Structural insights into immune recognition of the severe acute respiratory syndrome coronavirus S protein receptor binding domain.
Identifieur interne : 001935 ( PubMed/Corpus ); précédent : 001934; suivant : 001936Structural insights into immune recognition of the severe acute respiratory syndrome coronavirus S protein receptor binding domain.
Auteurs : John E. Pak ; Chetna Sharon ; Malathy Satkunarajah ; Thierry C. Auperin ; Cheryl M. Cameron ; David J. Kelvin ; Jayaraman Seetharaman ; Alan Cochrane ; Francis A. Plummer ; Jody D. Berry ; James M. RiniSource :
- Journal of molecular biology [ 1089-8638 ] ; 2009.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (chemistry), Antibodies, Monoclonal (immunology), Antibody Formation (immunology), Binding Sites, Cell Line, Crystallography, X-Ray, Humans, Immunoglobulin Fab Fragments (chemistry), Immunoglobulin Fab Fragments (immunology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Mice, Models, Molecular, Molecular Sequence Data, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (immunology), Protein Structure, Tertiary, Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (immunology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology).
- MESH :
- chemical , chemistry : Antibodies, Monoclonal, Immunoglobulin Fab Fragments, Membrane Glycoproteins, Peptidyl-Dipeptidase A, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Monoclonal, Immunoglobulin Fab Fragments, Membrane Glycoproteins, Peptidyl-Dipeptidase A, Viral Envelope Proteins.
- immunology : Antibody Formation, SARS Virus.
- chemical , metabolism : Recombinant Fusion Proteins.
- Animals, Binding Sites, Cell Line, Crystallography, X-Ray, Humans, Mice, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus.
Abstract
The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for host cell attachment and fusion of the viral and host cell membranes. Within S the receptor binding domain (RBD) mediates the interaction with angiotensin-converting enzyme 2 (ACE2), the SARS-CoV host cell receptor. Both S and the RBD are highly immunogenic and both have been found to elicit neutralizing antibodies. Reported here is the X-ray crystal structure of the RBD in complex with the Fab of a neutralizing mouse monoclonal antibody, F26G19, elicited by immunization with chemically inactivated SARS-CoV. The RBD-F26G19 Fab complex represents the first example of the structural characterization of an antibody elicited by an immune response to SARS-CoV or any fragment of it. The structure reveals that the RBD surface recognized by F26G19 overlaps significantly with the surface recognized by ACE2 and, as such, suggests that F26G19 likely neutralizes SARS-CoV by blocking the virus-host cell interaction.
DOI: 10.1016/j.jmb.2009.03.042
PubMed: 19324051
Links to Exploration step
pubmed:19324051Le document en format XML
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Pak</name><affiliation><nlm:affiliation>Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Sharon, Chetna" sort="Sharon, Chetna" uniqKey="Sharon C" first="Chetna" last="Sharon">Chetna Sharon</name></author><author><name sortKey="Satkunarajah, Malathy" sort="Satkunarajah, Malathy" uniqKey="Satkunarajah M" first="Malathy" last="Satkunarajah">Malathy Satkunarajah</name></author><author><name sortKey="Auperin, Thierry C" sort="Auperin, Thierry C" uniqKey="Auperin T" first="Thierry C" last="Auperin">Thierry C. Auperin</name></author><author><name sortKey="Cameron, Cheryl M" sort="Cameron, Cheryl M" uniqKey="Cameron C" first="Cheryl M" last="Cameron">Cheryl M. Cameron</name></author><author><name sortKey="Kelvin, David J" sort="Kelvin, David J" uniqKey="Kelvin D" first="David J" last="Kelvin">David J. Kelvin</name></author><author><name sortKey="Seetharaman, Jayaraman" sort="Seetharaman, Jayaraman" uniqKey="Seetharaman J" first="Jayaraman" last="Seetharaman">Jayaraman Seetharaman</name></author><author><name sortKey="Cochrane, Alan" sort="Cochrane, Alan" uniqKey="Cochrane A" first="Alan" last="Cochrane">Alan Cochrane</name></author><author><name sortKey="Plummer, Francis A" sort="Plummer, Francis A" uniqKey="Plummer F" first="Francis A" last="Plummer">Francis A. Plummer</name></author><author><name sortKey="Berry, Jody D" sort="Berry, Jody D" uniqKey="Berry J" first="Jody D" last="Berry">Jody D. Berry</name></author><author><name sortKey="Rini, James M" sort="Rini, James M" uniqKey="Rini J" first="James M" last="Rini">James M. Rini</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="eISSN">1089-8638</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Monoclonal (chemistry)</term><term>Antibodies, Monoclonal (immunology)</term><term>Antibody Formation (immunology)</term><term>Binding Sites</term><term>Cell Line</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Immunoglobulin Fab Fragments (chemistry)</term><term>Immunoglobulin Fab Fragments (immunology)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (immunology)</term><term>Mice</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Peptidyl-Dipeptidase A (immunology)</term><term>Protein Structure, Tertiary</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (immunology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Immunoglobulin Fab Fragments</term><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Immunoglobulin Fab Fragments</term><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Antibody Formation</term><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Cell Line</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Mice</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for host cell attachment and fusion of the viral and host cell membranes. Within S the receptor binding domain (RBD) mediates the interaction with angiotensin-converting enzyme 2 (ACE2), the SARS-CoV host cell receptor. Both S and the RBD are highly immunogenic and both have been found to elicit neutralizing antibodies. Reported here is the X-ray crystal structure of the RBD in complex with the Fab of a neutralizing mouse monoclonal antibody, F26G19, elicited by immunization with chemically inactivated SARS-CoV. The RBD-F26G19 Fab complex represents the first example of the structural characterization of an antibody elicited by an immune response to SARS-CoV or any fragment of it. The structure reveals that the RBD surface recognized by F26G19 overlaps significantly with the surface recognized by ACE2 and, as such, suggests that F26G19 likely neutralizes SARS-CoV by blocking the virus-host cell interaction.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19324051</PMID><DateCompleted><Year>2009</Year><Month>06</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1089-8638</ISSN><JournalIssue CitedMedium="Internet"><Volume>388</Volume><Issue>4</Issue><PubDate><Year>2009</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J. Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Structural insights into immune recognition of the severe acute respiratory syndrome coronavirus S protein receptor binding domain.</ArticleTitle><Pagination><MedlinePgn>815-23</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jmb.2009.03.042</ELocationID><Abstract><AbstractText>The spike (S) protein of the severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for host cell attachment and fusion of the viral and host cell membranes. Within S the receptor binding domain (RBD) mediates the interaction with angiotensin-converting enzyme 2 (ACE2), the SARS-CoV host cell receptor. Both S and the RBD are highly immunogenic and both have been found to elicit neutralizing antibodies. Reported here is the X-ray crystal structure of the RBD in complex with the Fab of a neutralizing mouse monoclonal antibody, F26G19, elicited by immunization with chemically inactivated SARS-CoV. The RBD-F26G19 Fab complex represents the first example of the structural characterization of an antibody elicited by an immune response to SARS-CoV or any fragment of it. The structure reveals that the RBD surface recognized by F26G19 overlaps significantly with the surface recognized by ACE2 and, as such, suggests that F26G19 likely neutralizes SARS-CoV by blocking the virus-host cell interaction.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pak</LastName><ForeName>John E</ForeName><Initials>JE</Initials><AffiliationInfo><Affiliation>Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sharon</LastName><ForeName>Chetna</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Satkunarajah</LastName><ForeName>Malathy</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Auperin</LastName><ForeName>Thierry C</ForeName><Initials>TC</Initials></Author><Author ValidYN="Y"><LastName>Cameron</LastName><ForeName>Cheryl M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Kelvin</LastName><ForeName>David J</ForeName><Initials>DJ</Initials></Author><Author ValidYN="Y"><LastName>Seetharaman</LastName><ForeName>Jayaraman</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Cochrane</LastName><ForeName>Alan</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Plummer</LastName><ForeName>Francis A</ForeName><Initials>FA</Initials></Author><Author ValidYN="Y"><LastName>Berry</LastName><ForeName>Jody D</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Rini</LastName><ForeName>James M</ForeName><Initials>JM</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>3BGF</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>03</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007140">Immunoglobulin Fab Fragments</NameOfSubstance></Chemical><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="D011993">Recombinant Fusion 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