Venezuelan equine encephalomyelitis virus structure and its divergence from old world alphaviruses.
Although alphaviruses have been extensively studied as model systems for the structural organization of enveloped viruses, no structures exist for the phylogenetically distinct eastern equine encephalomyelitis (EEE)-Venezuelan equine encephalomyelitis (VEE) lineage of New World alphaviruses. Here we report the 25-A structure of VEE virus, obtained from electron cryomicroscopy and image reconstruction. The envelope spike glycoproteins of VEE virus have a T=4 icosahedral arrangement, similar to that observed in Old World Sindbis, Semliki Forest, and Ross River alphaviruses. However, VEE virus has pronounced differences in its nucleocapsid structure relative to nucleocapsid structures repeatedly observed in Old World alphaviruses.
Paredes
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A
National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Alwell-Warda
K
K
Weaver
S C
SC
Chiu
W
W
Watowich
S J
SJ
D000524:Alphavirus / Q000648:ultrastructure; D000818:Animals; D005075:Biological Evolution; D004666:Encephalitis Virus, Venezuelan Equine / Q000648:ultrastructure*