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Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus strain Towne.

Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus... Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus strain Towne. R R Spaete , A Saxena , P I Scott , G J Song , W S Probert , W J Britt , W Gibson , L Rasmussen and C Pachl Chiron Corporation, Emeryville, California 94608-2916. ABSTRACT Truncated versions of the human cytomegalovirus (CMV) strain Towne glycoprotein B (gB) gene were stably expressed in CHO cell lines. The calcium-specific ionophore A23187 inhibited proteolytic cleavage of C-terminal-truncated gB expressed by cell line 67.77. These inhibition studies also showed that the 93-kilodalton cleavage product most likely represents the N-terminal cleavage fragment of gB. The ionophore carboxyl cyanide m-chlorophenyl-hydrazone was used to show that proteolytic cleavage of gB did not occur in the endoplasmic reticulum. Two-dimensional polyacrylamide gel electrophoresis demonstrated that the N- and C-terminal cleavage products of gB remained associated by disulfide linkages after cleavage. Expression studies using constructs in which 80% or all of the N terminus was deleted demonstrated that the N terminus was required for secretion of the gB molecule. The amino acid sequence at the site of cleavage was shown to be critical for cleavage by a cellular protease. Our results indicate that an arginine-to-threonine change at either amino acid 457 or 460, a lysine-to-glutamine change at amino acid 459, or all three substitutions together block gB cleavage. The effect on proteolysis of the arginine-to-threonine amino acid change at residue 457 (position -4 relative to the cleavage site) demonstrated that a basic pair of amino acids at the endoproteolytic processing site is not the only requirement in cis for gB cleavage. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Virol. June 1990 vol. 64 no. 6 2922-2931 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JVI Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Spaete, R. R. Articles by Pachl, C. Search for related content PubMed PubMed citation Articles by Spaete, R. R. Articles by Pachl, C. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue January 2012, volume 86, issue 1 Spotlights in the Current Issue Two Xenotropic Murine Leukemia Virus Parents Breaking the Entry Targeting Barrier Complex Morphology and Dynamic Development of Poliovirus Membranous Replication Structures Revealed A Staining Artifact Explains Apparent Varicella-Zoster Virus Protein Expression in Neurons Recent Mumps Outbreaks Are Not Caused by Immune Escape Alert me to new issues of JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: http://intl- JVI .asm.org | More Info» var gaJsHost = (("https:" == document.location.protocol) ? "https://ssl." : "http://www."); document.write(unescape("%3Cscript src='" + gaJsHost + "google-analytics.com/ga.js' type='text/javascript'%3E%3C/script%3E")); var pageTracker = _gat._getTracker("UA-5821458-1"); pageTracker._trackPageview(); http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Virology American Society For Microbiology

Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus strain Towne.

Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus strain Towne.

Journal of Virology , Volume 64 (6): 2922 – Jun 1, 1990

Abstract

Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus strain Towne. R R Spaete , A Saxena , P I Scott , G J Song , W S Probert , W J Britt , W Gibson , L Rasmussen and C Pachl Chiron Corporation, Emeryville, California 94608-2916. ABSTRACT Truncated versions of the human cytomegalovirus (CMV) strain Towne glycoprotein B (gB) gene were stably expressed in CHO cell lines. The calcium-specific ionophore A23187 inhibited proteolytic cleavage of C-terminal-truncated gB expressed by cell line 67.77. These inhibition studies also showed that the 93-kilodalton cleavage product most likely represents the N-terminal cleavage fragment of gB. The ionophore carboxyl cyanide m-chlorophenyl-hydrazone was used to show that proteolytic cleavage of gB did not occur in the endoplasmic reticulum. Two-dimensional polyacrylamide gel electrophoresis demonstrated that the N- and C-terminal cleavage products of gB remained associated by disulfide linkages after cleavage. Expression studies using constructs in which 80% or all of the N terminus was deleted demonstrated that the N terminus was required for secretion of the gB molecule. The amino acid sequence at the site of cleavage was shown to be critical for cleavage by a cellular protease. Our results indicate that an arginine-to-threonine change at either amino acid 457 or 460, a lysine-to-glutamine change at amino acid 459, or all three substitutions together block gB cleavage. The effect on proteolysis of the arginine-to-threonine amino acid change at residue 457 (position -4 relative to the cleavage site) demonstrated that a basic pair of amino acids at the endoproteolytic processing site is not the only requirement in cis for gB cleavage. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Virol. June 1990 vol. 64 no. 6 2922-2931 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JVI Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Spaete, R. R. Articles by Pachl, C. Search for related content PubMed PubMed citation Articles by Spaete, R. R. Articles by Pachl, C. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue January 2012, volume 86, issue 1 Spotlights in the Current Issue Two Xenotropic Murine Leukemia Virus Parents Breaking the Entry Targeting Barrier Complex Morphology and Dynamic Development of Poliovirus Membranous Replication Structures Revealed A Staining Artifact Explains Apparent Varicella-Zoster Virus Protein Expression in Neurons Recent Mumps Outbreaks Are Not Caused by Immune Escape Alert me to new issues of JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: http://intl- JVI .asm.org | More Info» var gaJsHost = (("https:" == document.location.protocol) ? "https://ssl." : "http://www."); document.write(unescape("%3Cscript src='" + gaJsHost + "google-analytics.com/ga.js' type='text/javascript'%3E%3C/script%3E")); var pageTracker = _gat._getTracker("UA-5821458-1"); pageTracker._trackPageview();

