Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.
Identifieur interne : 001F76 ( PubMed/Corpus ); précédent : 001F75; suivant : 001F77Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.
Auteurs : Chad M. Petit ; Vladimir N. Chouljenko ; Arun Iyer ; Robin Colgrove ; Michael Farzan ; David M. Knipe ; K G KousoulasSource :
- Virology [ 0042-6822 ] ; 2007.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Fusion, Cell Membrane (chemistry), Chlorocebus aethiops, Cysteine (genetics), Cysteine (physiology), Immunohistochemistry, Isotope Labeling, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Mutagenesis, Site-Directed, Palmitic Acid (analysis), Palmitic Acid (metabolism), Protein Processing, Post-Translational, SARS Virus (chemistry), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Tritium (metabolism), Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , analysis : Palmitic Acid.
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Cysteine, Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : Cell Membrane, SARS Virus.
- chemical , metabolism : Membrane Glycoproteins, Palmitic Acid, Tritium, Viral Envelope Proteins.
- chemical , physiology : Cysteine, SARS Virus.
- Amino Acid Sequence, Animals, Cell Fusion, Chlorocebus aethiops, Immunohistochemistry, Isotope Labeling, Membrane Fusion, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Processing, Post-Translational, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
The SARS-coronavirus (SARS-CoV) is the etiological agent of the severe acute respiratory syndrome (SARS). The SARS-CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. The cytoplasmic portion of the S glycoprotein contains four cysteine-rich amino acid clusters. Individual cysteine clusters were altered via cysteine-to-alanine amino acid replacement and the modified S glycoproteins were tested for their transport to cell-surfaces and ability to cause cell fusion in transient transfection assays. Mutagenesis of the cysteine cluster I, located immediately proximal to the predicted transmembrane, domain did not appreciably reduce cell-surface expression, although S-mediated cell fusion was reduced by more than 50% in comparison to the wild-type S. Similarly, mutagenesis of the cysteine cluster II located adjacent to cluster I reduced S-mediated cell fusion by more than 60% compared to the wild-type S, while cell-surface expression was reduced by less than 20%. Mutagenesis of cysteine clusters III and IV did not appreciably affect S cell-surface expression or S-mediated cell fusion. The wild-type S was palmitoylated as evidenced by the efficient incorporation of (3)H-palmitic acid in wild-type S molecules. S glycoprotein palmitoylation was significantly reduced for mutant glycoproteins having cluster I and II cysteine changes, but was largely unaffected for cysteine cluster III and IV mutants. These results show that the S cytoplasmic domain is palmitoylated and that palmitoylation of the membrane proximal cysteine clusters I and II may be important for S-mediated cell fusion.
DOI: 10.1016/j.virol.2006.10.034
PubMed: 17134730
Links to Exploration step
pubmed:17134730Le document en format XML
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Chouljenko</name></author><author><name sortKey="Iyer, Arun" sort="Iyer, Arun" uniqKey="Iyer A" first="Arun" last="Iyer">Arun Iyer</name></author><author><name sortKey="Colgrove, Robin" sort="Colgrove, Robin" uniqKey="Colgrove R" first="Robin" last="Colgrove">Robin Colgrove</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author><author><name sortKey="Knipe, David M" sort="Knipe, David M" uniqKey="Knipe D" first="David M" last="Knipe">David M. Knipe</name></author><author><name sortKey="Kousoulas, K G" sort="Kousoulas, K G" uniqKey="Kousoulas K" first="K G" last="Kousoulas">K G Kousoulas</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17134730</idno><idno type="pmid">17134730</idno><idno type="doi">10.1016/j.virol.2006.10.034</idno><idno type="wicri:Area/PubMed/Corpus">001F76</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001F76</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.</title><author><name sortKey="Petit, Chad M" sort="Petit, Chad M" uniqKey="Petit C" first="Chad M" last="Petit">Chad M. Petit</name><affiliation><nlm:affiliation>Division of Biotechnology and Molecular Medicine (BIOMMED), USA.</nlm:affiliation></affiliation></author><author><name sortKey="Chouljenko, Vladimir N" sort="Chouljenko, Vladimir N" uniqKey="Chouljenko V" first="Vladimir N" last="Chouljenko">Vladimir N. Chouljenko</name></author><author><name sortKey="Iyer, Arun" sort="Iyer, Arun" uniqKey="Iyer A" first="Arun" last="Iyer">Arun Iyer</name></author><author><name sortKey="Colgrove, Robin" sort="Colgrove, Robin" uniqKey="Colgrove R" first="Robin" last="Colgrove">Robin Colgrove</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author><author><name sortKey="Knipe, David M" sort="Knipe, David M" uniqKey="Knipe D" first="David M" last="Knipe">David M. Knipe</name></author><author><name sortKey="Kousoulas, K G" sort="Kousoulas, K G" uniqKey="Kousoulas K" first="K G" last="Kousoulas">K G Kousoulas</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Fusion</term><term>Cell Membrane (chemistry)</term><term>Chlorocebus aethiops</term><term>Cysteine (genetics)</term><term>Cysteine (physiology)</term><term>Immunohistochemistry</term><term>Isotope Labeling</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Palmitic Acid (analysis)</term><term>Palmitic Acid (metabolism)</term><term>Protein Processing, Post-Translational</term><term>SARS Virus (chemistry)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Tritium (metabolism)</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Palmitic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Palmitic