Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Identifieur interne : 001937 ( PubMed/Corpus ); précédent : 001936; suivant : 001938Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Auteurs : Sandrine Belouzard ; Victor C. Chu ; Gary R. WhittakerSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2009.
English descriptors
- KwdEn :
- Binding Sites, Cell Fusion, Furin, Hydrolysis, Membrane Glycoproteins (metabolism), Membrane Glycoproteins (physiology), Mutagenesis, Site-Directed, SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus, Trypsin (metabolism), Viral Envelope Proteins (metabolism), Viral Envelope Proteins (physiology), Virus Internalization.
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Trypsin, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical : Furin, Spike Glycoprotein, Coronavirus.
- pathogenicity : SARS Virus.
- Binding Sites, Cell Fusion, Hydrolysis, Mutagenesis, Site-Directed, Virus Internalization.
Abstract
The coronavirus spike protein (S) plays a key role in the early steps of viral infection, with the S1 domain responsible for receptor binding and the S2 domain mediating membrane fusion. In some cases, the S protein is proteolytically cleaved at the S1-S2 boundary. In the case of the severe acute respiratory syndrome coronavirus (SARS-CoV), it has been shown that virus entry requires the endosomal protease cathepsin L; however, it was also found that infection of SARS-CoV could be strongly induced by trypsin treatment. Overall, in terms of how cleavage might activate membrane fusion, proteolytic processing of the SARS-CoV S protein remains unclear. Here, we identify a proteolytic cleavage site within the SARS-CoV S2 domain (S2', R797). Mutation of R797 specifically inhibited trypsin-dependent fusion in both cell-cell fusion and pseudovirion entry assays. We also introduced a furin cleavage site at both the S2' cleavage site within S2 793-KPTKR-797 (S2'), as well as at the junction of S1 and S2. Introduction of a furin cleavage site at the S2' position allowed trypsin-independent cell-cell fusion, which was strongly increased by the presence of a second furin cleavage site at the S1-S2 position. Taken together, these data suggest a novel priming mechanism for a viral fusion protein, with a critical proteolytic cleavage event on the SARS-CoV S protein at position 797 (S2'), acting in concert with the S1-S2 cleavage site to mediate membrane fusion and virus infectivity.
DOI: 10.1073/pnas.0809524106
PubMed: 19321428
Links to Exploration step
pubmed:19321428Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.</title><author><name sortKey="Belouzard, Sandrine" sort="Belouzard, Sandrine" uniqKey="Belouzard S" first="Sandrine" last="Belouzard">Sandrine Belouzard</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Chu, Victor C" sort="Chu, Victor C" uniqKey="Chu V" first="Victor C" last="Chu">Victor C. Chu</name></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R" last="Whittaker">Gary R. Whittaker</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19321428</idno><idno type="pmid">19321428</idno><idno type="doi">10.1073/pnas.0809524106</idno><idno type="wicri:Area/PubMed/Corpus">001937</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001937</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.</title><author><name sortKey="Belouzard, Sandrine" sort="Belouzard, Sandrine" uniqKey="Belouzard S" first="Sandrine" last="Belouzard">Sandrine Belouzard</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Chu, Victor C" sort="Chu, Victor C" uniqKey="Chu V" first="Victor C" last="Chu">Victor C. Chu</name></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R" last="Whittaker">Gary R. Whittaker</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Cell Fusion</term><term>Furin</term><term>Hydrolysis</term><term>Membrane Glycoproteins (metabolism)</term><term>Membrane Glycoproteins (physiology)</term><term>Mutagenesis, Site-Directed</term><term>SARS Virus (pathogenicity)</term><term>Spike Glycoprotein, Coronavirus</term><term>Trypsin (metabolism)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Envelope Proteins (physiology)</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Trypsin</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Furin</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Cell Fusion</term><term>Hydrolysis</term><term>Mutagenesis, Site-Directed</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus spike protein (S) plays a key role in the early steps of viral infection, with the S1 domain responsible for receptor binding and the S2 domain mediating membrane fusion. In some cases, the S protein is proteolytically cleaved at the S1-S2 boundary. In the case of the severe acute respiratory syndrome coronavirus (SARS-CoV), it has been shown that virus entry requires the endosomal protease cathepsin L; however, it was also found that infection of SARS-CoV could be strongly induced by trypsin treatment. Overall, in terms of how cleavage might activate membrane fusion, proteolytic processing of the SARS-CoV S protein remains unclear. Here, we identify a proteolytic cleavage site within the SARS-CoV S2 domain (S2', R797). Mutation of R797 specifically inhibited trypsin-dependent fusion in both cell-cell fusion and pseudovirion entry assays. We also introduced a furin cleavage site at both the S2' cleavage site within S2 793-KPTKR-797 (S2'), as well as at the junction of S1 and S2. Introduction of a furin cleavage site at the S2' position allowed trypsin-independent cell-cell fusion, which was strongly increased by the presence of a second furin cleavage site at the S1-S2 position. Taken together, these data suggest a novel priming mechanism for a viral fusion protein, with a critical proteolytic cleavage event on the SARS-CoV S protein at position 797 (S2'), acting in concert with the S1-S2 cleavage site to mediate membrane fusion and virus infectivity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19321428</PMID><DateCompleted><Year>2009</Year><Month>05</Month><Day>06</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>106</Volume><Issue>14</Issue><PubDate><Year>2009</Year><Month>Apr</Month><Day>07</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.</ArticleTitle><Pagination><MedlinePgn>5871-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.0809524106</ELocationID><Abstract><AbstractText>The coronavirus spike protein (S) plays a key role in the early steps of viral infection, with the S1 domain responsible for receptor binding and the S2 domain mediating membrane fusion. In some cases, the S protein is proteolytically cleaved at the S1-S2 boundary. In the case of the severe acute respiratory syndrome coronavirus (SARS-CoV), it has been shown that virus entry requires the endosomal protease cathepsin L; however, it was also found that infection of SARS-CoV could be strongly induced by trypsin treatment. Overall, in terms of how cleavage might activate membrane fusion, proteolytic processing of the SARS-CoV S protein remains unclear. Here, we identify a proteolytic cleavage site within the SARS-CoV S2 domain (S2', R797). Mutation of R797 specifically inhibited trypsin-dependent fusion in both cell-cell fusion and pseudovirion entry assays. We also introduced a furin cleavage site at both the S2' cleavage site within S2 793-KPTKR-797 (S2'), as well as at the junction of S1 and S2. Introduction of a furin cleavage site at the S2' position allowed trypsin-independent cell-cell fusion, which was strongly increased by the presence of a second furin cleavage site at the S1-S2 position. Taken together, these data suggest a novel priming mechanism for a viral fusion protein, with a critical proteolytic cleavage event on the SARS-CoV S protein at position 797 (S2'), acting in concert with the S1-S2 cleavage site to mediate membrane fusion and virus infectivity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Belouzard</LastName><ForeName>Sandrine</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chu</LastName><ForeName>Victor C</ForeName><Initials>VC</Initials></Author><Author ValidYN="Y"><LastName>Whittaker</LastName><ForeName>Gary R</ForeName><Initials>GR</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R03 AI060946</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>03</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><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 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.75</RegistryNumber><NameOfSubstance UI="D045683">Furin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002459" MajorTopicYN="N">Cell Fusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045683" MajorTopicYN="N">Furin</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" 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