Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation.
Identifieur interne : 000080 ( Main/Exploration ); précédent : 000079; suivant : 000081Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation.
Auteurs : Christopher P. Lapointe [États-Unis] ; Rosslyn Grosely [États-Unis] ; Alex G. Johnson [États-Unis] ; Jinfan Wang [États-Unis] ; Israel S. Fernández [États-Unis] ; Joseph D. Puglisi [États-Unis]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2021.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a beta-CoV that recently emerged as a human pathogen and is the causative agent of the COVID-19 pandemic. A molecular framework of how the virus manipulates host cellular machinery to facilitate infection remains unclear. Here, we focus on SARS-CoV-2 NSP1, which is proposed to be a virulence factor that inhibits protein synthesis by directly binding the human ribosome. We demonstrate biochemically that NSP1 inhibits translation of model human and SARS-CoV-2 messenger RNAs (mRNAs). NSP1 specifically binds to the small (40S) ribosomal subunit, which is required for translation inhibition. Using single-molecule fluorescence assays to monitor NSP1-40S subunit binding in real time, we determine that eukaryotic translation initiation factors (eIFs) allosterically modulate the interaction of NSP1 with ribosomal preinitiation complexes in the absence of mRNA. We further elucidate that NSP1 competes with RNA segments downstream of the start codon to bind the 40S subunit and that the protein is unable to associate rapidly with 80S ribosomes assembled on an mRNA. Collectively, our findings support a model where NSP1 proteins from viruses in at least two subgenera of beta-CoVs associate with the open head conformation of the 40S subunit to inhibit an early step of translation, by preventing accommodation of mRNA within the entry channel.
DOI: 10.1073/pnas.2017715118
PubMed: 33479166
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Lapointe</name><affiliation wicri:level="2"><nlm:affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Structural Biology, Stanford University School of Medicine, Stanford</wicri:cityArea></affiliation></author><author><name sortKey="Grosely, Rosslyn" sort="Grosely, Rosslyn" uniqKey="Grosely R" first="Rosslyn" last="Grosely">Rosslyn Grosely</name><affiliation wicri:level="2"><nlm:affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Structural Biology, Stanford University School of Medicine, Stanford</wicri:cityArea></affiliation></author><author><name sortKey="Johnson, Alex G" sort="Johnson, Alex G" uniqKey="Johnson A" first="Alex G" last="Johnson">Alex G. Johnson</name><affiliation wicri:level="2"><nlm:affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Structural Biology, Stanford University School of Medicine, Stanford</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:affiliation>Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford</wicri:cityArea></affiliation></author><author><name sortKey="Wang, Jinfan" sort="Wang, Jinfan" uniqKey="Wang J" first="Jinfan" last="Wang">Jinfan Wang</name><affiliation wicri:level="2"><nlm:affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Structural Biology, Stanford University School of Medicine, Stanford</wicri:cityArea></affiliation></author><author><name sortKey="Fernandez, Israel S" sort="Fernandez, Israel S" uniqKey="Fernandez I" first="Israel S" last="Fernández">Israel S. Fernández</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York City, NY 10032.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Columbia University, New York City</wicri:cityArea></affiliation></author><author><name sortKey="Puglisi, Joseph D" sort="Puglisi, Joseph D" uniqKey="Puglisi J" first="Joseph D" last="Puglisi">Joseph D. Puglisi</name><affiliation wicri:level="3"><nlm:affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305; puglisi@stanford.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Structural Biology, Stanford University School of Medicine, Stanford</wicri:regionArea><placeName><settlement type="city">Stanford (Californie)</settlement><region type="state">Californie</region></placeName></affiliation></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="2021" type="published">2021</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a beta-CoV that recently emerged as a human pathogen and is the causative agent of the COVID-19 pandemic. A molecular framework of how the virus manipulates host cellular machinery to facilitate infection remains unclear. Here, we focus on SARS-CoV-2 NSP1, which is proposed to be a virulence factor that inhibits protein synthesis by directly binding the human ribosome. We demonstrate biochemically that NSP1 inhibits translation of model human and SARS-CoV-2 messenger RNAs (mRNAs). NSP1 specifically binds to the small (40S) ribosomal subunit, which is required for translation inhibition. Using single-molecule fluorescence assays to monitor NSP1-40S subunit binding in real time, we determine that eukaryotic translation initiation factors (eIFs) allosterically modulate the interaction of NSP1 with ribosomal preinitiation complexes in the absence of mRNA. We further elucidate that NSP1 competes with RNA segments downstream of the start codon to bind the 40S subunit and that the protein is unable to associate rapidly with 80S ribosomes assembled on an mRNA. Collectively, our findings support a model where NSP1 proteins from viruses in at least two subgenera of beta-CoVs associate with the open head conformation of the 40S subunit to inhibit an early step of translation, by preventing accommodation of mRNA within the entry channel.