9HVW
Respiratory Syncytial Virus Fusion protein in the postfusion conformation in complex with monoclonal antibody 131-2a Fab
This is a non-PDB format compatible entry.
Summary for 9HVW
| Entry DOI | 10.2210/pdb9hvw/pdb |
| EMDB information | 52444 |
| Descriptor | Fusion glycoprotein F0, Fusion glycoprotein F1,Probable N-acetylmuramidase, 131-2a heavy chain, ... (4 entities in total) |
| Functional Keywords | antigenic site i, viral protein |
| Biological source | human respiratory syncytial virus More |
| Total number of polymer chains | 8 |
| Total formula weight | 219086.15 |
| Authors | Snijder, J. (deposition date: 2025-01-02, release date: 2025-02-26, Last modification date: 2025-08-20) |
| Primary citation | Peng, W.,Siborova, M.,Wu, X.,Du, W.,Schulte, D.,Pronker, M.F.,de Haan, C.A.M.,Snijder, J. Structural Basis for Postfusion-Specific Binding to the Respiratory Syncytial Virus F Protein by the Canonical Antigenic Site I Antibody 131-2a. Acs Infect Dis., 11:2357-2366, 2025 Cited by PubMed 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 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. PubMed: 40693554DOI: 10.1021/acsinfecdis.5c00368 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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