infection, LLC-MK2 cells were plated in growth media at 5 × 104cells per well in 24 well plates and incubated at 37ºC, 5% CO2. On the day of viral infection, mAbs were serially diluted in Opti-MEM with a starting concentration of 40 µg / mL. Docket No.10644-185WO1 HPIV3 or HPIV1 virus was diluted in Opti-MEM to a final concentration of 2400 plaque forming units (pfu) / mL and added to the mAb mixtures at a 1:1 volume ratio. The mAb / virus mixture incubated for 1 hour at room temperature. Prior to adding the mAb / virus mixture to cells, confluent LLC-MK2 cells in 24 well plates were washed gently three times with PBS. mAb / virus mixture was added to each well (50 µL per well) and the plates rocked at 37ºC, 5% CO2 for 1 hour. Warm overlay (0.75% methylcellulose in Opti-MEM, 5 µg / mL trypsin-EDTA and 1% antibiotic-antimycotic) was added to each well and the plates incubated for 4 days at 37ºC, 5% CO2. Following incubation, the cells were fixed with 10% neutral buffered formalin, washed with water three times, then blocked with milk blocking buffer (2% milk powder, 2% goat serum in PBS-T). Plates were washed three times with water and developed with PIA174 mAb for HPIV3 and 3×1 mAb for HPIV1 diluted to 5 µg / mL in milk blocking solution for 1 hour at room temperature. Plates were washed three times with water before adding the secondary antibody, goat anti-human IgG Fc conjugated to horse radish peroxidase, at a dilution of 1:2000 in milk blocking solution and incubated for 1 hour at room temperature. Plates were washed three times with water and developed with TrueBlue substrate by rocking for 10 minutes. After plaques were visibly stained by the substrate, the plates were washed once with water to stop the developing reaction. Immunostained plaques were counted and graphed on GraphPad Prism9. Real time cell analysis (RTCA) Neutralization assay based on a real time cell analysis (RTCA) impedance assay. The xCelligence RTCA HT Analyzer (formerly ACEA Biosciences, now Agilent ) assesses kinetic changes in cell physiology, including virus-induced cytopathic effect (CPE). Fifty μl of cell culture medium (Opti-MEM supplemented with 2% PenStrep 100X) was added to wells of a 96-well E-plate to obtain background reading. Twenty-two thousand, five hundred (22,5000) Hep-2 cells in 50 μl of cell culture medium were seeded per well, and the plate was placed on the analyzer. Sensograms were visualized using RTCA HT software version2.1.0 (Agilent). A previously determined titer of virus (PIV3 JS) to cause CPE was combined with purified antibodies in a total volume of 120 μl using Opti-MEM supplemented with 2% by volume PenStrep (100X) as a diluent and incubated for 1 h at 37 °C in 5% CO2. At ∼17–20 h after seeding the cells, 100 μl of the virus–mAb mixtures were added to the cells in the 96-well E-plates. Wells containing virus only (in the absence of mAb) and wells containing only Hep- 2 cells in medium were included as controls. Plates were measured every 15 m for 74 h to Docket No.10644-185WO1 assess virus neutralization. Antibodies were assessed in 3-fold dilutions, starting at 20 μg / ml. mAbs were tested in technical and biological duplicate. Neutralization was calculated as the percent of maximal cell index in control wells without virus minus cell index in control (virus- only) wells that exhibited maximal CPE at 40–48 h after applying virus–antibody mixture to the cells. Public antibody analysis HPIV3 antibodies identified in this paper were compared against previously published healthy adult B cell repertoires consisting of 1,689,608 paired antibody sequences (data from Jaffe et al.(22)). In comparing pairs of B cells, V gene paralogues were treated as the same and CDR3 identity was calculated employing the Levenshtein distance metric, measuring the difference between amino acid sequences and dividing it by the length of the longer CDR3 region in the pair to get percent identity. Scatter plots in Figure 3B depict these pairs of B cells, characterized by their percentage identities in the complementarity determining region 3 (CDR3) of the heavy chain (represented on the x-axis) and the light chain (CDRL3) (on the y- axis). The color coding of each dot in the plots corresponds to the usage of variable (V) genes: blue dots indicate identical use of both heavy chain (VH) and light chain (VL) genes, orange signifies matching VH gene use, purple represents matching VL gene use, and gray denotes cases where neither VH nor VL genes match, but there is at least 50% sequence identity in either the CDRH3 or CDRL3 regions. RESULTS Identification and characterization of HPIV3 F-specific monoclonal antibodies by LIBRA-seq LIBRA-seq datasets generated between 2020-2023 that included prefusion stabilized HPIV3 F in the LIBRA-seq antigen screening library were mined to identify B cells with high signal for binding to HPIV3 F and low signal for binding to control antigens. For all experiments, peripheral blood mononuclear cells from otherwise healthy adult individuals were used as the input for flow cytometric cell sorting. These adult participants were not pre- screened for seropositivity to HPIV3, as HPIV3 infection universally occurs in childhood. B cells were sorted based on expression of several phenotypic markers: CD14-, CD3-, CD19+, immunoglobulin G (IgG)+, antigen+. Following computational filtering, a total of 19 IgG+ B cells with a robust LIBRA-seq signal, a measure of antigen binding, for HPIV3 F for recombinant expression as IgG1 monoclonal antibodies were identified. The HPIV3 F Docket No.10644-185WO1 reactivity was confirmed via enzyme-linked immunosorbent assay (ELISA) for 18 / 19 antibodies (Figure 1A). Epitope mapping on HPIV3 F prefusion trimer and virus neutralization To interrogate the antigenic binding sites targeted by the sixteen mAbs that reached saturation of binding in the ELISA, competition analysis were performed with previously published recombinant HPIV3 F-specific antibodies. Ten of the sixteen mAbs were determined to likely target site Ø at the apex of the pre-fusion trimer, as evidenced by intermediate (≤ 40% binding) to strong (0%-40% binding) competition with at least one of the two published neutralizing antibodies, PIA174 or PI3-E12, with eight of these ten mAbs competing with both (Figure 1B). Separately, three mAbs strongly competed for binding with 3x1 only, an HPIV3 / HPIV1 cross-neutralizing antibody that binds at site X. Finally, mAbs 75163-6, 3-4, and 3-8 did not compete / weakly competed for binding with site Ø and site X binding mAbs (Figure 1B). Additionally, when tested against each other, mAbs 75163-6, 3-4, and 3-8 did not compete for binding, showing that these antibodies target different sites on HPIV3 F (Figure 5). Taken together, these results support the finding that both antigenic sites Ø and X are common targets of HPIV3 F-specific antibodies. Next, the ability of the twelve mAbs that strongly competed with PIA174, PI3-E12, and / or 3x1 to neutralize HPIV3 was examined. Neutralization potency was determined by plaque reduction neutralization test (PRNT) using live virus to inoculate cells. All twelve mAbs neutralized the virus, with potencies that ranged from 0.002 μg / mL to 1.63 μg / mL. Notably, eight mAbs neutralized virus more potently than PIA174, with four antibodies having an ultra- high potency of better than 10 ng / ml and antibody 3-11 being the most potent at 2 ng / ml (Figure 2 and Table 1). Despite several antibodies competing with the HPIV3 / HPIV1 cross- neutralizing antibody 3x1 at site X, none could neutralize the related HPIV1 virus (Figure 5A). While mAb 75163-6 did not compete for binding with site Ø or site X binding mAbs, when tested for neutralization using a real-time cell analysis (RTCA) neutralizing antibody assay based on impedance and microsensor electrodes, mAb 75163-6 neutralized virus with a half- maximal inhibitory concentration (IC50) value of 0.062 μg / mL (Table I and Figure 5B), showing that this antibody may target a different site of virus vulnerability. Interestingly, six out of twelve neutralizing antibodies, across two separate donors, leveraged immunoglobulin heavy chain variable gene IGHV5-51. While five of these antibodies targeted the epitope defined by site Ø, they were paired with diverse (three) immunoglobulin light chain variable genes (Table 1). Further, the CDRH3 sequences for these Docket No.10644-185WO1 five antibodies were also diverse, with lengths ranging from ten to twelve amino acids and sequence identities reaching as low as 30% (Figure 6). These results show that IGHV 5-51 provides a common mechanism for recognition of antigenic site Ø, despite promiscuity in light chain pairing