The monoclonal antibody 131-2a specifically binds to the postfusion conformation of the RSV F protein at a composite epitope that is sterically blocked in the prefusion state.
The study defines the precise sequence and structural epitope of the canonical RSV-F antigenic site I antibody 131-2a, explaining its specificity for the postfusion conformation.
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 de novo sequencing of 131–2a to reverse engineer a recombinant product and study the epitope to define antigenic site I with molecular detail, revealing the structural basis for the antibody’s specificity toward postfusion RSV-F.
Peng et al. (Tue,) conducted a other in Respiratory Syncytial Virus (RSV). Monoclonal antibody 131-2a was evaluated on Epitope mapping and structural basis of postfusion specificity. The monoclonal antibody 131-2a specifically binds to the postfusion conformation of the RSV F protein at a composite epitope that is sterically blocked in the prefusion state.
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