+Search query
-Structure paper
Title | Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 9, Issue 1, Page 5326, Year 2018 |
Publish date | Dec 14, 2018 |
![]() | Lihong Chen / Ming Wang / Dongjie Zhu / Zhenzhao Sun / Jun Ma / Jinglin Wang / Lingfei Kong / Shida Wang / Zaisi Liu / Lili Wei / Yuwen He / Jingfei Wang / Xinzheng Zhang / ![]() |
PubMed Abstract | 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. ...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 Å 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. |
![]() | ![]() ![]() ![]() |
Methods | EM (single particle) |
Resolution | 3.5 - 4.7 Å |
Structure data | ![]() EMDB-9692: |
Chemicals | ![]() ChemComp-8K6: |
Source |
|
![]() | VIRUS / Alphavirus / Sindbis virus / Glycoprotein |