Importance of SARS-CoV spike protein Trp-rich region in viral infectivity.
Identifieur interne : 001B63 ( PubMed/Corpus ); précédent : 001B62; suivant : 001B64Importance of SARS-CoV spike protein Trp-rich region in viral infectivity.
Auteurs : Yanning Lu ; Tuan Ling Neo ; Ding Xiang Liu ; James P. TamSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2008.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Animals, Chlorocebus aethiops, Conserved Sequence, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Molecular Sequence Data, Mutation, SARS Virus (genetics), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Tryptophan (chemistry), Tryptophan (genetics), Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Virus Internalization.
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Tryptophan, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Tryptophan, Viral Envelope Proteins.
- genetics : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Animals, Chlorocebus aethiops, Conserved Sequence, Humans, Molecular Sequence Data, Mutation, Spike Glycoprotein, Coronavirus, Vero Cells, Virus Internalization.
Abstract
SARS-CoV entry is mediated by spike glycoprotein. During the viral and host cellular membrane fusion, HR1 and HR2 form 6-helix bundle, positioning the fusion peptide closely to the C-terminal region of ectodomain to drive apposition and subsequent membrane fusion. Connecting to the HR2 region is a Trp-rich region which is absolutely conserved in members of coronaviruses. To investigate the importance of Trp-rich region in SARS-CoV entry, we produced different mutated S proteins using Alanine scan strategy. SARS-CoV pseudotyped with mutated S protein was used to measure viral infectivity. To restore the aromaticity of Ala-mutants, we performed rescue experiments using phenylalanine substitutions. Our results show that individually substituted Ala-mutants substantially decrease infectivity by >90%, global Ala-mutants totally abrogated infectivity. In contrast, Phe-substituted mutants are able to restore 10-25% infectivity comparing to the wild-type. The results suggest that the Trp-rich region of S protein is essential for SARS-CoV infectivity.
DOI: 10.1016/j.bbrc.2008.04.044
PubMed: 18424264
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pubmed:18424264Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Importance of SARS-CoV spike protein Trp-rich region in viral infectivity.</title><author><name sortKey="Lu, Yanning" sort="Lu, Yanning" uniqKey="Lu Y" first="Yanning" last="Lu">Yanning Lu</name><affiliation><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</nlm:affiliation></affiliation></author><author><name sortKey="Neo, Tuan Ling" sort="Neo, Tuan Ling" uniqKey="Neo T" first="Tuan Ling" last="Neo">Tuan Ling Neo</name></author><author><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name></author><author><name sortKey="Tam, James P" sort="Tam, James P" uniqKey="Tam J" first="James P" last="Tam">James P. Tam</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18424264</idno><idno type="pmid">18424264</idno><idno type="doi">10.1016/j.bbrc.2008.04.044</idno><idno type="wicri:Area/PubMed/Corpus">001B63</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001B63</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Importance of SARS-CoV spike protein Trp-rich region in viral infectivity.</title><author><name sortKey="Lu, Yanning" sort="Lu, Yanning" uniqKey="Lu Y" first="Yanning" last="Lu">Yanning Lu</name><affiliation><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</nlm:affiliation></affiliation></author><author><name sortKey="Neo, Tuan Ling" sort="Neo, Tuan Ling" uniqKey="Neo T" first="Tuan Ling" last="Neo">Tuan Ling Neo</name></author><author><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name></author><author><name sortKey="Tam, James P" sort="Tam, James P" uniqKey="Tam J" first="James P" last="Tam">James P. Tam</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Chlorocebus aethiops</term><term>Conserved Sequence</term><term>Humans</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Molecular Sequence Data</term><term>Mutation</term><term>SARS Virus (genetics)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Tryptophan (chemistry)</term><term>Tryptophan (genetics)</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Tryptophan</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Tryptophan</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Chlorocebus aethiops</term><term>Conserved Sequence</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Virus Internalization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">SARS-CoV entry is mediated by spike glycoprotein. During the viral and host cellular membrane fusion, HR1 and HR2 form 6-helix bundle, positioning the fusion peptide closely to the C-terminal region of ectodomain to drive apposition and subsequent membrane fusion. Connecting to the HR2 region is a Trp-rich region which is absolutely conserved in members of coronaviruses. To investigate the importance of Trp-rich region in SARS-CoV entry, we produced different mutated S proteins using Alanine scan strategy. SARS-CoV pseudotyped with mutated S protein was used to measure viral infectivity. To restore the aromaticity of Ala-mutants, we performed rescue experiments using phenylalanine substitutions. Our results show that individually substituted Ala-mutants substantially decrease infectivity by >90%, global Ala-mutants totally abrogated infectivity. In contrast, Phe-substituted mutants are able to restore 10-25% infectivity comparing to the wild-type. The results suggest that the Trp-rich region of S protein is essential for SARS-CoV infectivity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18424264</PMID><DateCompleted><Year>2008</Year><Month>07</Month><Day>03</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>371</Volume><Issue>3</Issue><PubDate><Year>2008</Year><Month>Jul</Month><Day>04</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>Importance of SARS-CoV spike protein Trp-rich region in viral infectivity.</ArticleTitle><Pagination><MedlinePgn>356-60</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2008.04.044</ELocationID><Abstract><AbstractText>SARS-CoV entry is mediated by spike glycoprotein. During the viral and host cellular membrane fusion, HR1 and HR2 form 6-helix bundle, positioning the fusion peptide closely to the C-terminal region of ectodomain to drive apposition and subsequent membrane fusion. Connecting to the HR2 region is a Trp-rich region which is absolutely conserved in members of coronaviruses. To investigate the importance of Trp-rich region in SARS-CoV entry, we produced different mutated S proteins using Alanine scan strategy. SARS-CoV pseudotyped with mutated S protein was used to measure viral infectivity. To restore the aromaticity of Ala-mutants, we performed rescue experiments using phenylalanine substitutions. Our results show that individually substituted Ala-mutants substantially decrease infectivity by >90%, global Ala-mutants totally abrogated infectivity. In contrast, Phe-substituted mutants are able to restore 10-25% infectivity comparing to the wild-type. The results suggest that the Trp-rich region of S protein is essential for SARS-CoV infectivity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Yanning</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Neo</LastName><ForeName>Tuan Ling</ForeName><Initials>TL</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Ding Xiang</ForeName><Initials>DX</Initials></Author><Author ValidYN="Y"><LastName>Tam</LastName><ForeName>James P</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 EB001986-21</GrantID><Acronym>EB</Acronym><Agency>NIBIB NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>04</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</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>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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