6IMM

Cryo-EM structure of an alphavirus, Sindbis virus

Summary for 6IMM

• Entry DOI: 10.2210/pdb6imm/pdb
• EMDB information: 9692 9693
• Descriptor: Spike glycoprotein E1, Spike glycoprotein E2, Assembly protein E3, ... (4 entities in total)
• Functional Keywords: alphavirus, sindbis virus, glycoprotein, virus
• Biological source: Sindbis virus (SINV); More
• Total number of polymer chains: 12
• Total formula weight: 391659.95

Authors

Zhang, X.,Ma, J.,Chen, L. (deposition date: 2018-10-23, release date: 2019-03-13, Last modification date: 2024-11-20)

Primary citation

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 3.5 angstrom resolution cryo-EM structure.
Nat Commun, 9:5326-5326, 2018

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. 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.

PubMed: 30552337
DOI: 10.1038/s41467-018-07704-x

Experimental method

ELECTRON MICROSCOPY (3.5 Å)