Old World and Clade C New World Arenaviruses Mimic the Molecular Mechanism of Receptor Recognition Used by α-Dystroglycan's Host-Derived Ligands

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Published in	Journal of Virology Vol. 81; no. 11; pp. 5685 - 5695
Main Authors	Rojek, Jillian M., Spiropoulou, Christina F., Campbell, Kevin P., Kunz, Stefan
Format	Journal Article
Language	English
Published	Washington, DC American Society for Microbiology 01.06.2007
Subjects	Animals Arenavirus Arenaviruses, New World - chemistry Arenaviruses, New World - metabolism Arenaviruses, Old World - chemistry Arenaviruses, Old World - metabolism Biological and medical sciences Cell Line, Tumor Cercopithecus aethiops Dystroglycans - chemistry Dystroglycans - metabolism Fundamental and applied biological sciences. Psychology Glycosylation Humans Jurkat Cells Lassa virus Lassa virus - metabolism Ligands Lymphocytic choriomeningitis virus Lymphocytic choriomeningitis virus - chemistry Lymphocytic choriomeningitis virus - metabolism Mice Microbiology Miscellaneous Mobala virus Molecular Mimicry Rabbits Receptors, Virus - chemistry Receptors, Virus - metabolism Vero Cells Virology Virus-Cell Interactions World Mechanism Recognition Virology
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ISSN	0022-538X 1098-5514
DOI	10.1128/JVI.02574-06

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Abstract	Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue 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 © 2014 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: JVI
AbstractList	alpha-Dystroglycan (DG) is an important cellular receptor for extracellular matrix (ECM) proteins and also serves as the receptor for Old World arenaviruses Lassa fever virus (LFV) and lymphocytic choriomeningitis virus (LCMV) and clade C New World arenaviruses. In the host cell, alpha-DG is subject to a remarkably complex pattern of O glycosylation that is crucial for its interactions with ECM proteins. Two of these unusual sugar modifications, protein O mannosylation and glycan modifications involving the putative glycosyltransferase LARGE, have recently been implicated in arenavirus binding. Considering the complexity of alpha-DG O glycosylation, our present study was aimed at the identification of the specific O-linked glycans on alpha-DG that are recognized by arenaviruses. As previously shown for LCMV, we found that protein O mannosylation of alpha-DG is crucial for the binding of arenaviruses of distinct phylogenetic origins, including LFV, Mobala virus, and clade C New World arenaviruses. In contrast to the highly conserved requirement for O mannosylation, more generic O glycans present on alpha-DG are dispensable for arenavirus binding. Despite the critical role of O-mannosyl glycans for arenavirus binding under normal conditions, the overexpression of LARGE in cells deficient in O mannosylation resulted in highly glycosylated alpha-DG that was functional as a receptor for arenaviruses. Thus, modifications by LARGE but not O-mannosyl glycans themselves are most likely the crucial structures recognized by arenaviruses. Together, the data demonstrate that arenaviruses recognize the same highly conserved O-glycan structures on alpha-DG involved in ECM protein binding, indicating a strikingly similar mechanism of receptor recognition by pathogen- and host-derived ligands.alpha-Dystroglycan (DG) is an important cellular receptor for extracellular matrix (ECM) proteins and also serves as the receptor for Old World arenaviruses Lassa fever virus (LFV) and lymphocytic choriomeningitis virus (LCMV) and clade C New World arenaviruses. In the host cell, alpha-DG is subject to a remarkably complex pattern of O glycosylation that is crucial for its interactions with ECM proteins. Two of these unusual sugar modifications, protein O mannosylation and glycan modifications involving the putative glycosyltransferase LARGE, have recently been implicated in arenavirus binding. Considering the complexity of alpha-DG O glycosylation, our present study was aimed at the identification of the specific O-linked glycans on alpha-DG that are recognized by arenaviruses. As previously shown for LCMV, we found that protein O mannosylation of alpha-DG is crucial for the binding of arenaviruses of distinct phylogenetic origins, including LFV, Mobala virus, and clade C New World arenaviruses. In contrast to the highly conserved requirement for O mannosylation, more generic O glycans present on alpha-DG are dispensable for arenavirus binding. Despite the critical role of O-mannosyl glycans for arenavirus binding under normal conditions, the overexpression of LARGE in cells deficient in O mannosylation resulted in highly glycosylated alpha-DG that was functional as a receptor for arenaviruses. Thus, modifications by LARGE but not O-mannosyl glycans themselves are most likely the crucial structures recognized by arenaviruses. Together, the data demonstrate that arenaviruses recognize the same highly conserved O-glycan structures on alpha-DG involved in ECM protein binding, indicating a strikingly similar mechanism of receptor recognition by pathogen- and host-derived ligands. alpha-Dystroglycan (DG) is an important cellular receptor for extracellular matrix (ECM) proteins and also serves as the receptor for Old World arenaviruses Lassa fever virus (LFV) and lymphocytic choriomeningitis virus (LCMV) and clade C New World arenaviruses. In the host cell, alpha-DG is subject to a remarkably complex pattern of O glycosylation that is crucial for its interactions with ECM proteins. Two of these unusual sugar modifications, protein O mannosylation and glycan modifications involving the putative glycosyltransferase LARGE, have recently been implicated in arenavirus binding. Considering the complexity of alpha-DG O glycosylation, our present study was aimed at the identification of the specific O-linked glycans on alpha-DG that are recognized by arenaviruses. As previously shown for LCMV, we found that protein O mannosylation of alpha-DG is crucial for the binding of arenaviruses of distinct phylogenetic origins, including LFV, Mobala virus, and clade C New World arenaviruses. In contrast to the highly conserved requirement for O mannosylation, more generic O glycans present