HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Hope, R. G. Articles by Marsden, H. S. Search for Related Content PubMed PubMed Citation Articles by Hope, R. G. Articles by Marsden, H. S. Agricola Articles by Hope, R. G. Articles by Marsden, H. S.

Sulphated Glycoproteins Induced by Herpes Simplex Virus

M. Suh

Medical Research Council Virology Unit, Institute of Virology, University of Glasgow, Church Street, Glasgow G11 5JR, U.K.

BHK cells infected with strain 17 syn⁺ (HSV-1) or HG52 (HSC-2) incorporated inorganic sulphate into polypeptides which co-migrated on SDS-polyacrylamide gels with virus-induced glycoproteins. The major sulphated glycoprotein was glycoprotein E. In addition, less-intense sulphated bands co-migrated with glycoprotein D and HSV-1 glycoprotein A/B/C. Sulphate label co-migrating with HSV-2 glycoprotein A/B/C was occasionally observed. We have investigated which sulphated polypeptides are excreted from infected cells. Major ones of apparent mol. wt. 32000, 34000 and 35000 were excreted from cells infected with 17 syn⁺. In addition, polypeptides which migrated in the vicinity of glycoprotein D were often excreted from cells infected with either 17 syn⁺ or HG52. The 32K, 34K and 35K polypeptides were antigenically related to glycoprotein D and over 95% of the total amount synthesized was excreted. Analysis of intracellular sulphated polypeptides using intertypic recombinants mapped glycoprotein E to between 0·832 and 0·950 units of the HSV genome.

Keywords: HSV, glycoproteins, sulphation, gene mapping

Present address: Institute du Cancer de Montreal, Centre Hospitalier Notre-dame, 1560 Est, Sherbrooke, Montreal, Canada, H21 4MI.

Received 20 July 1981; accepted 7 October 1981.

This article has been cited by other articles:

				V. Miriagou, L. Stevanato, R. Manservigi, and P. Mavromara The C-terminal cytoplasmic tail of herpes simplex virus type 1 gE protein is phosphorylated in vivo and in vitro by cellular enzymes in the absence of other viral proteins J. Gen. Virol., April 1, 2000; 81(4): 1027 - 1031. [Abstract] [Full Text]