3J0C

Models of E1, E2 and CP of Venezuelan Equine Encephalitis Virus TC-83 strain restrained by a near atomic resolution cryo-EM map

Summary for 3J0C

• Entry DOI: 10.2210/pdb3j0c/pdb
• Related: 3J0G
• EMDB information: 5275 5276
• Descriptor: E1 envelope glycoprotein, E2 envelope glycoprotein, Capsid protein (3 entities in total)
• Functional Keywords: alphavirus, bioweapon, virus
• Biological source: Venezuelan equine encephalitis virus (VEEV); More
• Total number of polymer chains: 12
• Total formula weight: 453046.61

Authors

Zhang, R.,Hryc, C.F.,Cong, Y.,Liu, X.,Jakana, J.,Gorchakov, R.,Baker, M.L.,Weaver, S.C.,Chiu, W. (deposition date: 2011-06-22, release date: 2011-08-24, Last modification date: 2024-10-30)

Primary citation

Zhang, R.,Hryc, C.F.,Cong, Y.,Liu, X.,Jakana, J.,Gorchakov, R.,Baker, M.L.,Weaver, S.C.,Chiu, W.
4.4 A cryo-EM structure of an enveloped alphavirus Venezuelan equine encephalitis virus.
Embo J., 30:3854-3863, 2011

PubMed Abstract: Venezuelan equine encephalitis virus (VEEV), a member of the membrane-containing Alphavirus genus, is a human and equine pathogen, and has been developed as a biological weapon. Using electron cryo-microscopy (cryo-EM), we determined the structure of an attenuated vaccine strain, TC-83, of VEEV to 4.4 Å resolution. Our density map clearly resolves regions (including E1, E2 transmembrane helices and cytoplasmic tails) that were missing in the crystal structures of domains of alphavirus subunits. These new features are implicated in the fusion, assembly and budding processes of alphaviruses. Furthermore, our map reveals the unexpected E3 protein, which is cleaved and generally thought to be absent in the mature VEEV. Our structural results suggest a mechanism for the initial stage of nucleocapsid core formation, and shed light on the virulence attenuation, host recognition and neutralizing activities of VEEV and other alphavirus pathogens.

PubMed: 21829169
DOI: 10.1038/emboj.2011.261

Experimental method

ELECTRON MICROSCOPY (4.8 Å)