and CDRH3 sequence identity (Table 1). Public antibody sequence analysis In an effort to understand the propensity of HPIV3 F neutralizing epitopes towards elicitation of population-level antibody responses, the complementarity determining region 3 (CDR3) sequence identities of the twelve neutralizing antibodies were analyzed against previously published antibody gene repertoires from healthy individuals. Interestingly, the site X mAb 6400-5 had the highest number of B cell matches that exhibited ≥ 50% CDRH3 and ≥ 50% CDRL3 sequence identity while leveraging identical VH and VL gene usage (Figure 3A and 3B). Expectedly, CDRL3 identity was highest in pairs of B cells encoded by the same VL gene, with several B cells displaying 100% CDRL3 identity for site Ø or site X mAbs. Unlike CDRL3, B cell gene matches with high percent identity (≥ 70%) in the CDRH3 region were exceedingly rare (Figure 3A and Table 2). As mAb 75163-6 did not strongly compete with any site-specific antibodies tested here, for the purpose of this analysis, mAb 75163-6 were categorized into a separate bin (termed “A”), to represent recognition of an uncharacterized epitope. While several hundred B cells expressing antibody genes with ≥ 50% CDRL3 identity to mAb 75163-6 were identified, CDRH3 identity was markedly lower in the antibody genes encoded by identical VHand VLgenes (Figure 3A), showing antibodies to this site may either be rare in nature or may exhibit high plasticity in the CDRH3 region. DISCUSSION Neutralizing antibodies are immensely useful tools against viral infections, as evidenced by recent clinical applications of therapeutic and prophylactic monoclonal antibodies against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the etiological agent of coronavirus disease 2019 (COVID-19), and respiratory syncytial virus (RSV). Understanding population-level neutralizing antibody responses is of particular interest as such responses may identify the most common epitopes to elicit antibodies following infection and could be promising to target in reverse vaccinology approaches. In the present disclosure, the existing LIBRA-seq datasets that included HPIV3 as an antigen bait for B cells with promising signal for binding against the prefusion-stabilized HPIV3 F antigen was mined. HPIV3 F binding was experimentally confirmed for 18 out of 19 tested mAbs, with 16 reaching Docket No.10644-185WO1 saturating levels of binding to recombinant F protein in ELISA. As others have shown, site Ø is commonly targeted by prefusion F-binding cells, with only four of the antibodies reported here competing for binding with the recently described antigenic site X. Three antibodies from the analysis presented herein did not compete / weakly competed for binding with PIA174, PI3- E12, and 3x1, showing that the antigenic landscape of HPIV3 F has yet to be characterized to its full extent. Interestingly, six neutralizing antibodies encoded by IGHV 5-51 were found to target site Ø, showing a selective pressure towards the use of this gene in the formation of critical antigenic contacts necessary for recognition of site Ø, despite promiscuity in light chain pairing and CDRH3 sequence. In immunocompetent adults, HPIV3 causes self-limiting disease, but it is a frequent driver of morbidity and mortality in at-risk groups. Passive administration of neutralizing antibodies has become an attractive option for populations not well suited towards immunization, such as infants incapable of mounting robust humoral responses and immunocompromised individuals, particularly hematopoietic stem cell transplant patients, for whom HPIV3 respiratory illness is associated with near 40% mortality. Herein, thirteen antibodies were identified that potently neutralize HPIV3 virus, with IC50 values ranging from 0.002 μg / mL to 1.18 μg / mL. It will be apparent to those skilled in the art that various modifications and variations can be made in the present disclosure without departing from the scope or spirit of the invention. Other embodiments of the disclosure will be apparent to those skilled in the art from consideration of the specification and practice of the methods disclosed herein. It is intended that the specification and examples be considered as exemplary only, with a true scope and spirit of the invention being indicated by the following claims.

