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Journal of Virology, April 2003, p. 4291-4297, Vol. 77, No. 7
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.7.4291-4297.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Three-Dimensional Localization of pORF65 in Kaposi's Sarcoma-Associated Herpesvirus Capsid

Pierrette Lo,1 Xuekui Yu,1 Ivo Atanasov,1 Bala Chandran,2 and Z. Hong Zhou1*

Department of Pathology and Laboratory Medicine, University of Texas—Houston Medical School, Houston, Texas 77030,1 Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, Kansas 661602

Received 14 October 2002/ Accepted 3 January 2003

Of the six herpesvirus capsid proteins, the smallest capsid proteins (SCPs) share the least sequence homology among herpesvirus family members and have been implicated in virus specificity during infection. The herpes simplex virus-1 (HSV-1) SCP was shown to be horn shaped and to specifically bind the upper domain of each major capsid protein in hexons but not in pentons. In Kaposi's sarcoma-associated herpesvirus (KSHV), the protein encoded by the ORF65 gene (pORF65) is the putative SCP but its location remains controversial due to the absence of such horn-shaped densities from both the pentons and hexons of the KSHV capsid reconstructions. To directly locate the KSHV SCP, we have used electron cryomicroscopy and three-dimensional reconstruction techniques to compare the three-dimensional structure of KSHV capsids to that of anti-pORF65 antibody-labeled capsids. Our difference map shows prominent antibody densities bound to the tips of the hexons but not to pentons, indicating that KSHV SCP is attached to the upper domain of the major capsid protein in hexons but not to that in pentons, similar to HSV-1 SCP. The lack of horn-shaped densities on the hexons indicates that KSHV SCP exhibits structural features that are substantially different from those of HSV-1 SCP. The location of SCP at the outermost regions of the capsid suggests a possible role in mediating capsid interactions with the tegument and cytoskeletal proteins during infection.

* Corresponding author. Mailing address: Department of Pathology and Laboratory Medicine, University of Texas—Houston Medical School, 6431 Fannin St., MSB 2.136, Houston, TX 77030. Phone: (713) 500-5358. Fax: (713) 500-0730. E-mail: z.h.zhou{at}uth.tmc.edu.

Journal of Virology, April 2003, p. 4291-4297, Vol. 77, No. 7
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.7.4291-4297.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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