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J Gen Virol 72 (1991), 2771-2775; DOI 10.1099/0022-1317-72-11-2771
© 1991 Society for General Microbiology
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Post-translational modification of the tegument proteins (VP13 and VP14) of herpes simplex virus type 1 by glycosylation and phosphorylation

David M. Meredith, Jennifer A. Lindsay, Ian W. Halliburton and Gary R. Whittaker

Department of Microbiology, University of Leeds, Leeds LS2 9JT, U.K.

VP13 and VP14, major tegument proteins of herpes simplex virus type 1 (HSV-1) and the products of the UL47 gene, have been shown by partial proteolytic mapping to have closely related protein sequences. These proteins are phosphorylated in virus-infected cells, but not in preparations of purified virus. They also contain O-linked oligosaccharide units which include beta-1,4-N-acetyl galactosamine residues, as demonstrated by the binding of Dolichos biflorus lectin. This modification was detected only in purified virus and appears to be restricted to VP13/14 and VP22, another HSV-1 tegument protein.

Received 19 April 1991; accepted 17 July 1991.


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