ArticlePLoS pathogens2018
Human antibody recognition of antigenic site IV on Pneumovirus fusion proteins.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 48 citations in OpenAlex.
- Stabilization of prefusion hMPV F improves manufacturability and protective immunity across hMPV lineages.Virologica Sinica · 2026Article
- Phylodynamics and molecular epidemiology of the respiratory syncytial virus fusion protein in China.Microbiology spectrum · 2026Article
- A potently neutralizing and protective human antibody targeting antigenic site V on RSV and hMPV fusion glycoprotein.Cell reports. Medicine · 2026Article
- Structural basis for childhood antibody recognition of the human metapneumovirus fusion protein.Nature communications · 2025Article
- Structural Basis for Childhood Antibody Recognition of The Human Metapneumovirus Fusion Protein.bioRxiv : the preprint server for biology · 2025Article
- Vaccine Development for Human Pneumoviruses.Vaccines · 2025Review
- Article
- A potent broad-spectrum neutralizing antibody targeting a conserved region of the prefusion RSV F protein.Nature communications · 2024Article
- A potently neutralizing and protective human antibody targeting antigenic site V on RSV and hMPV fusion glycoprotein.bioRxiv : the preprint server for biology · 2024Article
- Structural characterization of M8C10, a neutralizing antibody targeting a highly conserved prefusion-specific epitope on the metapneumovirus fusion trimerization interface.Journal of virology · 2023Article
- Structural basis for respiratory syncytial virus and human metapneumovirus neutralization.Current opinion in virology · 2023Review
- Potently neutralizing human mAbs against the zoonotic pararubulavirus Sosuga virus.JCI insight · 2023Article
- Cross-protective antibodies against common endemic respiratory viruses.Nature communications · 2023Article
- Structural basis for ultrapotent antibody-mediated neutralization of human metapneumovirus.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Profiling of hMPV F-specific antibodies isolated from human memory B cells.Nature communications · 2022Article
- A Pan-Pneumovirus vaccine based on immunodominant epitopes of the fusion protein.Frontiers in immunology · 2022Article
- Antivirals targeting paramyxovirus membrane fusion.Current opinion in virology · 2021Review
- Structure, Immunogenicity, and Conformation-Dependent Receptor Binding of the Postfusion Human Metapneumovirus F Protein.Journal of virology · 2021Article
- Potent Human Single-Domain Antibodies Specific for a Novel Prefusion Epitope of Respiratory Syncytial Virus F Glycoprotein.Journal of virology · 2021Article
- Passive Immunoprophylaxis against Respiratory Syncytial Virus in Children: Where Are We Now?International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Respiratory syncytial virus (RSV) is a major human pathogen that infects the majority of children by two years of age. The RSV fusion (F) protein is a primary target of human antibodies, and it has several antigenic regions capable of inducing neutralizing antibodies. Antigenic site IV is preserved in both the pre-fusion and post-fusion conformations of RSV F. Antibodies to antigenic site IV have been described that bind and neutralize both RSV and human metapneumovirus (hMPV). To explore the diversity of binding modes at antigenic site IV, we generated a panel of four new human monoclonal antibodies (mAbs) and competition-binding suggested the mAbs bind at antigenic site IV. Mutagenesis experiments revealed that binding and neutralization of two mAbs (3M3 and 6F18) depended on arginine (R) residue R429. We discovered two R429-independent mAbs (17E10 and 2N6) at this site that neutralized an RSV R429A mutant strain, and one of these mAbs (17E10) neutralized both RSV and hMPV. To determine the mechanism of cross-reactivity, we performed competition-binding, recombinant protein mutagenesis, peptide binding, and electron microscopy experiments. It was determined that the human cross-reactive mAb 17E10 binds to RSV F with a binding pose similar to 101F, which may be indicative of cross-reactivity with hMPV F. The data presented provide new concepts in RSV immune recognition and vaccine design, as we describe the novel idea that binding pose may influence mAb cross-reactivity between RSV and hMPV. Characterization of the site IV epitope bound by human antibodies may inform the design of a pan-Pneumovirus vaccine.
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Registered trials
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