5C4W
Crystal structure of coxsackievirus A16
Summary for 5C4W
Entry DOI | 10.2210/pdb5c4w/pdb |
Descriptor | VP1, VP2, VP3, ... (9 entities in total) |
Functional Keywords | hand-foot-and-mouth disease, immunogenicity, picornavirus, icosahedral virus, virus |
Biological source | Coxsackievirus A16 More |
Cellular location | Host cytoplasm : I3W9E1 I3W9E1 I3W9E1 I3W9E1 |
Total number of polymer chains | 4 |
Total formula weight | 95460.95 |
Authors | |
Primary citation | Ren, J.,Wang, X.,Zhu, L.,Hu, Z.,Gao, Q.,Yang, P.,Li, X.,Wang, J.,Shen, X.,Fry, E.E.,Rao, Z.,Stuart, D.I. Structures of Coxsackievirus A16 Capsids with Native Antigenicity: Implications for Particle Expansion, Receptor Binding, and Immunogenicity. J.Virol., 89:10500-10511, 2015 Cited by PubMed Abstract: Enterovirus 71 (EV71) and coxsackievirus A16 (CVA16) are the primary causes of the epidemics of hand-foot-and-mouth disease (HFMD) that affect more than a million children in China each year and lead to hundreds of deaths. Although there has been progress with vaccines for EV71, the development of a CVA16 vaccine has proved more challenging, and the EV71 vaccine does not give useful cross-protection, despite the capsid proteins of the two viruses sharing about 80% sequence identity. The structural details of the expanded forms of the capsids, which possess nonnative antigenicity, are now well understood, but high resolution information for the native antigenic form of CVA16 has been missing. Here, we remedy this with high resolution X-ray structures of both mature and natural empty CVA16 particles and also of empty recombinant viruslike particles of CVA16 produced in insect cells, a potential vaccine antigen. All three structures are unexpanded native particles and antigenically identical. The recombinant particles have recruited a lipid moiety to stabilize the native antigenic state that is different from the one used in a natural virus infection. As expected, the mature CVA16 virus is similar to EV71; however, structural and immunogenic comparisons highlight differences that may have implications for vaccine production. PubMed: 26269176DOI: 10.1128/JVI.01102-15 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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