3IYW
West Nile virus in complex with Fab fragments of MAb CR4354 (fitted coordinates of envelope proteins and Fab fragments of one icosahedral ASU)
Summary for 3IYW
| Entry DOI | 10.2210/pdb3iyw/pdb |
| Related | 2HG0 3N9G |
| EMDB information | 5190 |
| Descriptor | Envelope glycoprotein, CR4354 Fab fragment X1, heavy chain H, CR4354 Fab fragment X1, light chain L, ... (4 entities in total) |
| Functional Keywords | virus-antibody complex, neutralizing fab fragment, flavivirus, west nile virus, envelope protein, icosahedral virus, virus |
| Biological source | West Nile virus More |
| Total number of polymer chains | 7 |
| Total formula weight | 226835.64 |
| Authors | Rossmann, M.G.,Kaufmann, B. (deposition date: 2010-06-18, release date: 2010-11-24, Last modification date: 2024-11-20) |
| Primary citation | Kaufmann, B.,Vogt, M.R.,Goudsmit, J.,Holdaway, H.A.,Aksyuk, A.A.,Chipman, P.R.,Kuhn, R.J.,Diamond, M.S.,Rossmann, M.G. Neutralization of West Nile virus by cross-linking of its surface proteins with Fab fragments of the human monoclonal antibody CR4354. Proc.Natl.Acad.Sci.USA, 107:18950-18955, 2010 Cited by PubMed Abstract: Many flaviviruses are significant human pathogens, with the humoral immune response playing an essential role in restricting infection and disease. CR4354, a human monoclonal antibody isolated from a patient, neutralizes West Nile virus (WNV) infection at a postattachment stage in the viral life-cycle. Here, we determined the structure of WNV complexed with Fab fragments of CR4354 using cryoelectron microscopy. The outer glycoprotein shell of a mature WNV particle is formed by 30 rafts of three homodimers of the viral surface protein E. CR4354 binds to a discontinuous epitope formed by protein segments from two neighboring E molecules, but does not cause any detectable structural disturbance on the viral surface. The epitope occurs at two independent positions within an icosahedral asymmetric unit, resulting in 120 binding sites on the viral surface. The cross-linking of the six E monomers within one raft by four CR4354 Fab fragments suggests that the antibody neutralizes WNV by blocking the pH-induced rearrangement of the E protein required for virus fusion with the endosomal membrane. PubMed: 20956322DOI: 10.1073/pnas.1011036107 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (13.7 Å) |
Structure validation
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