Proteomic analysis of the herpes simplex virus 1 virion protein 16 transactivator protein in infected cells. Issue 12 (29th April 2015)

• Record Type: Journal Article
• Authors: Suk, Hyung; Knipe, David M.; Cristea, Ileana M.; Graham, David
• Is Part Of: Proteomics. Volume 15:Issue 12(2015:Jun.)
• Page Start: 1957
• Page End: 1967
• Publication Date: 2015-04-29
• Subjects: Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.201500020
• Languages: English
• ISSNs: 1615-9853

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The herpes simplex virus 1 virion protein 16 (VP16) tegument protein forms a transactivation complex with the cellular proteins host cell factor 1 (HCF‐1) and octamer‐binding transcription factor 1 (Oct‐1) upon entry into the host cell. VP16 has also been shown to interact with a number of virion tegument proteins and viral glycoprotein H to promote viral assembly, but no comprehensive study of the VP16 proteome has been performed at early times postinfection. We therefore performed a proteomic analysis of VP16‐interacting proteins at 3 h postinfection. We confirmed the interaction of VP16 with HCF‐1 and a large number of cellular Mediator complex proteins, but most surprisingly, we found that the major viral protein associating with VP16 is the infected cell protein 4 (ICP4) immediate‐early (IE) transactivator protein. These results raise the potential for a new function for VP16 in associating with the IE ICP4 and playing a role in transactivation of early and late gene expression, in addition to its well‐documented function in transactivation of IE gene expression.</p> </abstract>