Acid</term><term>Tritium</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Cysteine</term><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Fusion</term><term>Chlorocebus aethiops</term><term>Immunohistochemistry</term><term>Isotope Labeling</term><term>Membrane Fusion</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Protein Processing, Post-Translational</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) is the etiological agent of the severe acute respiratory syndrome (SARS). The SARS-CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. The cytoplasmic portion of the S glycoprotein contains four cysteine-rich amino acid clusters. Individual cysteine clusters were altered via cysteine-to-alanine amino acid replacement and the modified S glycoproteins were tested for their transport to cell-surfaces and ability to cause cell fusion in transient transfection assays. Mutagenesis of the cysteine cluster I, located immediately proximal to the predicted transmembrane, domain did not appreciably reduce cell-surface expression, although S-mediated cell fusion was reduced by more than 50% in comparison to the wild-type S. Similarly, mutagenesis of the cysteine cluster II located adjacent to cluster I reduced S-mediated cell fusion by more than 60% compared to the wild-type S, while cell-surface expression was reduced by less than 20%. Mutagenesis of cysteine clusters III and IV did not appreciably affect S cell-surface expression or S-mediated cell fusion. The wild-type S was palmitoylated as evidenced by the efficient incorporation of (3)H-palmitic acid in wild-type S molecules. S glycoprotein palmitoylation was significantly reduced for mutant glycoproteins having cluster I and II cysteine changes, but was largely unaffected for cysteine cluster III and IV mutants. These results show that the S cytoplasmic domain is palmitoylated and that palmitoylation of the membrane proximal cysteine clusters I and II may be important for S-mediated cell fusion.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17134730</PMID><DateCompleted><Year>2007</Year><Month>06</Month><Day>07</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0042-6822</ISSN><JournalIssue CitedMedium="Print"><Volume>360</Volume><Issue>2</Issue><PubDate><Year>2007</Year><Month>Apr</Month><Day>10</Day></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.</ArticleTitle><Pagination><MedlinePgn>264-74</MedlinePgn></Pagination><Abstract><AbstractText>The SARS-coronavirus (SARS-CoV) is the etiological agent of the severe acute respiratory syndrome (SARS). The SARS-CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. The cytoplasmic portion of the S glycoprotein contains four cysteine-rich amino acid clusters. Individual cysteine clusters were altered via cysteine-to-alanine amino acid replacement and the modified S glycoproteins were tested for their transport to cell-surfaces and ability to cause cell fusion in transient transfection assays. Mutagenesis of the cysteine cluster I, located immediately proximal to the predicted transmembrane, domain did not appreciably reduce cell-surface expression, although S-mediated cell fusion was reduced by more than 50% in comparison to the wild-type S. Similarly, mutagenesis of the cysteine cluster II located adjacent to cluster I reduced S-mediated cell fusion by more than 60% compared to the wild-type S, while cell-surface expression was reduced by less than 20%. Mutagenesis of cysteine clusters III and IV did not appreciably affect S cell-surface expression or S-mediated cell fusion. The wild-type S was palmitoylated as evidenced by the efficient incorporation of (3)H-palmitic acid in wild-type S molecules. S glycoprotein palmitoylation was significantly reduced for mutant glycoproteins having cluster I and II cysteine changes, but was largely unaffected for cysteine cluster III and IV mutants. These results show that the S cytoplasmic domain is palmitoylated and that palmitoylation of the membrane proximal cysteine clusters I and II may be important for S-mediated cell fusion.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Petit</LastName><ForeName>Chad M</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>Division of Biotechnology and Molecular Medicine (BIOMMED), USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chouljenko</LastName><ForeName>Vladimir N</ForeName><Initials>VN</Initials></Author><Author ValidYN="Y"><LastName>Iyer</LastName><ForeName>Arun</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Colgrove</LastName><ForeName>Robin</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Farzan</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Knipe</LastName><ForeName>David M</ForeName><Initials>DM</Initials></Author><Author ValidYN="Y"><LastName>Kousoulas</LastName><ForeName>K G</ForeName><Initials>KG</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>11</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</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>10028-17-8</RegistryNumber><NameOfSubstance UI="D014316">Tritium</NameOfSubstance></Chemical><Chemical><RegistryNumber>2V16EO95H1</RegistryNumber><NameOfSubstance UI="D019308">Palmitic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002459" MajorTopicYN="Y">Cell Fusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell 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MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019308" MajorTopicYN="N">Palmitic Acid</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="Y">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014316" MajorTopicYN="N">Tritium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></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="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>06</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>08</Month><Day>14</Day></PubMedPubDate><PubMedPubDate 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