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Journal of Virology, October 2001, p. 9532-9537, Vol. 75, No. 19
National Center for Macromolecular Imaging,
Verna and Marrs McLean Department of Biochemistry and Molecular
Biology, Baylor College of Medicine, Houston, Texas
77030,1 and Department of Pathology and
the Center for Tropical Diseases2 and
the Department of Human Biological Chemistry & Genetics and
Sealy Center for Structural Biology,3 University
of Texas Medical Branch, Galveston, Texas 77555
Received 9 April 2001/Accepted 22 June 2001
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-Å 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.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.19.9532-9537.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Venezuelan Equine Encephalomyelitis Virus Structure
and Its Divergence from Old World Alphaviruses
*
Corresponding author. Mailing address: Department of
Human Biological Chemistry & Genetics, University of Texas Medical
Branch, Galveston, TX 77555-0645. Phone: (409) 747-4749. Fax: (409)
747-4745. E-mail: watowich{at}bloch.utmb.edu.
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