A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted.
Gene UL13 of herpes simplex virus type 1 (HSV-1) has previously been proposed to encode a protein kinase. An HSV-1 mutant with UL13 inactivated by insertion of the Escherichia coli lacZ gene was constructed. This UL13-lacZ mutant was found to grow to near wild-type (wt) titres in tissue culture. Comparison of silver-stained SDS-PAGE profiles of wt and UL13-lacZ virions demonstrated that the UL13 protein is a readily detectable component of wt virions, located in the tegument and probably equivalent to the previously described species VP18.8. Studies of in vitro phosphorylation with nuclear extracts of virus-infected cells and with detergent-treated virions showed that the UL13 protein is involved in phosphorylation of the tegument protein VP22. Extracts of cells engineered to express UL13, and infected with UL13-lacZ virus, were also capable of VP22 phosphorylation.
Coulter
L J
LJ
Institute of Virology, University of Glasgow, U.K.
Moss
H W
HW
Lang
J
J
McGeoch
D J
DJ
D000818:Animals; D002460:Cell Line; D002874:Chromosome Mapping; D006224:Cricetinae; D004926:Escherichia coli / Q000235:genetics; D005814:Genes, Viral / Q000235:genetics* / Q000502:physiology; D007763:Lac Operon; D009154:Mutation / Q000235:genetics* / Q000502:physiology; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics* / Q000378:metabolism; D018139:Simplexvirus / Q000235:genetics* / Q000302:isolation & purification; D014771:Virion / Q000737:chemistry
D011494:Protein Kinases