on alpha-DG are dispensable for arenavirus binding. Despite the critical role of O-mannosyl glycans for arenavirus binding under normal conditions, the overexpression of LARGE in cells deficient in O mannosylation resulted in highly glycosylated alpha-DG that was functional as a receptor for arenaviruses. Thus, modifications by LARGE but not O-mannosyl glycans themselves are most likely the crucial structures recognized by arenaviruses. Together, the data demonstrate that arenaviruses recognize the same highly conserved O-glycan structures on alpha-DG involved in ECM protein binding, indicating a strikingly similar mechanism of receptor recognition by pathogen- and host-derived ligands. α-Dystroglycan (DG) is an important cellular receptor for extracellular matrix (ECM) proteins and also serves as the receptor for Old World arenaviruses Lassa fever virus (LFV) and lymphocytic choriomeningitis virus (LCMV) and clade C New World arenaviruses. In the host cell, α-DG is subject to a remarkably complex pattern of O glycosylation that is crucial for its interactions with ECM proteins. Two of these unusual sugar modifications, protein O mannosylation and glycan modifications involving the putative glycosyltransferase LARGE, have recently been implicated in arenavirus binding. Considering the complexity of α-DG O glycosylation, our present study was aimed at the identification of the specific O-linked glycans on α-DG that are recognized by arenaviruses. As previously shown for LCMV, we found that protein O mannosylation of α-DG is crucial for the binding of arenaviruses of distinct phylogenetic origins, including LFV, Mobala virus, and clade C New World arenaviruses. In contrast to the highly conserved requirement for O mannosylation, more generic O glycans present on α-DG are dispensable for arenavirus binding. Despite the critical role of O -mannosyl glycans for arenavirus binding under normal conditions, the overexpression of LARGE in cells deficient in O mannosylation resulted in highly glycosylated α-DG that was functional as a receptor for arenaviruses. Thus, modifications by LARGE but not O -mannosyl glycans themselves are most likely the crucial structures recognized by arenaviruses. Together, the data demonstrate that arenaviruses recognize the same highly conserved O-glycan structures on α-DG involved in ECM protein binding, indicating a strikingly similar mechanism of receptor recognition by pathogen- and host-derived ligands. Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue 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 © 2014 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: JVI
Author	Christina F. Spiropoulou Jillian M. Rojek Stefan Kunz Kevin P. Campbell
AuthorAffiliation	Molecular and Integrative Neurosciences Department, The Scripps Research Institute, La Jolla, California 92037, 1 Howard Hughes Medical Institute, University of Iowa College of Medicine, Department of Molecular Physiology and Biophysics, Department of Neurology, and Department of Internal Medicine, Iowa City, Iowa 52242, 2 Special Pathogens Branch, Centers for Disease Control and Prevention, Atlanta, Georgia 30333 3
AuthorAffiliation_xml	– name: Molecular and Integrative Neurosciences Department, The Scripps Research Institute, La Jolla, California 92037, 1 Howard Hughes Medical Institute, University of Iowa College of Medicine, Department of Molecular Physiology and Biophysics, Department of Neurology, and Department of Internal Medicine, Iowa City, Iowa 52242, 2 Special Pathogens Branch, Centers for Disease Control and Prevention, Atlanta, Georgia 30333 3
Author_xml	– sequence: 1 givenname: Jillian M. surname: Rojek fullname: Rojek, Jillian M. organization: Molecular and Integrative Neurosciences Department, The Scripps Research Institute, La Jolla, California 92037 – sequence: 2 givenname: Christina F. surname: Spiropoulou fullname: Spiropoulou, Christina F. organization: Special Pathogens Branch, Centers for Disease Control and Prevention, Atlanta, Georgia 30333 – sequence: 3 givenname: Kevin P. surname: Campbell fullname: Campbell, Kevin P. organization: Howard Hughes Medical Institute, University of Iowa College of Medicine, Department of Molecular Physiology and Biophysics, Department of Neurology, and Department of Internal Medicine, Iowa City, Iowa 52242 – sequence: 4 givenname: Stefan surname: Kunz fullname: Kunz, Stefan organization: Molecular and Integrative Neurosciences Department, The Scripps Research Institute, La Jolla, California 92037
BackLink	http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18772110$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/17360738$$D View this record in MEDLINE/PubMed
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Snippet	Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... α-Dystroglycan (DG) is an important cellular receptor for extracellular matrix (ECM) proteins and also serves as the receptor for Old World arenaviruses Lassa... alpha-Dystroglycan (DG) is an important cellular receptor for extracellular matrix (ECM) proteins and also serves as the receptor for Old World arenaviruses... alpha -Dystroglycan (DG) is an important cellular receptor for extracellular matrix (ECM) proteins and also serves as the receptor for Old World arenaviruses...
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StartPage	5685
SubjectTerms	Animals Arenavirus Arenaviruses, New World - chemistry Arenaviruses, New World - metabolism Arenaviruses, Old World - chemistry Arenaviruses, Old World - metabolism Biological and medical sciences Cell Line, Tumor Cercopithecus aethiops Dystroglycans - chemistry Dystroglycans - metabolism Fundamental and applied biological sciences. Psychology Glycosylation Humans Jurkat Cells Lassa virus Lassa virus - metabolism Ligands Lymphocytic choriomeningitis virus Lymphocytic choriomeningitis virus - chemistry Lymphocytic choriomeningitis virus - metabolism Mice Microbiology Miscellaneous Mobala virus Molecular Mimicry Rabbits Receptors, Virus - chemistry Receptors, Virus - metabolism Vero Cells Virology Virus-Cell Interactions
Title	Old World and Clade C New World Arenaviruses Mimic the Molecular Mechanism of Receptor Recognition Used by α-Dystroglycan's Host-Derived Ligands
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