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A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted

1 Institute of Virology, University of Glasgow, Church Street, Glasgow G11 5JR and 2 Beatson Institute for Cancer Research, Wolfson Laboratory for Molecular Pathology, Garscube Estate, Switchback Road, Bearsden, Glasgow G61 1BD, U.K. Gene UL13 of herpes simplex virus type 1 (HSV-1) has previously be...

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Published in:Journal of general virology 1993-03, Vol.74 (3), p.387-395
Main Authors: Coulter, L. J, Moss, H. W. M, Lang, J, McGeoch, D. J
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Moss, H. W. M
Lang, J
McGeoch, D. J
description 1 Institute of Virology, University of Glasgow, Church Street, Glasgow G11 5JR and 2 Beatson Institute for Cancer Research, Wolfson Laboratory for Molecular Pathology, Garscube Estate, Switchback Road, Bearsden, Glasgow G61 1BD, U.K. 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. Members of the MRC Virology Unit. Present address: Ohio State University, Department of Hematology and Oncology, 1248 James Cancer Hospital, 300 West Tenth Avenue, Columbus, Ohio 43210, U.S.A. Received 3 July 1992; accepted 16 October 1992.
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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. Members of the MRC Virology Unit. Present address: Ohio State University, Department of Hematology and Oncology, 1248 James Cancer Hospital, 300 West Tenth Avenue, Columbus, Ohio 43210, U.S.A. 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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. Members of the MRC Virology Unit. Present address: Ohio State University, Department of Hematology and Oncology, 1248 James Cancer Hospital, 300 West Tenth Avenue, Columbus, Ohio 43210, U.S.A. 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source Freely Accessible Journals
subjects Animals
Biological and medical sciences
Cell Line
Chromosome Mapping
Cricetinae
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genes, Viral - genetics
Genes, Viral - physiology
herpes simplex virus 1
Lac Operon
Microbiology
Mutation - genetics
Mutation - physiology
Phosphorylation
Protein Kinases - genetics
Protein Kinases - metabolism
Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains
Simplexvirus - genetics
Simplexvirus - isolation & purification
Virion - chemistry
Virology
title A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted
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