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J. Virol. doi:10.1128/JVI.01113-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The capsid and tegument of the alpha herpesviruses are linked by an interaction between the UL25 and VP1/2 proteins

Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611

^* To whom correspondence should be addressed. Email: g-smith3{at}northwestern.edu.

	Abstract

How alpha-herpesvirus capsids acquire tegument proteins remains a key question in viral assembly. Using pseudorabies virus (PRV), we have previously shown that the 62 carboxy-terminal amino acids of the VP1/2 large tegument protein are essential for viral propagation, and when transiently expressed as a fusion to GFP relocalize to nuclear capsid assemblons following viral infection. Here we show that localization of the VP1/2 capsid-binding domain (VP1/2cbd) into assemblons is conserved in herpes simplex virus type-1 and that this recruitment is specifically on capsids. Using a mutant virus screen, we find that the protein product of the UL25 gene is essential for VP1/2cbd association with capsids. An interaction between UL25 and VP1/2 was corroborated by co-immunoprecipitation from cells transiently expressing either HSV-1 or PRV proteins. Taken together, these findings suggest that the essential function of the VP1/2 carboxy terminus serves to anchor the VP1/2 tegument protein to capsids. Furthermore, UL25 encodes a multifunctional capsid protein not only involved in encapsidation, as previously described, but also tegumentation.

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