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Journal of Virology, May 2002, p. 4785-4791, Vol. 76, No. 10
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.10.4785-4791.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

DNA Cleavage and Packaging Proteins Encoded by Genes U_L28, U_L15, and U_L33 of Herpes Simplex Virus Type 1 Form a Complex in Infected Cells

Philippa M. Beard, Naomi S. Taus,^, and Joel D. Baines^*

Department of Microbiology and Immunology, Cornell University, Ithaca, New York 14853

Received 5 November 2001/ Accepted 18 February 2002

Previous studies have indicated that the U_L6, U_L15, U_L17, U_L28, U_L32, and U_L33 genes are required for the cleavage and packaging of herpes simplex viral DNA. To identify proteins that interact with the U_L28-encoded DNA binding protein of herpes simplex virus type 1 (HSV-1), a previously undescribed rabbit polyclonal antibody directed against the U_L28 protein fused to glutathione S-transferase was used to immunopurify U_L28 and the proteins with which it associated. It was found that the antibody specifically coimmunoprecipitated proteins encoded by the genes U_L28, U_L15, and U_L33 from lysates of both HEp-2 cells infected with HSV-1(F) and insect cells infected with recombinant baculoviruses expressing these three proteins. In reciprocal reactions, antibodies directed against the U_L15- or U_L33-encoded proteins also coimmunoprecipitated the U_L28 protein. The coimmunoprecipitation of the three proteins from HSV-infected cells confirms earlier reports of an association between the U_L28 and U_L15 proteins and represents the first evidence of the involvement of the U_L33 protein in this complex.

Present address: Department of Veterinary Pathobiology, University of Missouri, Columbia, MO 65211.

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