GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry.
Identifieur interne : 001E13 ( PubMed/Corpus ); précédent : 001E12; suivant : 001E14GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry.
Auteurs : Jeroen Corver ; Rene Broer ; Puck Van Kasteren ; Willy SpaanSource :
- Journal of virology [ 0022-538X ] ; 2007.
English descriptors
- KwdEn :
- Amino Acid Motifs, Animals, Cells, Cultured, Humans, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Molecular Sequence Data, Protein Structure, Quaternary, SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Severe Acute Respiratory Syndrome, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Internalization.
- MESH :
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Motifs, Animals, Cells, Cultured, Humans, Mice, Molecular Sequence Data, Protein Structure, Quaternary, Sequence Alignment, Severe Acute Respiratory Syndrome, Spike Glycoprotein, Coronavirus, Virus Internalization.
Abstract
Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.
DOI: 10.1128/JVI.00014-07
PubMed: 17507478
Links to Exploration step
pubmed:17507478Le document en format XML
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Box 9600, 2300 RC Leiden, The Netherlands. j.corver@lumc.nl</nlm:affiliation></affiliation></author><author><name sortKey="Broer, Rene" sort="Broer, Rene" uniqKey="Broer R" first="Rene" last="Broer">Rene Broer</name></author><author><name sortKey="Van Kasteren, Puck" sort="Van Kasteren, Puck" uniqKey="Van Kasteren P" first="Puck" last="Van Kasteren">Puck Van Kasteren</name></author><author><name sortKey="Spaan, Willy" sort="Spaan, Willy" uniqKey="Spaan W" first="Willy" last="Spaan">Willy Spaan</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17507478</idno><idno type="pmid">17507478</idno><idno type="doi">10.1128/JVI.00014-07</idno><idno type="wicri:Area/PubMed/Corpus">001E13</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001E13</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry.</title><author><name sortKey="Corver, Jeroen" sort="Corver, Jeroen" uniqKey="Corver J" first="Jeroen" last="Corver">Jeroen Corver</name><affiliation><nlm:affiliation>Department of Medical Microbiology, Leiden University Medical Center, E4-P, P.O. Box 9600, 2300 RC Leiden, The Netherlands. j.corver@lumc.nl</nlm:affiliation></affiliation></author><author><name sortKey="Broer, Rene" sort="Broer, Rene" uniqKey="Broer R" first="Rene" last="Broer">Rene Broer</name></author><author><name sortKey="Van Kasteren, Puck" sort="Van Kasteren, Puck" uniqKey="Van Kasteren P" first="Puck" last="Van Kasteren">Puck Van Kasteren</name></author><author><name sortKey="Spaan, Willy" sort="Spaan, Willy" uniqKey="Spaan W" first="Willy" last="Spaan">Willy Spaan</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</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 Motifs</term><term>Animals</term><term>Cells, Cultured</term><term>Humans</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Molecular Sequence Data</term><term>Protein Structure, Quaternary</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>Sequence Alignment</term><term>Severe Acute Respiratory Syndrome</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><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="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Animals</term><term>Cells, Cultured</term><term>Humans</term><term>Mice</term><term>Molecular Sequence Data</term><term>Protein Structure, Quaternary</term><term>Sequence Alignment</term><term>Severe Acute Respiratory Syndrome</term><term>Spike Glycoprotein, Coronavirus</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17507478</PMID><DateCompleted><Year>2007</Year><Month>09</Month><Day>26</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>81</Volume><Issue>15</Issue><PubDate><Year>2007</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry.</ArticleTitle><Pagination><MedlinePgn>8352-5</MedlinePgn></Pagination><Abstract><AbstractText>Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Corver</LastName><ForeName>Jeroen</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Medical Microbiology, Leiden University Medical Center, E4-P, P.O. Box 9600, 2300 RC Leiden, The Netherlands. j.corver@lumc.nl</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Broer</LastName><ForeName>Rene</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>van Kasteren</LastName><ForeName>Puck</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Spaan</LastName><ForeName>Willy</ForeName><Initials>W</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>05</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="Y">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="Y">Severe Acute Respiratory Syndrome</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="Y">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053586" MajorTopicYN="Y">Virus Internalization</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>5</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>9</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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