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 Blewett, E. L. Articles by Misra, V. Search for Related Content PubMed PubMed Citation Articles by Blewett, E. L. Articles by Misra, V. Agricola Articles by Blewett, E. L. Articles by Misra, V.

Cleavage of the bovine herpesvirus glycoprotein B is not essential for its function

Department of Veterinary Microbiology, Western College of Veterinary Medicine, University of Saskatchewan, Saskatoon, Saskatchewan S7N 0W0, Canada

Herpes simplex virus glycoprotein B (HSVgB) and its bovine herpesvirus homologue (BHVgB) share similar primary structures. These glycoproteins are present in the envelope of the virion and are believed to initiate infection by fusing the virus envelope with a host cell membrane. BHVgB, like the membrane-fusing glycoproteins of most enveloped viruses, is normally cleaved and is present as a disulphide-linked complex in the virus envelope and host cell membranes. HSVgB, however, remains uncleaved, presumably because it lacks a similar protease recognition sequence. To determine whether the cleavage of BHVgB is essential for its role in initiating infection, we altered the coding sequence of this glycoprotein by removing the protease cleavage site and making this region similar to that of HSVgB. The mutant BHVgB gene was expressed by an HSV recombinant virus in mouse L cells and produced an uncleaved BHVgB. The uncleaved BHVgB could complement the function of HSVgB which had been neutralized by monoclonal antibody H233. When expressed in mouse L cells, the uncleaved mutant BHVgB retained its ability to fuse membranes.

Received 22 March 1991; accepted 31 May 1991.

This article has been cited by other articles:

				W. Li, T. J. Minova-Foster, D. D. Norton, and M. I. Muggeridge Identification of functional domains in herpes simplex virus 2 glycoprotein B. J. Virol., April 1, 2006; 80(8): 3792 - 3800. [Abstract] [Full Text] [PDF]