Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing.
Identifieur interne : 001283 ( PubMed/Corpus ); précédent : 001282; suivant : 001284Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing.
Auteurs : Hatem A. Elshabrawy ; Melissa M. Coughlin ; Susan C. Baker ; Bellur S. PrabhakarSource :
- PloS one [ 1932-6203 ] ; 2012.
English descriptors
- KwdEn :
- Antibodies, Neutralizing (pharmacology), Antibodies, Viral (pharmacology), Antibody Affinity, Antibody Specificity, Binding Sites, Antibody, Cross Reactions, Epitope Mapping, HEK293 Cells, Humans, Membrane Glycoproteins (antagonists & inhibitors), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Neutralization Tests, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins (antagonists & inhibitors), Recombinant Proteins (genetics), Recombinant Proteins (immunology), SARS Virus (drug effects), SARS Virus (genetics), SARS Virus (immunology), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (prevention & control), Spike Glycoprotein, Coronavirus, Transfection, Viral Envelope Proteins (antagonists & inhibitors), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology).
- MESH :
- chemical , antagonists & inhibitors : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , pharmacology : Antibodies, Neutralizing, Antibodies, Viral.
- drug effects : SARS Virus.
- genetics : SARS Virus.
- immunology : SARS Virus, Severe Acute Respiratory Syndrome.
- prevention & control : Severe Acute Respiratory Syndrome.
- Antibody Affinity, Antibody Specificity, Binding Sites, Antibody, Cross Reactions, Epitope Mapping, HEK293 Cells, Humans, Neutralization Tests, Protein Binding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Transfection.
Abstract
Immune sera from convalescent patients have been shown to be effective in the treatment of patients infected with Severe Acute Respiratory Syndrome Virus (SARS-CoV) making passive immune therapy with human monoclonal antibodies an attractive treatment strategy for SARS. Previously, using Xenomouse (Amgen British Columbia Inc), we produced a panel of neutralizing Human monoclonal antibodies (HmAbs) that could specifically bind to the ectodomain of the SARS-CoV spike (S) glycoprotein. Some of the HmAbs were S1 domain specific, while some were not. In this study, we describe non-S1 binding neutralizing HmAbs that can specifically bind to the conserved S2 domain of the S protein. However, unlike the S1 specific HmAbs, the S2 specific HmAbs can neutralize pseudotyped viruses expressing different S proteins containing receptor binding domain sequences of various clinical isolates. These data indicate that HmAbs which bind to conserved regions of the S protein are more suitable for conferring protection against a wide range of SARS-CoV variants and have implications for generating therapeutic antibodies or subunit vaccines against other enveloped viruses.
DOI: 10.1371/journal.pone.0050366
PubMed: 23185609
Links to Exploration step
pubmed:23185609Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing.</title><author><name sortKey="Elshabrawy, Hatem A" sort="Elshabrawy, Hatem A" uniqKey="Elshabrawy H" first="Hatem A" last="Elshabrawy">Hatem A. Elshabrawy</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Coughlin, Melissa M" sort="Coughlin, Melissa M" uniqKey="Coughlin M" first="Melissa M" last="Coughlin">Melissa M. Coughlin</name></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C" last="Baker">Susan C. Baker</name></author><author><name sortKey="Prabhakar, Bellur S" sort="Prabhakar, Bellur S" uniqKey="Prabhakar B" first="Bellur S" last="Prabhakar">Bellur S. Prabhakar</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:23185609</idno><idno type="pmid">23185609</idno><idno type="doi">10.1371/journal.pone.0050366</idno><idno type="wicri:Area/PubMed/Corpus">001283</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001283</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing.</title><author><name sortKey="Elshabrawy, Hatem A" sort="Elshabrawy, Hatem A" uniqKey="Elshabrawy H" first="Hatem A" last="Elshabrawy">Hatem A. Elshabrawy</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois, United States of America.