Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion.
Identifieur interne : 001C94 ( PubMed/Corpus ); précédent : 001C93; suivant : 001C95Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion.
Auteurs : Daniel R. Beniac ; Shauna L. Devarennes ; Anton Andonov ; Runtao He ; Tim F. BoothSource :
- PloS one [ 1932-6203 ] ; 2007.
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
Links to Exploration step
pubmed:17957264Le document en format XML
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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. Booth</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17957264</idno><idno type="pmid">17957264</idno><idno type="doi">10.1371/journal.pone.0001082</idno><idno type="wicri:Area/PubMed/Corpus">001C94</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001C94</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion.</title><author><name sortKey="Beniac, Daniel R" sort="Beniac, Daniel R" uniqKey="Beniac D" first="Daniel R" last="Beniac">Daniel R. Beniac</name><affiliation><nlm:affiliation>Viral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.</nlm:affiliation></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="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" 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></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17957264</PMID><DateCompleted><Year>2008</Year><Month>07</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>2</Volume><Issue>10</Issue><PubDate><Year>2007</Year><Month>Oct</Month><Day>24</Day></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion.</ArticleTitle><Pagination><MedlinePgn>e1082</MedlinePgn></Pagination><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Beniac</LastName><ForeName>Daniel R</ForeName><Initials>DR</Initials><AffiliationInfo><Affiliation>Viral Diseases Division, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Manitoba, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>deVarennes</LastName><ForeName>Shauna L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Andonov</LastName><ForeName>Anton</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>He</LastName><ForeName>Runtao</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Booth</LastName><ForeName>Tim F</ForeName><Initials>TF</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>10</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber><NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020285" MajorTopicYN="N">Cryoelectron Microscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007091" MajorTopicYN="N">Image Processing, Computer-Assisted</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008561" MajorTopicYN="N">Membrane Fusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016253" MajorTopicYN="N">Microscopy, Immunoelectron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008968" MajorTopicYN="N">Molecular Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2007</Year><Month>07</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>10</Month><Day>05</Day></PubMedPubDate><PubMedPubDate 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