Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion.
Identifieur interne : 003743 ( Main/Exploration ); précédent : 003742; suivant : 003744Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion.
Auteurs : Daniel R. Beniac [Canada] ; Shauna L. Devarennes ; Anton Andonov ; Runtao He ; Tim F. BoothSource :
- PloS one [ 1932-6203 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux, Cellules Vero, Conformation des protéines, Conformation moléculaire, Cryomicroscopie électronique, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Humains, Liaison aux protéines, Microscopie immunoélectronique, Modèles moléculaires, Peptidyl-Dipeptidase A (), Protéines de l'enveloppe virale (), Traitement d'image par ordinateur, Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Virus du SRAS.
- Animaux, Cellules Vero, Conformation des protéines, Conformation moléculaire, Cryomicroscopie électronique, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Microscopie immunoélectronique, Modèles moléculaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Traitement d'image par ordinateur.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, Cryoelectron Microscopy, Humans, Image Processing, Computer-Assisted, Membrane Fusion, Membrane Glycoproteins (chemistry), Microscopy, Immunoelectron, Models, Molecular, Molecular Conformation, Peptidyl-Dipeptidase A (chemistry), Protein Binding, Protein Conformation, SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Viral Envelope Proteins.
- metabolism : SARS Virus.
- Animals, Chlorocebus aethiops, Cryoelectron Microscopy, Humans, Image Processing, Computer-Assisted, Membrane Fusion, Microscopy, Immunoelectron, Models, Molecular, Molecular Conformation, Protein Binding, Protein Conformation, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
The SARS coronavirus (SARS-CoV) spike is the largest known viral spike molecule, and shares a similar function with all class 1 viral fusion proteins. Previous structural studies of membrane fusion proteins have largely used crystallography of static molecular fragments, in isolation of their transmembrane domains. In this study we have produced purified, irradiated SARS-CoV virions that retain their morphology, and are fusogenic in cell culture. We used cryo-electron microscopy and image processing to investigate conformational changes that occur in the entire spike of intact virions when they bind to the viral receptor, angiotensin-converting enzyme 2 (ACE2). We have shown that ACE2 binding results in structural changes that appear to be the initial step in viral membrane fusion, and precisely localized the receptor-binding and fusion core domains within the entire spike. Furthermore, our results show that receptor binding and subsequent membrane fusion are distinct steps, and that each spike can bind up to three ACE2 molecules. The SARS-CoV spike provides an ideal model system to study receptor binding and membrane fusion in the native state, employing cryo-electron microscopy and single-particle image analysis.
DOI: 10.1371/journal.pone.0001082
PubMed: 17957264
Affiliations:
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Devarennes</name></author><author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name></author><author><name sortKey="He, Runtao" sort="He, Runtao" uniqKey="He R" first="Runtao" last="He">Runtao He</name></author><author><name sortKey="Booth, Tim F" sort="Booth, Tim F" uniqKey="Booth T" first="Tim F" last="Booth">Tim F. 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Beniac</name><affiliation wicri:level="1"><nlm:affiliation>Viral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Viral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba</wicri:regionArea><wicri:noRegion>Manitoba</wicri:noRegion></affiliation></author><author><name sortKey="Devarennes, Shauna L" sort="Devarennes, Shauna L" uniqKey="Devarennes S" first="Shauna L" last="Devarennes">Shauna L. Devarennes</name></author><author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name></author><author><name sortKey="He, Runtao" sort="He, Runtao" uniqKey="He R" first="Runtao" last="He">Runtao He</name></author><author><name sortKey="Booth, Tim F" sort="Booth, Tim F" uniqKey="Booth T" first="Tim F" last="Booth">Tim F. Booth</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Cryoelectron Microscopy</term><term>Humans</term><term>Image Processing, Computer-Assisted</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (chemistry)</term><term>Microscopy, Immunoelectron</term><term>Models, Molecular</term><term>Molecular Conformation</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Protein Binding</term><term>Protein Conformation</term><term>SARS Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Conformation des protéines</term><term>Conformation moléculaire</term><term>Cryomicroscopie électronique</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Humains</term><term>Liaison aux protéines</term><term>Microscopie immunoélectronique</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A ()</term><term>Protéines de l'enveloppe virale ()</term><term>Traitement d'image par ordinateur</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Cryoelectron Microscopy</term><term>Humans</term><term>Image Processing, Computer-Assisted</term><term>Membrane Fusion</term><term>Microscopy, Immunoelectron</term><term>Models, Molecular</term><term>Molecular Conformation</term><term>Protein Binding</term><term>Protein Conformation</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Conformation des protéines</term><term>Conformation moléculaire</term><term>Cryomicroscopie électronique</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Liaison aux protéines</term><term>Microscopie immunoélectronique</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Traitement d'image par ordinateur</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The SARS coronavirus (SARS-CoV) spike is the largest known viral spike molecule, and shares a similar function with all class 1 viral fusion proteins. Previous structural studies of membrane fusion proteins have largely used crystallography of static molecular fragments, in isolation of their transmembrane domains. In this study we have produced purified, irradiated SARS-CoV virions that retain their morphology, and are fusogenic in cell culture. We used cryo-electron microscopy and image processing to investigate conformational changes that occur in the entire spike of intact virions when they bind to the viral receptor, angiotensin-converting enzyme 2 (ACE2). We have shown that ACE2 binding results in structural changes that appear to be the initial step in viral membrane fusion, and precisely localized the receptor-binding and fusion core domains within the entire spike. Furthermore, our results show that receptor binding and subsequent membrane fusion are distinct steps, and that each spike can bind up to three ACE2 molecules. The SARS-CoV spike provides an ideal model system to study receptor binding and membrane fusion in the native state, employing cryo-electron microscopy and single-particle image analysis.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name><name sortKey="Booth, Tim F" sort="Booth, Tim F" uniqKey="Booth T" first="Tim F" last="Booth">Tim F. Booth</name><name sortKey="Devarennes, Shauna L" sort="Devarennes, Shauna L" uniqKey="Devarennes S" first="Shauna L" last="Devarennes">Shauna L. Devarennes</name><name sortKey="He, Runtao" sort="He, Runtao" uniqKey="He R" first="Runtao" last="He">Runtao He</name></noCountry><country name="Canada"><noRegion><name sortKey="Beniac, Daniel R" sort="Beniac, Daniel R" uniqKey="Beniac D" first="Daniel R" last="Beniac">Daniel R. 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