</nlm:affiliation></affiliation></author><author><name sortKey="Coughlin, Melissa M" sort="Coughlin, Melissa M" uniqKey="Coughlin M" first="Melissa M" last="Coughlin">Melissa M. Coughlin</name></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C" last="Baker">Susan C. Baker</name></author><author><name sortKey="Prabhakar, Bellur S" sort="Prabhakar, Bellur S" uniqKey="Prabhakar B" first="Bellur S" last="Prabhakar">Bellur S. Prabhakar</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Neutralizing (pharmacology)</term><term>Antibodies, Viral (pharmacology)</term><term>Antibody Affinity</term><term>Antibody Specificity</term><term>Binding Sites, Antibody</term><term>Cross Reactions</term><term>Epitope Mapping</term><term>HEK293 Cells</term><term>Humans</term><term>Membrane Glycoproteins (antagonists & inhibitors)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (immunology)</term><term>Neutralization Tests</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Recombinant Proteins (antagonists & inhibitors)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (immunology)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (genetics)</term><term>SARS Virus (immunology)</term><term>Severe Acute Respiratory Syndrome (immunology)</term><term>Severe Acute Respiratory Syndrome (prevention & control)</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term><term>Viral Envelope Proteins (antagonists & inhibitors)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antibodies, Neutralizing</term><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Antibody Affinity</term><term>Antibody Specificity</term><term>Binding Sites, Antibody</term><term>Cross Reactions</term><term>Epitope Mapping</term><term>HEK293 Cells</term><term>Humans</term><term>Neutralization Tests</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Immune sera from convalescent patients have been shown to be effective in the treatment of patients infected with Severe Acute Respiratory Syndrome Virus (SARS-CoV) making passive immune therapy with human monoclonal antibodies an attractive treatment strategy for SARS. Previously, using Xenomouse (Amgen British Columbia Inc), we produced a panel of neutralizing Human monoclonal antibodies (HmAbs) that could specifically bind to the ectodomain of the SARS-CoV spike (S) glycoprotein. Some of the HmAbs were S1 domain specific, while some were not. In this study, we describe non-S1 binding neutralizing HmAbs that can specifically bind to the conserved S2 domain of the S protein. However, unlike the S1 specific HmAbs, the S2 specific HmAbs can neutralize pseudotyped viruses expressing different S proteins containing receptor binding domain sequences of various clinical isolates. These data indicate that HmAbs which bind to conserved regions of the S protein are more suitable for conferring protection against a wide range of SARS-CoV variants and have implications for generating therapeutic antibodies or subunit vaccines against other enveloped viruses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23185609</PMID><DateCompleted><Year>2013</Year><Month>05</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>11</Issue><PubDate><Year>2012</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing.</ArticleTitle><Pagination><MedlinePgn>e50366</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0050366</ELocationID><Abstract><AbstractText>Immune sera from convalescent patients have been shown to be effective in the treatment of patients infected with Severe Acute Respiratory Syndrome Virus (SARS-CoV) making passive immune therapy with human monoclonal antibodies an attractive treatment strategy for SARS. Previously, using Xenomouse (Amgen British Columbia Inc), we produced a panel of neutralizing Human monoclonal antibodies (HmAbs) that could specifically bind to the ectodomain of the SARS-CoV spike (S) glycoprotein. Some of the HmAbs were S1 domain specific, while some were not. In this study, we describe non-S1 binding neutralizing HmAbs that can specifically bind to the conserved S2 domain of the S protein. However, unlike the S1 specific HmAbs, the S2 specific HmAbs can neutralize pseudotyped viruses expressing different S proteins containing receptor binding domain sequences of various clinical isolates. These data indicate that HmAbs which bind to conserved regions of the S protein are more suitable for conferring protection against a wide range of SARS-CoV variants and have implications for generating therapeutic antibodies or subunit vaccines against other enveloped viruses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Elshabrawy</LastName><ForeName>Hatem A</ForeName><Initials>HA</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois, United States of America.