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Proteomics. 2015 Jun;15(12):1957-67. doi: 10.1002/pmic.201500020. Epub 2015 Apr 29.

Proteomic analysis of the herpes simplex virus 1 virion protein 16 transactivator protein in infected cells.

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Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, USA.


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.


Herpes simplex virus; ICP4; Infected; Microbiology; VP16

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