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Virology. 2007 Nov 10;368(1):26-31. Epub 2007 Jul 24.

Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1/2) mediate binding of tegument protein pUL37.

Author information

1
Centre For Virus Research, The Westmead Millennium Institute, The University of Sydney and Westmead Hospital, PO Box 412, Westmead, NSW 2145, Australia.

Abstract

The herpes simplex virus type 1 (HSV-1) structural tegument proteins pUL36 (VP1/2) and pUL37 are essential for secondary envelopment during the egress of viral particles. Our laboratory has previously shown that HSV-1 pUL36(512-767) fragment interacts with full-length pUL37. A number of single and double amino acid changes of conserved residues in the pUL36(512-767) fragment were generated using alanine-scanning site-directed mutagenesis. The interaction of pUL36(512-767) and pUL37 was then assessed using a combination of yeast two-hybrid and coimmunoprecipitation assays. Single changes to alanine of pUL36 residues F593 and E596 impaired binding of pUL37 with the greatest effect observed for the substitution E596A. Double mutations involving either of these residues in combination with the substitution E580A essentially blocked binding of pUL37. This information will provide the basis for generation of viral mutants to further define the importance of the pUL36/pUL37 interaction in assembly of HSV-1.

PMID:
17651773
DOI:
10.1016/j.virol.2007.07.005
[Indexed for MEDLINE]
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