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Journal of Virology, March 2001, p. 2866-2878, Vol. 75, No. 6
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.6.2866-2878.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Lytic Replication of Kaposi's Sarcoma-Associated Herpesvirus Results in the Formation of Multiple Capsid Species: Isolation and Molecular Characterization of A, B, and C Capsids from a Gammaherpesvirus

K. Nealon,1 W. W. Newcomb,1 T. R. Pray,2 C. S. Craik,2 J. C. Brown,1 and D. H. Kedes1,3,4,*

Department of Internal Medicine,3 Myles H. Thaler Center for AIDS and Human Retrovirus Research,4 and Department of Microbiology,1 University of Virginia Health System, Charlottesville, Virginia, and Departments of Pharmaceutical Chemistry, Pharmacology, and Biochemistry & Biophysics, University of California, San Francisco, San Francisco, California2

Received 2 October 2000/Accepted 11 December 2000

Despite the discovery of Epstein-Barr virus more than 35 years ago, a thorough understanding of gammaherpesvirus capsid composition and structure has remained elusive. We approached this problem by purifying capsids from Kaposi's sarcoma-associated herpesvirus (KSHV), the only other known human gammaherpesvirus. The results from our biochemical and imaging analyses demonstrate that KSHV capsids possess a typical herpesvirus icosahedral capsid shell composed of four structural proteins. The hexameric and pentameric capsomers are composed of the major capsid protein (MCP) encoded by open reading frame 25. The heterotrimeric complexes, forming the capsid floor between the hexons and pentons, are each composed of one molecule of ORF62 and two molecules of ORF26. Each of these proteins has significant amino acid sequence homology to capsid proteins in alpha- and betaherpesviruses. In contrast, the fourth protein, ORF65, lacks significant sequence homology to its structural counterparts from the other subfamilies. Nevertheless, this small, basic, and highly antigenic protein decorates the surface of the capsids, as does, for example, the even smaller basic capsid protein VP26 of herpes simplex virus type 1. We have also found that, as with the alpha- and betaherpesviruses, lytic replication of KSHV leads to the formation of at least three capsid species, A, B, and C, with masses of approximately 200, 230, and 300 MDa, respectively. A capsids are empty, B capsids contain an inner array of a fifth structural protein, ORF17.5, and C capsids contain the viral genome.

* Corresponding author. Mailing address: Myles H. Thaler Center for HIV and Retrovirus Research, Departments of Microbiology and Internal Medicine, Division of Infectious Diseases, University of Virginia Health System, P.O. Box 800734, Jordan Hall, Rm. 7069, 1300 Jefferson Park Ave., Charlottesville, VA 22908-0734. Phone: (804) 243-2758. Fax: (804) 982-1071. E-mail: kedes{at}virginia.edu.

Journal of Virology, March 2001, p. 2866-2878, Vol. 75, No. 6
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.6.2866-2878.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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