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Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses

Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses Maurice C. Kemp , Sukla Basak and Richard W. Compans Department of Microbiology, University of Alabama Medical Center, Birmingham, Alabama 35294 ABSTRACT The glycopeptides obtained by pronase digestion of two ecotropic strains of murine leukemia virus (MuLV) were compared by gel filtration. Four different glycopeptide size classes, designated G 1 , G 2 , G 3 , and G 4 , with molecular weights of approximately 5,100, 2,900, 2,200, and 1,500, respectively, were shown to be associated with Rauscher MuLV virions grown in JLS-V9 cells. Various sugar precursors, including glucosamine, galactose, fucose, and mannose were incorporated into G 1 and G 2 , suggesting that these are complex (type I) glycopeptides. The two smaller glycopeptide size classes, G 3 and G 4 , were shown to be mannoserich (type II) glycopeptides. G 4 was more sensitive to digestion with endo-β- N -acetylglucosaminidase H than G 3 , suggesting that the core of G 3 may contain fewer mannose residues. Glycopeptides of the same size class as G 1 and G 2 were associated with both Rauscher MuLV and AKR-MuLV grown in III6A (mouse embryo) cells. Previous studies have shown that gp52, a proteolytic cleavage product of gp70, possessed primarily G 1 glycopeptides and that gp52 was more highly sulfated than gp70. We observed that G 1 is approximately twofold more highly sulfated than G 2 , explaining the observed difference in sulfation of gp52. The unusually large size of G 1 suggested that infection with MuLV may alter the host cell glycosylation pattern. To test this possibility, glycopeptides from Sindbis virions grown in uninfected and Rauscher MuLV-infected JLS-V9 cells were compared, and no differences were observed. G 1 was not detected in Sindbis virions, indicating that acquisition of G 1 depends on properties of the virus-coded polypeptide backbone of the gp70 molecule. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Virol. July 1979 vol. 31 no. 1 1-7 » Abstract PDF Classifications Animal Viruses 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 Kemp, M. C. Articles by Compans, R. W. Search for related content PubMed PubMed citation Articles by Kemp, M. C. Articles by Compans, R. W. 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

Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses

Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses

Journal of Virology , Volume 31 (1): 1 – Jul 1, 1979

Abstract

Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses Maurice C. Kemp , Sukla Basak and Richard W. Compans Department of Microbiology, University of Alabama Medical Center, Birmingham, Alabama 35294 ABSTRACT The glycopeptides obtained by pronase digestion of two ecotropic strains of murine leukemia virus (MuLV) were compared by gel filtration. Four different glycopeptide size classes, designated G 1 , G 2 , G 3 , and G 4 , with molecular weights of approximately 5,100, 2,900, 2,200, and 1,500, respectively, were shown to be associated with Rauscher MuLV virions grown in JLS-V9 cells. Various sugar precursors, including glucosamine, galactose, fucose, and mannose were incorporated into G 1 and G 2 , suggesting that these are complex (type I) glycopeptides. The two smaller glycopeptide size classes, G 3 and G 4 , were shown to be mannoserich (type II) glycopeptides. G 4 was more sensitive to digestion with endo-β- N -acetylglucosaminidase H than G 3 , suggesting that the core of G 3 may contain fewer mannose residues. Glycopeptides of the same size class as G 1 and G 2 were associated with both Rauscher MuLV and AKR-MuLV grown in III6A (mouse embryo) cells. Previous studies have shown that gp52, a proteolytic cleavage product of gp70, possessed primarily G 1 glycopeptides and that gp52 was more highly sulfated than gp70. We observed that G 1 is approximately twofold more highly sulfated than G 2 , explaining the observed difference in sulfation of gp52. The unusually large size of G 1 suggested that infection with MuLV may alter the host cell glycosylation pattern. To test this possibility, glycopeptides from Sindbis virions grown in uninfected and Rauscher MuLV-infected JLS-V9 cells were compared, and no differences were observed. G 1 was not detected in Sindbis virions, indicating that acquisition of G 1 depends on properties of the virus-coded polypeptide backbone of the gp70 molecule. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Virol. July 1979 vol. 31 no. 1 1-7 » Abstract PDF Classifications Animal Viruses 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 Kemp, M. C. Articles by Compans, R. W. Search for related content PubMed PubMed citation Articles by Kemp, M. C. Articles by Compans, R. W. 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 © 1979 by the American society for Microbiology.
ISSN
0022-538X
eISSN
1098-5514
Publisher site
See Article on Publisher Site

Abstract

Glycopeptides of Murine Leukemia Viruses I. Comparison of Two Ecotropic Viruses Maurice C. Kemp , Sukla Basak and Richard W. Compans Department of Microbiology, University of Alabama Medical Center, Birmingham, Alabama 35294 ABSTRACT The glycopeptides obtained by pronase digestion of two ecotropic strains of murine leukemia virus (MuLV) were compared by gel filtration. Four different glycopeptide size classes, designated G 1 , G 2 , G 3 , and G 4 , with molecular weights of approximately 5,100, 2,900, 2,200, and 1,500, respectively, were shown to be associated with Rauscher MuLV virions grown in JLS-V9 cells. Various sugar precursors, including glucosamine, galactose, fucose, and mannose were incorporated into G 1 and G 2 , suggesting that these are complex (type I) glycopeptides. The two smaller glycopeptide size classes, G 3 and G 4 , were shown to be mannoserich (type II) glycopeptides. G 4 was more sensitive to digestion with endo-β- N -acetylglucosaminidase H than G 3 , suggesting that the core of G 3 may contain fewer mannose residues. Glycopeptides of the same size class as G 1 and G 2 were associated with both Rauscher MuLV and AKR-MuLV grown in III6A (mouse embryo) cells. Previous studies have shown that gp52, a proteolytic cleavage product of gp70, possessed primarily G 1 glycopeptides and that gp52 was more highly sulfated than gp70. We observed that G 1 is approximately twofold more highly sulfated than G 2 , explaining the observed difference in sulfation of gp52. The unusually large size of G 1 suggested that infection with MuLV may alter the host cell glycosylation pattern. To test this possibility, glycopeptides from Sindbis virions grown in uninfected and Rauscher MuLV-infected JLS-V9 cells were compared, and no differences were observed. G 1 was not detected in Sindbis virions, indicating that acquisition of G 1 depends on properties of the virus-coded polypeptide backbone of the gp70 molecule. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Virol. July 1979 vol. 31 no. 1 1-7 » Abstract PDF Classifications Animal Viruses 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 Kemp, M. C. Articles by Compans, R. W. Search for related content PubMed PubMed citation Articles by Kemp, M. C. Articles by Compans, R. W. 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: Jul 1, 1979

There are no references for this article.