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The UL97 protein kinase of human cytomegalovirus and homologues in other herpesviruses: impact on virus and host by Detlef Michel; Thomas Mertens is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The human herpesviruses, herpes simplex virus 1 (HSV-1), HSV-2, varicella zoster virus (VZV), Epstein -Barr virus (EBV), human cytomegalovirus (HCMV), human herpesvirus 6A (HHV-6A), HHV-6B, HHV-7 and HHV-8, establish persistent infections with possible recurrence during immunosuppression. HCMV replication is inhibited by the nucleoside analogue ganciclovir (GCV), the compound of choice for the treatment of HCMV diseases and preemptive treatment of infections. The viral UL97 protein (pUL97) which shares homologies with protein kinases and bacterial phosphotransferases is able to monophosphorylate GCV. Homologues of pUL97 are found in HSV (UL13), VZV (ORF47), EBV (BGLF4), HHV-6 (U69), HHV-8 (ORF36) as well as in murine CMV (M97) or rat CMV (R97). Several indolocarbazoles have been reported to be specific inhibitors of pUL97. The protein is important for efficient replication of the virus. Autophosphorylation of pUL97 was observed using different experimental systems. Most recently, it has been shown that pUL97 interacts with the DNA polymerase processivity factor pUL44. Indolocarbazole protein kinase inhibitors are promising lead compounds for the development of more specific inhibit

Who reads The UL97 protein kinase of human cytomegalovirus and homologues in other herpesviruses: impact on virus and host?

Author

Detlef Michel; Thomas Mertens

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1570-9639)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)