4YVS
crystal structure of the virus-like particle of a c4 strain EV71
Summary for 4YVS
| Entry DOI | 10.2210/pdb4yvs/pdb |
| Related | 4RQP 4RR3 4RS5 4YVW 4n43 4n53 |
| Descriptor | Capsid protein VP1, Capsid protein VP3, Capsid protein VP0 (3 entities in total) |
| Functional Keywords | virus-like particle, neutralization epitope, 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 | 471745.70 |
| Authors | |
| Primary citation | Lyu, K.,He, Y.L.,Li, H.Y.,Chen, R. Crystal Structures of Yeast-Produced Enterovirus 71 and Enterovirus 71/Coxsackievirus A16 Chimeric Virus-Like Particles Provide the Structural Basis for Novel Vaccine Design against Hand-Foot-and-Mouth Disease J.Virol., 89:6196-6208, 2015 Cited by PubMed Abstract: Human enterovirus 71 (EV71) and coxsackievirus A16 (CVA16) are the two major causative agents for hand-foot-and-mouth disease (HFMD). Previously, we demonstrated that a virus-like particle (VLP) for EV71 produced from Saccharomyces cerevisiae is a potential vaccine candidate against EV71 infection, and an EV71/CVA16 chimeric VLP can elicit protective immune responses against both virus infections. Here, we presented the crystal structures of both VLPs, showing that both the linear and conformational neutralization epitopes identified in EV71 are mostly preserved on both VLPs. The replacement of only 4 residues in the VP1 GH loop converted strongly negatively charged surface patches formed by portions of the SP70 epitope in EV71 VLP into a relatively neutral surface in the chimeric VLP, which likely accounted for the additional neutralization capability of the chimeric VLP against CVA16 infection. Such local variations in the amino acid sequences and the surface charge potential are also present in different types of polioviruses. In comparison to EV71 VLP, the chimeric VLP exhibits structural changes at the local site of amino acid replacement and the surface loops of all capsid proteins. This is consistent with the observation that the VP1 GH loop located near the pseudo-3-fold junction is involved in extensive interactions with other capsid regions. Furthermore, portions of VP0 and VP1 in EV71 VLP are at least transiently exposed, revealing the structural flexibility of the VLP. Together, our structural analysis provided insights into the structural basis of enterovirus neutralization and novel vaccine design against HFMD and other enterovirus-associated diseases. PubMed: 25833050DOI: 10.1128/JVI.00422-15 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.65 Å) |
Structure validation
Download full validation report