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">33479166</PMID><DateRevised><Year>2021</Year><Month>01</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>118</Volume><Issue>6</Issue><PubDate><Year>2021</Year><Month>02</Month><Day>09</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>Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e2017715118</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.2017715118</ELocationID><Abstract><AbstractText>Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a beta-CoV that recently emerged as a human pathogen and is the causative agent of the COVID-19 pandemic. A molecular framework of how the virus manipulates host cellular machinery to facilitate infection remains unclear. Here, we focus on SARS-CoV-2 NSP1, which is proposed to be a virulence factor that inhibits protein synthesis by directly binding the human ribosome. We demonstrate biochemically that NSP1 inhibits translation of model human and SARS-CoV-2 messenger RNAs (mRNAs). NSP1 specifically binds to the small (40S) ribosomal subunit, which is required for translation inhibition. Using single-molecule fluorescence assays to monitor NSP1-40S subunit binding in real time, we determine that eukaryotic translation initiation factors (eIFs) allosterically modulate the interaction of NSP1 with ribosomal preinitiation complexes in the absence of mRNA. We further elucidate that NSP1 competes with RNA segments downstream of the start codon to bind the 40S subunit and that the protein is unable to associate rapidly with 80S ribosomes assembled on an mRNA. Collectively, our findings support a model where NSP1 proteins from viruses in at least two subgenera of beta-CoVs associate with the open head conformation of the 40S subunit to inhibit an early step of translation, by preventing accommodation of mRNA within the entry channel.</AbstractText><CopyrightInformation>Copyright © 2021 the Author(s). Published by PNAS.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lapointe</LastName><ForeName>Christopher P</ForeName><Initials>CP</Initials><Identifier Source="ORCID">0000-0002-0406-105X</Identifier><AffiliationInfo><Affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grosely</LastName><ForeName>Rosslyn</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Alex G</ForeName><Initials>AG</Initials><Identifier Source="ORCID">0000-0002-4040-9797</Identifier><AffiliationInfo><Affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Jinfan</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0003-4170-9289</Identifier><AffiliationInfo><Affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernández</LastName><ForeName>Israel S</ForeName><Initials>IS</Initials><Identifier Source="ORCID">0000-0001-7218-1603</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biophysics, Columbia University, New York City, NY 10032.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Puglisi</LastName><ForeName>Joseph D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305; puglisi@stanford.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM011378</GrantID><Acronym>NH</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI047365</GrantID><Acronym>NH</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AG064690</GrantID><Acronym>NH</Acronym><Agency>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><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">NSP1</Keyword><Keyword MajorTopicYN="Y">SARS-CoV-2</Keyword><Keyword MajorTopicYN="Y">eukaryotic translation initiation</Keyword><Keyword MajorTopicYN="Y">human ribosome</Keyword><Keyword MajorTopicYN="Y">single-molecule fluorescence</Keyword></KeywordList><CoiStatement>The authors declare no competing interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2021</Year><Month>1</Month><Day>22</Day><Hour>6</Hour><Minute>16</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2021</Year><Month>1</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2021</Year><Month>1</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33479166</ArticleId><ArticleId IdType="pii">2017715118</ArticleId><ArticleId IdType="doi">10.1073/pnas.2017715118</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Cui J., Li F., Shi Z.-L.. 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Cell Rep.. 2020;31:107497.</Citation></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li><li>État de New York</li></region><settlement><li>Stanford (Californie)</li></settlement></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Lapointe, Christopher P" sort="Lapointe, Christopher P" uniqKey="Lapointe C" first="Christopher P" last="Lapointe">Christopher P. Lapointe</name></region><name sortKey="Fernandez, Israel S" sort="Fernandez, Israel S" uniqKey="Fernandez I" first="Israel S" last="Fernández">Israel S. Fernández</name><name sortKey="Grosely, Rosslyn" sort="Grosely, Rosslyn" uniqKey="Grosely R" first="Rosslyn" last="Grosely">Rosslyn Grosely</name><name sortKey="Johnson, Alex G" sort="Johnson, Alex G" uniqKey="Johnson A" first="Alex G" last="Johnson">Alex G. Johnson</name><name sortKey="Johnson, Alex G" sort="Johnson, Alex G" uniqKey="Johnson A" first="Alex G" last="Johnson">Alex G. Johnson</name><name sortKey="Puglisi, Joseph D" sort="Puglisi, Joseph D" uniqKey="Puglisi J" first="Joseph D" last="Puglisi">Joseph D. Puglisi</name><name sortKey="Wang, Jinfan" sort="Wang, Jinfan" uniqKey="Wang J" first="Jinfan" last="Wang">Jinfan Wang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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