6W52
Prefusion RSV F bound by neutralizing antibody RSB1
Summary for 6W52
| Entry DOI | 10.2210/pdb6w52/pdb |
| Descriptor | Fusion glycoprotein F0, Fusion glycoprotein F1 fused with Fibritin trimerization domain, RSB1 Fab Heavy Chain, ... (4 entities in total) |
| Functional Keywords | rsv, antibody, neutralization, prefusion, vaccine, viral protein |
| Biological source | Human respiratory syncytial virus A (strain A2) More |
| Total number of polymer chains | 4 |
| Total formula weight | 109939.02 |
| Authors | Harshbarger, W.,Chandramouli, S.,Malito, M. (deposition date: 2020-03-12, release date: 2020-11-11, Last modification date: 2024-11-06) |
| Primary citation | Harshbarger, W.,Tian, S.,Wahome, N.,Balsaraf, A.,Bhattacharya, D.,Jiang, D.,Pandey, R.,Tungare, K.,Friedrich, K.,Mehzabeen, N.,Biancucci, M.,Chinchilla-Olszar, D.,Mallett, C.P.,Huang, Y.,Wang, Z.,Bottomley, M.J.,Malito, E.,Chandramouli, S. Convergent structural features of respiratory syncytial virus neutralizing antibodies and plasticity of the site V epitope on prefusion F. Plos Pathog., 16:e1008943-e1008943, 2020 Cited by PubMed Abstract: Respiratory syncytial virus (RSV) is a global public health burden for which no licensed vaccine exists. To aid vaccine development via increased understanding of the protective antibody response to RSV prefusion glycoprotein F (PreF), we performed structural and functional studies using the human neutralizing antibody (nAb) RSB1. The crystal structure of PreF complexed with RSB1 reveals a conformational, pre-fusion specific site V epitope with a unique cross-protomer binding mechanism. We identify shared structural features between nAbs RSB1 and CR9501, elucidating for the first time how diverse germlines obtained from different subjects can develop convergent molecular mechanisms for recognition of the same PreF site of vulnerability. Importantly, RSB1-like nAbs were induced upon immunization with PreF in naturally-primed cattle. Together, this work reveals new details underlying the immunogenicity of site V and further supports PreF-based vaccine development efforts. PubMed: 33137810DOI: 10.1371/journal.ppat.1008943 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.74 Å) |
Structure validation
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