4rs5

Crystal structure of an uncoating intermediate of a EV71 recombinant virus

spinqualitylabelsall models 4rs5, resolution 3.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rs5 is a 15 chain structure with sequence from Ev-71. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4n43, 4n53, 4rqp, 4rr3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Crystal structures of enterovirus 71 (EV71) recombinant virus particles provide insights into vaccine design.,Lyu K, Wang GC, He YL, Han JF, Ye Q, Qin CF, Chen R J Biol Chem. 2015 Feb 6;290(6):3198-208. doi: 10.1074/jbc.M114.624536. Epub 2014 , Dec 9. PMID:25492868 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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