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TitleImplication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 5326, Year 2018
Publish dateDec 14, 2018
AuthorsLihong 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 AbstractAlphaviruses 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.
External linksNat Commun / PubMed:30552337 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 4.7 Å
Structure data

EMDB-9692:
Cryo-EM structure of alphavirus capsid
Method: EM (single particle) / Resolution: 4.7 Å

9693

6imm

EMDB-9693, PDB-6imm:
Cryo-EM structure of an alphavirus, Sindbis virus
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-8K6:
Octadecane

Source
  • SINV (virus)
  • sindbis virus
KeywordsVIRUS / Alphavirus / Sindbis virus / Glycoprotein

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