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Incorporation of the herpes simplex virus type 1 tegument protein VP22 into the virus particle is independent of interaction with VP16.

O'Regan KJ, Murphy MA, Bucks MA, Wills JW, Courtney RJ

Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033, USA.

Herpes simplex virus type 1 (HSV-1) virions contain a proteinaceous layer termed the tegument that lies between the nucleocapsid and viral envelope. The mechanisms underlying tegumentation remain largely undefined for all herpesviruses. Using glutathione S-transferase (GST) pulldowns and coimmunoprecipitation studies, we have identified a domain of the tegument protein VP22 that facilitates interaction with VP16. This region of VP22 (residues 165-225) overlaps the glycoprotein E (gE) binding domain of VP22 (residues 165-270), which is sufficient to mediate VP22 packaging into assembling virus particles. To ascertain the contribution of the VP16 and gE binding activities of VP22 to its virion incorporation, a transfection/infection based virion incorporation assay, using point mutants that discern between the two binding activities, was utilized. Our results suggest that interaction with VP16 is not required for incorporation of VP22 into virus particles and that binding to the cytoplasmic tail of gE is sufficient to facilitate packaging.

Published 20 November 2007 in Virology, 369(2): 263-80.
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