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Journal of Virology, January 2003, p. 659-664, Vol. 77, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.1.659-664.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Structure of Isolated Nucleocapsids from Venezuelan Equine Encephalitis Virus and Implications for Assembly and Disassembly of Enveloped Virus

Angel Paredes,1 Kathy Alwell-Warda,2,3 Scott C. Weaver,2,3 Wah Chiu,1 and Stanley J. Watowich4,5*

National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030,1 Department of Pathology,2 Center for Tropical Diseases,3 Department of Human Biological Chemistry and Genetics,4 Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 775555

Received 9 May 2002/ Accepted 23 September 2002

Venezuelan equine encephalitis virus (VEEV) is an important human and equine pathogen in the Americas, with widespread reoccurring epidemics extending from South America to the southern United States. Most troubling, VEEV has been made into a weapon by several countries and is currently restricted by the Centers for Disease Control and Prevention as a potential biological warfare and terrorism agent. To facilitate the development of antiviral compounds, the structure of the nucleocapsid isolated from VEEV has been determined by electron cryomicroscopy and image reconstruction and represents the first three-dimensional structure of a nucleocapsid isolated from a single-stranded enveloped RNA virus. The isolated VEEV nucleocapsid undergoes significant reorganization relative to its structure within VEEV. However, the isolated nucleocapsid clearly exhibits T=4 icosahedral symmetry, and its characteristic nucleocapsid hexons and pentons are preserved. The diameter of the isolated nucleocapsid is ~11.5% larger than that of the nucleocapsid within VEEV, with radial expansion being greatest near the hexons. Significantly, this is the first direct structural evidence showing that a simple enveloped virus undergoes large conformational changes during maturation, suggesting that the lipid bilayer and the transmembrane proteins of simple enveloped viruses provide the energy necessary to reorganize the nucleocapsid during maturation.

* Corresponding author. Mailing address: Department of Human Biological Chemistry and 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.

Journal of Virology, January 2003, p. 659-664, Vol. 77, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.1.659-664.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.





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