Structural highlights
Publication Abstract from PubMed
Alphaviruses are enveloped RNA viruses that contain several human pathogens. Due to intrinsic heterogeneity of alphavirus particles, a high resolution structure of the virion is currently lacking. Here we provide a 3.5 A cryo-EM structure of Sindbis virus, using block based reconstruction method that overcomes the heterogeneity problem. Our structural analysis identifies a number of conserved residues that play pivotal roles in the virus life cycle. We identify a hydrophobic pocket in the subdomain D of E2 protein that is stabilized by an unknown pocket factor near the viral membrane. Residues in the pocket are conserved in different alphaviruses. The pocket strengthens the interactions of the E1/E2 heterodimer and may facilitate virus assembly. Our study provides structural insights into alphaviruses that may inform the design of drugs and vaccines.
Implication for alphavirus host-cell entry and assembly indicated by a 3.5A resolution cryo-EM structure.,Chen L, Wang M, Zhu D, Sun Z, Ma J, Wang J, Kong L, Wang S, Liu Z, Wei L, He Y, Wang J, Zhang X Nat Commun. 2018 Dec 14;9(1):5326. doi: 10.1038/s41467-018-07704-x. PMID:30552337[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen L, Wang M, Zhu D, Sun Z, Ma J, Wang J, Kong L, Wang S, Liu Z, Wei L, He Y, Wang J, Zhang X. Implication for alphavirus host-cell entry and assembly indicated by a 3.5A resolution cryo-EM structure. Nat Commun. 2018 Dec 14;9(1):5326. doi: 10.1038/s41467-018-07704-x. PMID:30552337 doi:http://dx.doi.org/10.1038/s41467-018-07704-x
