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Journal of Virology, March 2001, p. 2879-2890, Vol. 75, No. 6
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.6.2879-2890.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Capsid Structure of Kaposi's Sarcoma-Associated Herpesvirus, a Gammaherpesvirus, Compared to Those of an Alphaherpesvirus, Herpes Simplex Virus Type 1, and a Betaherpesvirus, Cytomegalovirus

Benes L. Trus,1,2 J. Bernard Heymann,1 Karin Nealon,3,4 Naiqian Cheng,1 William W. Newcomb,3 Jay C. Brown,3 Dean H. Kedes,3,4,5 and Alasdair C. Steven1,*

Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases,1 and Computational Bioscience and Engineering Laboratory, Center for Information Technology,2 National Institutes of Health, Bethesda, Maryland 20892, and Department of Microbiology,3 Department of Internal Medicine,5 and Myles H. Thaler Center for AIDS and Human Retrovirus Research,4 University of Virginia Health System, Charlottesville, Virginia 22908

Received 3 October 2000/Accepted 13 December 2000

The capsid of Kaposi's sarcoma-associated herpesvirus (KSHV) was visualized at 24-Å resolution by cryoelectron microscopy. Despite limited sequence similarity between corresponding capsid proteins, KSHV has the same T=16 triangulation number and much the same capsid architecture as herpes simplex virus (HSV) and cytomegalovirus (CMV). Its capsomers are hexamers and pentamers of the major capsid protein, forming a shell with a flat, close-packed, inner surface (the "floor") and chimney-like external protrusions. Overlying the floor at trigonal positions are (alpha beta 2) heterotrimers called triplexes. The floor structure is well conserved over all three viruses, and the most variable capsid features reside on the outer surface, i.e., in the shapes of the protrusions and triplexes, in which KSHV resembles CMV and differs from HSV. Major capsid protein sequences from the three subfamilies have some similarity, which is closer between KSHV and CMV than between either virus and HSV. The triplex proteins are less highly conserved, but sequence analysis identifies relatively conserved tracts. In alphaherpesviruses, the alpha -subunit (VP19c in HSV) has a 100-residue N-terminal extension and an insertion near the C terminus. The small basic capsid protein sequences are highly divergent: whereas the HSV and CMV proteins bind only to hexons, difference mapping suggests that the KSHV protein, ORF65, binds around the tips of both hexons and pentons.

* Corresponding author. Mailing address: Bldg. 6, Rm. B2-34, MSC 2717, National Institutes of Health, Bethesda, MD 20892-2717. Phone: (301) 496-0132. Fax: (301) 480-7629. E-mail: Alasdair_Steven{at}nih.gov.

Journal of Virology, March 2001, p. 2879-2890, Vol. 75, No. 6
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.6.2879-2890.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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