4RS5
Crystal structure of an uncoating intermediate of a EV71 recombinant virus
Summary for 4RS5
| Entry DOI | 10.2210/pdb4rs5/pdb |
| Related | 4N43 4N53 4RQP 4RR3 |
| Descriptor | Capsid protein VP3, Capsid protein VP0, Capsid protein VP1 (3 entities in total) |
| Functional Keywords | eight-stranded beta barrel, replicate in cytoplasm, virus |
| Biological source | Enterovirus A71 More |
| Cellular location | Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : F6KTB0 F6KTB0 F6KTB0 |
| Total number of polymer chains | 15 |
| Total formula weight | 480095.60 |
| Authors | |
| Primary citation | Lyu, K.,Wang, G.C.,He, Y.L.,Han, J.F.,Ye, Q.,Qin, C.F.,Chen, R. Crystal structures of enterovirus 71 (EV71) recombinant virus particles provide insights into vaccine design. J.Biol.Chem., 290:3198-3208, 2015 Cited by PubMed Abstract: Hand-foot-and-mouth disease (HFMD) remains a major health concern in the Asia-Pacific regions, and its major causative agents include human enterovirus 71 (EV71) and coxsackievirus A16. A desirable vaccine against HFMD would be multivalent and able to elicit protective responses against multiple HFMD causative agents. Previously, we have demonstrated that a thermostable recombinant EV71 vaccine candidate can be produced by the insertion of a foreign peptide into the BC loop of VP1 without affecting viral replication. Here we present crystal structures of two different naturally occurring empty particles, one from a clinical C4 strain EV71 and the other from its recombinant virus containing an insertion in the VP1 BC loop. Crystal structure analysis demonstrated that the inserted foreign peptide is well exposed on the particle surface without significant structural changes in the capsid. Importantly, such insertions do not seem to affect the virus uncoating process as illustrated by the conformational similarity between an uncoating intermediate of another recombinant virus and that of EV71. Especially, at least 18 residues from the N terminus of VP1 are transiently externalized. Altogether, our study provides insights into vaccine development against HFMD. PubMed: 25492868DOI: 10.1074/jbc.M114.624536 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.805 Å) |
Structure validation
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