DNA Cleavage and Packaging Proteins Encoded by Genes UL28, UL15, and UL33 of Herpes Simplex Virus Type 1 Form a Complex in Infected Cells

AUTOR(ES)

Beard, Philippa M.

FONTE

American Society for Microbiology

RESUMO

Previous studies have indicated that the UL6, UL15, UL17, UL28, UL32, and UL33 genes are required for the cleavage and packaging of herpes simplex viral DNA. To identify proteins that interact with the UL28-encoded DNA binding protein of herpes simplex virus type 1 (HSV-1), a previously undescribed rabbit polyclonal antibody directed against the UL28 protein fused to glutathione S-transferase was used to immunopurify UL28 and the proteins with which it associated. It was found that the antibody specifically coimmunoprecipitated proteins encoded by the genes UL28, UL15, and UL33 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 UL15- or UL33-encoded proteins also coimmunoprecipitated the UL28 protein. The coimmunoprecipitation of the three proteins from HSV-infected cells confirms earlier reports of an association between the UL28 and UL15 proteins and represents the first evidence of the involvement of the UL33 protein in this complex.

Documentos Relacionados

• Quantification of the DNA Cleavage and Packaging Proteins UL15 and UL28 in A and B Capsids of Herpes Simplex Virus Type 1
• Physical and Functional Interactions between the Herpes Simplex Virus UL15 and UL28 DNA Cleavage and Packaging Proteins
• Herpes Simplex Virus Type 1 Cleavage and Packaging Proteins UL15 and UL28 Are Associated with B but Not C Capsids during Packaging
• Herpes Simplex Virus DNA Cleavage and Packaging: Association of Multiple Forms of UL15-Encoded Proteins with B Capsids Requires at Least the UL6, UL17, and UL28 Genes
• The cDNA of UL15, a highly conserved herpes simplex virus 1 gene, effectively replaces the two exons of the wild-type virus.