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Publisher
American Society For Microbiology
Copyright
Copyright © 1990 by the American society for Microbiology.
ISSN
0022-538X
eISSN
1098-5514
Publisher site
See Article on Publisher Site

Abstract

Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus strain Towne. R R Spaete , A Saxena , P I Scott , G J Song , W S Probert , W J Britt , W Gibson , L Rasmussen and C Pachl Chiron Corporation, Emeryville, California 94608-2916. ABSTRACT Truncated versions of the human cytomegalovirus (CMV) strain Towne glycoprotein B (gB) gene were stably expressed in CHO cell lines. The calcium-specific ionophore A23187 inhibited proteolytic cleavage of C-terminal-truncated gB expressed by cell line 67.77. These inhibition studies also showed that the 93-kilodalton cleavage product most likely represents the N-terminal cleavage fragment of gB. The ionophore carboxyl cyanide m-chlorophenyl-hydrazone was used to show that proteolytic cleavage of gB did not occur in the endoplasmic reticulum. Two-dimensional polyacrylamide gel electrophoresis demonstrated that the N- and C-terminal cleavage products of gB remained associated by disulfide linkages after cleavage. Expression studies using constructs in which 80% or all of the N terminus was deleted demonstrated that the N terminus was required for secretion of the gB molecule. The amino acid sequence at the site of cleavage was shown to be critical for cleavage by a cellular protease. Our results indicate that an arginine-to-threonine change at either amino acid 457 or 460, a lysine-to-glutamine change at amino acid 459, or all three substitutions together block gB cleavage. The effect on proteolysis of the arginine-to-threonine amino acid change at residue 457 (position -4 relative to the cleavage site) demonstrated that a basic pair of amino acids at the endoproteolytic processing site is not the only requirement in cis for gB cleavage. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Virol. June 1990 vol. 64 no. 6 2922-2931 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JVI Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Spaete, R. R. Articles by Pachl, C. Search for related content PubMed PubMed citation Articles by Spaete, R. R. Articles by Pachl, C. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue January 2012, volume 86, issue 1 Spotlights in the Current Issue Two Xenotropic Murine Leukemia Virus Parents Breaking the Entry Targeting Barrier Complex Morphology and Dynamic Development of Poliovirus Membranous Replication Structures Revealed A Staining Artifact Explains Apparent Varicella-Zoster Virus Protein Expression in Neurons Recent Mumps Outbreaks Are Not Caused by Immune Escape Alert me to new issues of JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: http://intl- JVI .asm.org | More Info» var gaJsHost = (("https:" == document.location.protocol) ? "https://ssl." : "http://www."); document.write(unescape("%3Cscript src='" + gaJsHost + "google-analytics.com/ga.js' type='text/javascript'%3E%3C/script%3E")); var pageTracker = _gat._getTracker("UA-5821458-1"); pageTracker._trackPageview();

Journal

Journal of VirologyAmerican Society For Microbiology

Published: Jun 1, 1990

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