SrasV1, PubMed, Checkpoint, bibRecord, 000588

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.

Identifieur interne : 000588 ( PubMed/Checkpoint ); précédent : 000587; suivant : 000589

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.

Auteurs : Daniel Wrapp [États-Unis] ; Nianshuang Wang [États-Unis] ; Kizzmekia S. Corbett [États-Unis] ; Jory A. Goldsmith [États-Unis] ; Ching-Lin Hsieh [États-Unis] ; Olubukola Abiona [États-Unis] ; Barney S. Graham [États-Unis] ; Jason S. Mclellan [États-Unis]

Source :

Science (New York, N.Y.) [ 1095-9203 ] ; 2020.

RBID : pubmed:32075877

Descripteurs français

English descriptors

KwdEn :
- Antibodies, Monoclonal (immunology), Antibodies, Viral (immunology), Betacoronavirus (chemistry), Betacoronavirus (immunology), Betacoronavirus (metabolism), Betacoronavirus (ultrastructure), Cross Reactions, Cryoelectron Microscopy, Image Processing, Computer-Assisted, Models, Molecular, Peptidyl-Dipeptidase A (metabolism), Protein Binding, Protein Conformation, Protein Domains, Protein Multimerization, Receptors, Virus (metabolism), SARS Virus (chemistry), SARS Virus (immunology), SARS Virus (ultrastructure), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (immunology), Spike Glycoprotein, Coronavirus (metabolism), Spike Glycoprotein, Coronavirus (ultrastructure).
MESH :
- chemical , chemistry : Spike Glycoprotein, Coronavirus.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Spike Glycoprotein, Coronavirus.
- chemistry : Betacoronavirus, SARS Virus.
- immunology : Betacoronavirus, SARS Virus.
- metabolism : Betacoronavirus, Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- ultrastructure : Betacoronavirus, SARS Virus, Spike Glycoprotein, Coronavirus.
- Cross Reactions, Cryoelectron Microscopy, Image Processing, Computer-Assisted, Models, Molecular, Protein Binding, Protein Conformation, Protein Domains, Protein Multimerization.

Abstract

The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis.

DOI: 10.1126/science.abb2507
PubMed: 32075877

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis.</div>
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<Abstract><AbstractText>The outbreak of a novel coronavirus (2019-nCoV) represents a pandemic threat that has been declared a public health emergency of international concern. The CoV spike (S) glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. To facilitate medical countermeasure development, we determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. We also provide biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. Additionally, we tested several published SARS-CoV RBD-specific monoclonal antibodies and found that they do not have appreciable binding to 2019-nCoV S, suggesting that antibody cross-reactivity may be limited between the two RBDs. The structure of 2019-nCoV S should enable the rapid development and evaluation of medical countermeasures to address the ongoing public health crisis.</AbstractText>
<CopyrightInformation>Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</CopyrightInformation>
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</AffiliationInfo>
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<Initials>BS</Initials>
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</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McLellan</LastName>
<ForeName>Jason S</ForeName>
<Initials>JS</Initials>
<Identifier Source="ORCID">0000-0003-3991-542X</Identifier>
<AffiliationInfo><Affiliation>Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. jmclellan@austin.utexas.edu.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 AI127521</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID 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="D052060">Research Support, N.I.H., Intramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
<PublicationType UI="D059040">Video-Audio Media</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2020</Year>
<Month>02</Month>
<Day>19</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Science</MedlineTA>
<NlmUniqueID>0404511</NlmUniqueID>
<ISSNLinking>0036-8075</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C078034">coronavirus receptors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C000657845">spike glycoprotein, COVID-19 virus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber>
<NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber>
<NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance>
</Chemical>
</ChemicalList>
<SupplMeshList><SupplMeshName Type="Organism" UI="C000656484">severe acute respiratory syndrome coronavirus 2</SupplMeshName>
</SupplMeshList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000073640" MajorTopicYN="N">Betacoronavirus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003429" MajorTopicYN="N">Cross Reactions</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020285" MajorTopicYN="N">Cryoelectron Microscopy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007091" MajorTopicYN="N">Image Processing, Computer-Assisted</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year>
<Month>02</Month>
<Day>10</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2020</Year>
<Month>02</Month>
<Day>17</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2020</Year>
<Month>2</Month>
<Day>23</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2020</Year>
<Month>3</Month>
<Day>20</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2020</Year>
<Month>2</Month>
<Day>21</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">32075877</ArticleId>
<ArticleId IdType="pii">science.abb2507</ArticleId>
<ArticleId IdType="doi">10.1126/science.abb2507</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Maryland</li>
<li>Texas</li>
</region>
<settlement><li>Austin (Texas)</li>
</settlement>
<orgName><li>Université du Texas à Austin</li>
</orgName>
</list>
<tree><country name="États-Unis"><region name="Texas"><name sortKey="Wrapp, Daniel" sort="Wrapp, Daniel" uniqKey="Wrapp D" first="Daniel" last="Wrapp">Daniel Wrapp</name>
</region>
<name sortKey="Abiona, Olubukola" sort="Abiona, Olubukola" uniqKey="Abiona O" first="Olubukola" last="Abiona">Olubukola Abiona</name>
<name sortKey="Corbett, Kizzmekia S" sort="Corbett, Kizzmekia S" uniqKey="Corbett K" first="Kizzmekia S" last="Corbett">Kizzmekia S. Corbett</name>
<name sortKey="Goldsmith, Jory A" sort="Goldsmith, Jory A" uniqKey="Goldsmith J" first="Jory A" last="Goldsmith">Jory A. Goldsmith</name>
<name sortKey="Graham, Barney S" sort="Graham, Barney S" uniqKey="Graham B" first="Barney S" last="Graham">Barney S. Graham</name>
<name sortKey="Hsieh, Ching Lin" sort="Hsieh, Ching Lin" uniqKey="Hsieh C" first="Ching-Lin" last="Hsieh">Ching-Lin Hsieh</name>
<name sortKey="Mclellan, Jason S" sort="Mclellan, Jason S" uniqKey="Mclellan J" first="Jason S" last="Mclellan">Jason S. Mclellan</name>
<name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name>
</country>
</tree>
</affiliations>
</record>

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   |texte=   Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.
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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.

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Abstract

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