[0002] Docket No.10644-185WO1 TABLES Docket No.10644-185WO1 . Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1

[0003] Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1 Docket No.10644-185WO1

[0004] Docket No.10644-185WO1 Docket No.10644-185WO1 SEQUENCES SEQ ID NO: 19 – Constant Heavy Chain ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAP ELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAK TKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPR EPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSD GSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK SEQ ID NO: 108 – Constant Light Chain GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTT PSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS SEQ ID NO: 109 – Constant Light Chain RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVT EQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Claims

Docket No.10644-185WO1 CLAIMS What is claimed is:

1. A neutralizing antibody comprising a heavy chain region and a light chain region, wherein the heavy chain region comprises SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25, SEQ ID NO: 26, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, or a variant thereof, and the light chain region comprises SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO: 114, SEQ ID NO: 115, SEQ ID NO: 116, SEQ ID NO: 117, SEQ ID NO: 118, SEQ ID NO: 119, SEQ ID NO: 119, SEQ ID NO: 120, SEQ ID NO: 121, SEQ ID NO: 122, SEQ ID NO: 123, SEQ ID NO: 124, SEQ ID NO: 125, SEQ ID NO: 126, SEQ ID NO: 127, or a variant thereof.

2. The neutralizing antibody of claim 1, wherein the heavy chain region comprises a variable heavy chain comprising SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, or a variant thereof.

3. The neutralizing antibody of claim 1, wherein the light chain region comprises a variable light chain comprising SEQ ID NO: 90, SEQ ID NO: 91, SEQ ID NO: 92, SEQ ID NO: 93, SEQ ID NO: 94, SEQ ID NO: 95, SEQ ID NO: 96, SEQ ID NO: 97, SEQ ID NO: 98, SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101, SEQ ID NO: 102, SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107, or a variant thereof.

4. The neutralizing antibody of any one of claims 1-3, wherein the neutralizing antibody comprises a first, a second, and a third heavy chain complementarity determining region (CDR) CDRH1, CDRH2, and CDRH3 selected from the group consisting of SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 42, SEQ ID NO: 43, SEQ ID NO: 44, SEQ ID NO: 45, SEQ ID NO: 46, SEQ ID NO: 47, SEQ ID NO: 48, SEQ ID NO: 49, SEQ ID NO: 50, SEQ ID NO: 51, SEQ ID NO: 52, SEQ ID NO: 53, SEQ ID NO: 54, SEQ ID NO: 55, SEQ ID NO: 56, SEQ ID NO: 57, SEQ ID NO: 58, SEQ ID NO: 59, SEQ ID NO: 60, SEQ ID NO: 61, SEQ ID NO:62, SEQ ID NO: 63, SEQ ID NO: 64, SEQ ID NO: 65, SEQ ID NO: 66,Docket No.10644-185WO1 SEQ ID NO: 67, SEQ ID NO:68, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 71, SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, SEQ ID NO: 78, SEQ ID NO: 79, SEQ ID NO: 80, SEQ ID NO: 81, SEQ ID NO: 82, SEQ ID NO: 83, SEQ ID NO: 84, SEQ ID NO:85, SEQ ID NO: 86, SEQ ID NO: 87, SEQ ID NO: 88, SEQ ID NO: 89, and SEQ ID NO: 163; and a first, a second, and a third light chain complementarity determining regions CDRL1, CDRL2, and CDRL3 selected from the group consisting of SEQ ID NO:128, SEQ ID NO: 129, SEQ ID NO: 130, SEQ ID NO:131, SEQ ID NO:132, SEQ ID NO: 133, SEQ ID NO: 134, SEQ ID NO: 135, SEQ ID NO:136, SEQ ID NO: 137, SEQ ID NO: 138, SEQ ID NO: 139, SEQ ID NO: 140, SEQ ID NO:141, SEQ ID NO:142, SEQ ID NO:143, SEQ ID NO: 144, SEQ ID NO: 145, SEQ ID NO: 146, SEQ ID NO: 147, SEQ ID NO: 148, SEQ ID NO: 149, SEQ ID NO: 150, SEQ ID NO: 151, SEQ ID NO: 152, SEQ ID NO: 153, SEQ ID NO: 154, SEQ ID NO: 155, SEQ ID NO: 156, SEQ ID NO: 157, SEQ ID NO: 158, SEQ ID NO: 159, SEQ ID NO:160, SEQ ID NO: 161, SEQ ID NO: 162, SEQ ID NO:164, SEQ ID NO: 165 and amino acid sequences selected from DVS, GVD, ANN, EDN, RND, DAS, ATS, KVS, EVS, RNS, MAS, AAS, and GTS.

5. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 38, SEQ ID NO: 55, and SEQ ID NO: 72, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 128, amino acid sequence DVS, and SEQ ID NO: 145, respectively.

6. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 39, SEQ ID NO: 56, and SEQ ID NO:73, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 129, amino acid sequence GVD, and SEQ ID NO: 146, respectively.

7. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 40, SEQ ID NO:57, and SEQ ID NO:74, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 130, amino acid sequence ANN, and SEQ ID NO: 147, respectively.

8. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 41, SEQ ID NO: 58,Docket No.10644-185WO1 and SEQ ID NO:75, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 131, amino acid sequence EDN, and SEQ ID NO: 148, respectively.

9. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 42, SEQ ID NO:55, and SEQ ID NO: 76; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 132, amino acid sequence RND, and SEQ ID NO:149, respectively.

10. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 43, SEQ ID NO: 59, and SEQ ID NO: 77; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 133, amino acid sequence DAS, and SEQ ID NO: 150, respectively.

11. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 44, SEQ ID NO: 60, and SEQ ID NO: 78, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 134, amino acid sequence ATS, and SEQ ID NO: 151, respectively.

12. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 45, SEQ ID NO: 61, and SEQ ID NO: 79, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 135, amino acid sequence DAS, and SEQ ID NO:152, respectively.

13. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 46, SEQ ID NO: 62, and SEQ ID NO: 80, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 136, amino acid sequence KVS, and SEQ ID NO: 153, respectively.

14. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 47, SEQ ID NO: 63, and SEQ ID NO:81, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 128, amino acid sequence EVS, SEQ ID NO: 154, respectively.Docket No.10644-185WO1 15. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 48, SEQ ID NO: 64, and SEQ ID NO: 82, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 137, amino acid sequence RNS, and SEQ ID NO: 155, respectively.

16. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 49, SEQ ID NO: 65, and SEQ ID NO: 83, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 138, amino acid sequence MAS, and SEQ ID NO: 156, respectively.

17. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 50, SEQ ID NO: 66, and SEQ ID NO: 84, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 139, amino acid sequence MAS, and SEQ ID NO: 157, respectively.

18. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 51, SEQ ID NO: 67, and SEQ ID NO: 85, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 140, amino acid sequence EVS, and SEQ ID NO: 158, respectively.

19. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 52, SEQ ID NO: 68, and SEQ ID NO: 86, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 141, amino acid sequence DAS, and SEQ ID NO: 159, respectively.

20. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 53, SEQ ID NO: 69, and SEQ ID NO: 87, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 142, amino acid sequence AAS, and SEQ ID NO: 160, respectively.

21. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 54, SEQ ID NO: 70, and SEQ ID NO: 88, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 143, SEQ ID NO: 144, and SEQ ID NO: 161, respectively.Docket No.10644-185WO1 22. The neutralizing antibody of any one of claims 1-4, wherein the neutralizing antibody comprises the CDRH1, CDRH2, and CDRH3 as set forth in SEQ ID NO: 42, SEQ ID NO: 71, and SEQ ID NO: 89, respectively; and the CDRL1, CDRL2, and CDRL3 as set forth in SEQ ID NO: 134, amino acid sequence GTS, and SEQ ID NO: 162, respectively.

23. A method of treating or preventing a human parainfluenza virus 3 (HPIV3) infection in a subject in need thereof, the method comprising administering to the subject a pharmaceutically effective amount of a composition comprising the HPIV3 neutralizing antibody of any one of claims 1-22.

24. The method of claim 23, wherein the HPIV3 neutralizing antibody targets an HPIV3 fusion (HPIV3 F) glycoprotein.

25. The method of claim 23 or 24, wherein the HPIV3 neutralizing antibody targets at least one epitope of the HPIV3 F glycoprotein.

26. The method of claim 25, wherein the at least one epitope of the HPIV3 F glycoprotein comprises an Ø antigenic site.

27. The method of claim 25, wherein the at least one epitope of the HPIV3 F glycoprotein comprises an X antigenic site.

28. The method of any one of claims 23-27, wherein the HPIV neutralizing antibody is encoded by an immunoglobulin heavy variable IGHV 5-51 gene.

29. The method of any one of claims 23-28, wherein the HPIV neutralizing antibody is encoded by an immunoglobulin light chain gene comprising IGLV 2-23, IGLV 2-11, IGLV 1- 51, IGLV 1-44, IGLV 2-23, IGLV 1-40, IGKV 1-33, IGKV 3-20, IGKV 1-5, or IGKV 4-69.

30. The method of any one of claims 23-29, wherein the composition further comprises a pharmaceutically acceptable carrier selected from an excipient, diluent, buffer, stabilizer, solubilizer, lipid, nanoparticle, or any variant thereof.Docket No.10644-185WO1 31. The method of any one of claims 23-30, wherein the composition is further administered with a pharmaceutical composition selected from an analgesic, an antibody, an antibiotic, a decongestant, a cough suppressant, or any combinations thereof.

32. The method of any one of claims 23-31, wherein the neutralizing antibody decreases one or more respiratory symptoms in the subject relative to an untreated subject.

33. The method of claim 32, wherein the one or more respiratory symptoms comprise fever, coughing, congested sinuses, respiratory inflammation, wheezing, sneezing, or any combinations thereof.

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