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

E. L. Blewett, V. Misra

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2083-2090
Number of pages8
JournalJournal of General Virology
Volume72
Issue number9
DOIs
StatePublished - 1 Jan 1991

Fingerprint

Cercopithecine Herpesvirus 1
Glycoproteins
Simplexvirus
Viruses
Peptide Hydrolases
Cell Membrane
Herpesviridae
Membrane Glycoproteins
Virus Diseases
Disulfides
Virion
Monoclonal Antibodies
Membranes
Infection
Genes

Cite this

@article{79fdd3c62fda4ff3b6c04660bc2c8afa,
title = "Cleavage of the bovine herpesvirus glycoprotein B is not essential for its function",
abstract = "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.",
author = "Blewett, {E. L.} and V. Misra",
year = "1991",
month = "1",
day = "1",
doi = "10.1099/0022-1317-72-9-2083",
language = "English",
volume = "72",
pages = "2083--2090",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "9",

}

Cleavage of the bovine herpesvirus glycoprotein B is not essential for its function. / Blewett, E. L.; Misra, V.

In: Journal of General Virology, Vol. 72, No. 9, 01.01.1991, p. 2083-2090.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Cleavage of the bovine herpesvirus glycoprotein B is not essential for its function

AU - Blewett, E. L.

AU - Misra, V.

PY - 1991/1/1

Y1 - 1991/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0025742835&partnerID=8YFLogxK

U2 - 10.1099/0022-1317-72-9-2083

DO - 10.1099/0022-1317-72-9-2083

M3 - Article

C2 - 1654372

AN - SCOPUS:0025742835

VL - 72

SP - 2083

EP - 2090

JO - Journal of General Virology

JF - Journal of General Virology

SN - 0022-1317

IS - 9

ER -