ArticleACS infectious diseases2025
Structural Basis for Postfusion-Specific Binding to the Respiratory Syncytial Virus F Protein by the Canonical Antigenic Site I Antibody 131-2a.
Article in ACS infectious diseases, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- Structural vaccinology expedites rational design of next-generation vaccines for influenza and respiratory syncytial virus.Virologica Sinica · 2026Review
- Rational design 2.0: transitioning from static structural biology to computational prioritization and iterative vaccine optimization for RSV.Frontiers in immunology · 2026Review
- Molecular Surveillance RevealsVaccines · 2025Article
- Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The respiratory syncytial virus (RSV) fusion (F) protein is a major target of antiviral antibodies following natural infection or vaccination and is responsible for mediating fusion between the viral envelope and the host membrane. The fusion process is driven by a large-scale conformational change in F, switching irreversibly from the metastable prefusion state to the stable postfusion conformation. Previous research has identified six distinct antigenic sites in RSV-F, termed sites Ø, I, II, III, IV, and V. Of these, only antigenic site I is fully specific to the postfusion conformation of F. A monoclonal antibody 131-2a that specifically targets postfusion F has been widely used as a research tool to probe for postfusion F and to define antigenic site I in serological studies, yet its sequence and precise epitope have remained unknown. Here, we use mass spectrometry-based
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