Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry.
Identifieur interne : 005427 ( Main/Exploration ); précédent : 005426; suivant : 005428Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry.
Auteurs : Graham Simmons [États-Unis] ; Jacqueline D. Reeves ; Andrew J. Rennekamp ; Sean M. Amberg ; Andrew J. Piefer ; Paul BatesSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.
Descripteurs français
- KwdFr :
- Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Protéines de capside (génétique), Protéines de capside (métabolisme), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Syndrome respiratoire aigu sévère (métabolisme), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de capside, Protéines de l'enveloppe virale, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de capside, Protéines de l'enveloppe virale, Syndrome respiratoire aigu sévère, Virus du SRAS.
- Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Humains.
English descriptors
- KwdEn :
- Capsid Proteins (genetics), Capsid Proteins (metabolism), Cell Fusion, Humans, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , genetics : Capsid Proteins, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Capsid Proteins, Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus, Severe Acute Respiratory Syndrome.
- Cell Fusion, Humans, Spike Glycoprotein, Coronavirus.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is a rapidly emerging pathogen with potentially serious consequences for public health. Here we describe conditions that result not only in the efficient expression of the SARS-CoV spike (S) protein on the surface of cells, but in its incorporation into lentiviral particles that can be used to transduce cells in an S glycoprotein-dependent manner. We found that although some primate cell lines, including Vero E6, 293T and Huh-7 cells, could be efficiently transduced by SARS-CoV S glycoprotein pseudoviruses, other cells lines were either resistant or very poorly permissive to virus entry. Infection by pseudovirions could be inhibited by several lysosomotropic agents, suggesting a requirement for acidification of endosomes for efficient S-mediated viral entry. In addition, we were able to develop a cell-cell fusion assay that could be used to monitor S glycoprotein-dependent membrane fusion. Although proteolysis did not enhance the infectivity of cell-free pseudovirions, trypsin activation is required for cell-cell fusion. Additionally, there was no apparent pH requirement for S glycoprotein-mediated cell-cell fusion. Together, these studies describe important tools that can be used to study SARS-CoV S glycoprotein structure and function, including approaches that can be used to identify inhibitors of the entry of SARS-CoV into target cells.
DOI: 10.1073/pnas.0306446101
PubMed: 15010527
Affiliations:
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Le document en format XML
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Reeves</name></author><author><name sortKey="Rennekamp, Andrew J" sort="Rennekamp, Andrew J" uniqKey="Rennekamp A" first="Andrew J" last="Rennekamp">Andrew J. Rennekamp</name></author><author><name sortKey="Amberg, Sean M" sort="Amberg, Sean M" uniqKey="Amberg S" first="Sean M" last="Amberg">Sean M. Amberg</name></author><author><name sortKey="Piefer, Andrew J" sort="Piefer, Andrew J" uniqKey="Piefer A" first="Andrew J" last="Piefer">Andrew J. Piefer</name></author><author><name sortKey="Bates, Paul" sort="Bates, Paul" uniqKey="Bates P" first="Paul" last="Bates">Paul Bates</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Capsid Proteins (genetics)</term><term>Capsid Proteins (metabolism)</term><term>Cell Fusion</term><term>Humans</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>Severe Acute Respiratory Syndrome (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Fusion cellulaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Protéines de capside (génétique)</term><term>Protéines de capside (métabolisme)</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Syndrome respiratoire aigu sévère (métabolisme)</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Capsid Proteins</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Capsid Proteins</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de capside</term><term>Protéines de l'enveloppe virale</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de capside</term><term>Protéines de l'enveloppe virale</term><term>Syndrome respiratoire aigu sévère</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Fusion</term><term>Humans</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Fusion cellulaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is a rapidly emerging pathogen with potentially serious consequences for public health. Here we describe conditions that result not only in the efficient expression of the SARS-CoV spike (S) protein on the surface of cells, but in its incorporation into lentiviral particles that can be used to transduce cells in an S glycoprotein-dependent manner. We found that although some primate cell lines, including Vero E6, 293T and Huh-7 cells, could be efficiently transduced by SARS-CoV S glycoprotein pseudoviruses, other cells lines were either resistant or very poorly permissive to virus entry. Infection by pseudovirions could be inhibited by several lysosomotropic agents, suggesting a requirement for acidification of endosomes for efficient S-mediated viral entry. In addition, we were able to develop a cell-cell fusion assay that could be used to monitor S glycoprotein-dependent membrane fusion. Although proteolysis did not enhance the infectivity of cell-free pseudovirions, trypsin activation is required for cell-cell fusion. Additionally, there was no apparent pH requirement for S glycoprotein-mediated cell-cell fusion. Together, these studies describe important tools that can be used to study SARS-CoV S glycoprotein structure and function, including approaches that can be used to identify inhibitors of the entry of SARS-CoV into target cells.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region></list><tree><noCountry><name sortKey="Amberg, Sean M" sort="Amberg, Sean M" uniqKey="Amberg S" first="Sean M" last="Amberg">Sean M. Amberg</name><name sortKey="Bates, Paul" sort="Bates, Paul" uniqKey="Bates P" first="Paul" last="Bates">Paul Bates</name><name sortKey="Piefer, Andrew J" sort="Piefer, Andrew J" uniqKey="Piefer A" first="Andrew J" last="Piefer">Andrew J. Piefer</name><name sortKey="Reeves, Jacqueline D" sort="Reeves, Jacqueline D" uniqKey="Reeves J" first="Jacqueline D" last="Reeves">Jacqueline D. Reeves</name><name sortKey="Rennekamp, Andrew J" sort="Rennekamp, Andrew J" uniqKey="Rennekamp A" first="Andrew J" last="Rennekamp">Andrew J. Rennekamp</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Simmons, Graham" sort="Simmons, Graham" uniqKey="Simmons G" first="Graham" last="Simmons">Graham Simmons</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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