Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.
Identifieur interne : 000A94 ( PubMed/Corpus ); précédent : 000A93; suivant : 000A95Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.
Auteurs : Yusuke Sakai ; Kengo Kawachi ; Yutaka Terada ; Hiroko Omori ; Yoshiharu Matsuura ; Wataru KamitaniSource :
- Virology [ 1096-0341 ] ; 2017.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Viral Nonstructural Proteins.
- genetics : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Substitution, DNA Mutational Analysis, Protein Interaction Mapping, Virus Replication.
Abstract
Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.
DOI: 10.1016/j.virol.2017.07.019
PubMed: 28738245
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Electronic address: wakamita@biken.osaka-u.ac.jp.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28738245</idno><idno type="pmid">28738245</idno><idno type="doi">10.1016/j.virol.2017.07.019</idno><idno type="wicri:Area/PubMed/Corpus">000A94</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A94</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.</title><author><name sortKey="Sakai, Yusuke" sort="Sakai, Yusuke" uniqKey="Sakai Y" first="Yusuke" last="Sakai">Yusuke Sakai</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan; Laboratory of Veterinary Pathology, Joint Faculty of Veterinary Medicine, Yamaguchi University, Yamaguchi, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kawachi, Kengo" sort="Kawachi, Kengo" uniqKey="Kawachi K" first="Kengo" last="Kawachi">Kengo Kawachi</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan; Department of Molecular Virology, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Terada, Yutaka" sort="Terada, Yutaka" uniqKey="Terada Y" first="Yutaka" last="Terada">Yutaka Terada</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Omori, Hiroko" sort="Omori, Hiroko" uniqKey="Omori H" first="Hiroko" last="Omori">Hiroko Omori</name><affiliation><nlm:affiliation>Core Instrumentation Facility, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Matsuura, Yoshiharu" sort="Matsuura, Yoshiharu" uniqKey="Matsuura Y" first="Yoshiharu" last="Matsuura">Yoshiharu Matsuura</name><affiliation><nlm:affiliation>Department of Molecular Virology, Osaka, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kamitani, Wataru" sort="Kamitani, Wataru" uniqKey="Kamitani W" first="Wataru" last="Kamitani">Wataru Kamitani</name><affiliation><nlm:affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan; Tsukuba Primate Research Center, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan. Electronic address: wakamita@biken.osaka-u.ac.jp.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Virology</title><idno type="eISSN">1096-0341</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>DNA Mutational Analysis</term><term>Protein Interaction Mapping</term><term>SARS Virus (genetics)</term><term>SARS Virus (physiology)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Virus Replication</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Viral Nonstructural 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 Substitution</term><term>DNA Mutational Analysis</term><term>Protein Interaction Mapping</term><term>Virus Replication</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28738245</PMID><DateCompleted><Year>2017</Year><Month>08</Month><Day>29</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0341</ISSN><JournalIssue CitedMedium="Internet"><Volume>510</Volume><PubDate><Year>2017</Year><Month>10</Month></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.</ArticleTitle><Pagination><MedlinePgn>165-174</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0042-6822(17)30238-6</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virol.2017.07.019</ELocationID><Abstract><AbstractText>Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sakai</LastName><ForeName>Yusuke</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan; Laboratory of Veterinary Pathology, Joint Faculty of Veterinary Medicine, Yamaguchi University, Yamaguchi, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kawachi</LastName><ForeName>Kengo</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan; Department of Molecular Virology, Osaka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Terada</LastName><ForeName>Yutaka</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Omori</LastName><ForeName>Hiroko</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Core Instrumentation Facility, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsuura</LastName><ForeName>Yoshiharu</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Molecular Virology, Osaka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kamitani</LastName><ForeName>Wataru</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan; Tsukuba Primate Research Center, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan. Electronic address: wakamita@biken.osaka-u.ac.jp.</Affiliation></AffiliationInfo></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>2017</Year><Month>07</Month><Day>21</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="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="Y">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004252" MajorTopicYN="N">DNA Mutational Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025941" MajorTopicYN="N">Protein Interaction Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014779" MajorTopicYN="Y">Virus Replication</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Coronavirus</Keyword><Keyword MajorTopicYN="Y">Nsp4</Keyword><Keyword MajorTopicYN="Y">Severe acute respiratory syndrome</Keyword><Keyword MajorTopicYN="Y">Viral 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