DNA Cleavage and Packaging Proteins Encoded by Genes U sub(L)28, U sub(L)15, and U sub(L)33 of Herpes Simplex Virus Type 1 Form a Complex in Infected Cells

• Published in: Journal of virology Vol. 76; no. 10; pp. 4785 - 4791
• Main Authors: Beard, P M, Taus, N S, Baines, J D
• Format: Journal Article
• Language: English
• Published: 01-05-2002
• Subjects: Herpes simplex virus 1; UL15 gene; UL28 gene; UL33 gene
• ISSN: 0022-538X
• DOI: 10.1128/JVI.76.10.4785-4791.2002

Previous studies have indicated that the U sub(L)6, U sub(L)15, U sub(L)17, U sub(L)28, U sub(L)32, and U sub(L)33 genes are required for the cleavage and packaging of herpes simplex viral DNA. To identify proteins that interact with the U sub(L)28-encoded DNA binding protein of herpes simplex virus type 1 (HSV-1), a previously undescribed rabbit polyclonal antibody directed against the U sub(L)28 protein fused to glutathione S-transferase was used to immunopurify U sub(L)28 and the proteins with which it associated. It was found that the antibody specifically coimmunoprecipitated proteins encoded by the genes U sub(L)28, U sub(L)15, and U sub(L)33 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 sub(L)15- or U sub(L)33-encoded proteins also coimmunoprecipitated the U sub(L)28 protein. The coimmunoprecipitation of the three proteins from HSV-infected cells confirms earlier reports of an association between the U sub(L)28 and U sub(L)15 proteins and represents the first evidence of the involvement of the U sub(L)33 protein in this complex.