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coughlin</LastName><ForeName>Melissa M</ForeName><Initials>MM</Initials></Author><Author ValidYN="Y"><LastName>Baker</LastName><ForeName>Susan C</ForeName><Initials>SC</Initials></Author><Author ValidYN="Y"><LastName>Prabhakar</LastName><ForeName>Bellur S</ForeName><Initials>BS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1U01AI082296</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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>11</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D057134">Antibodies, Neutralizing</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, Viral</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="D011994">Recombinant Proteins</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D057134" MajorTopicYN="N">Antibodies, Neutralizing</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000915" MajorTopicYN="N">Antibody Affinity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000918" MajorTopicYN="N">Antibody Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001666" MajorTopicYN="N">Binding Sites, Antibody</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003429" MajorTopicYN="N">Cross Reactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018604" MajorTopicYN="N">Epitope Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009500" MajorTopicYN="N">Neutralization Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000517" MajorTopicYN="N">prevention & control</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>06</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>10</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>5</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23185609</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0050366</ArticleId><ArticleId IdType="pii">PONE-D-12-18419</ArticleId><ArticleId IdType="pmc">PMC3503966</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Science. 2005 Sep 16;309(5742):1864-8</Citation><ArticleIdList><ArticleId IdType="pubmed">16166518</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Sep;79(18):11892-900</Citation><ArticleIdList><ArticleId IdType="pubmed">16140765</ArticleId></ArticleIdList></Reference><Reference><Citation>Virol J. 2005;2:73</Citation><ArticleIdList><ArticleId IdType="pubmed">16122388</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Mol Immunol. 2004 Apr;1(2):119-22</Citation><ArticleIdList><ArticleId IdType="pubmed">16212898</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2005 Oct 28;310(5748):676-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16195424</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomed Sci. 2005 Oct;12(5):711-27</Citation><ArticleIdList><ArticleId IdType="pubmed">16132115</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Jan;80(2):941-50</Citation><ArticleIdList><ArticleId IdType="pubmed">16378996</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Feb 10;281(6):3198-203</Citation><ArticleIdList><ArticleId IdType="pubmed">16339146</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS Med. 2006 Jul;3(7):e237</Citation><ArticleIdList><ArticleId IdType="pubmed">16796401</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2006;1:e24</Citation><ArticleIdList><ArticleId IdType="pubmed">17183651</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2007 Apr 25;361(1):93-102</Citation><ArticleIdList><ArticleId IdType="pubmed">17161858</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Biotechnol. 2007 Dec;25(12):1421-34</Citation><ArticleIdList><ArticleId IdType="pubmed">18066039</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Apr;82(7):3220-35</Citation><ArticleIdList><ArticleId IdType="pubmed">18199635</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Sep;82(17):8887-90</Citation><ArticleIdList><ArticleId IdType="pubmed">18562523</ArticleId></ArticleIdList></Reference><Reference><Citation>Antiviral Res. 2009 Jan;81(1):82-7</Citation><ArticleIdList><ArticleId IdType="pubmed">18983873</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Microbiol. 2009 Mar;7(3):226-36</Citation><ArticleIdList><ArticleId IdType="pubmed">19198616</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2009;4(5):e5672</Citation><ArticleIdList><ArticleId IdType="pubmed">19478856</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2009 Nov 10;394(1):39-46</Citation><ArticleIdList><ArticleId IdType="pubmed">19748648</ArticleId></ArticleIdList></Reference><Reference><Citation>J Infect Dis. 2010 Mar 15;201(6):946-55</Citation><ArticleIdList><ArticleId IdType="pubmed">20144042</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2010 Apr;84(7):3134-46</Citation><ArticleIdList><ArticleId IdType="pubmed">19906932</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cancer. 2010;9:299</Citation><ArticleIdList><ArticleId IdType="pubmed">21092230</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2011 Dec 15;480(7377):336-43</Citation><ArticleIdList><ArticleId IdType="pubmed">22113616</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 May 30;300(5624):1399-404</Citation><ArticleIdList><ArticleId IdType="pubmed">12730501</ArticleId></ArticleIdList></Reference><Reference><Citation>Lancet. 2003 May 24;361(9371):1767-72</Citation><ArticleIdList><ArticleId IdType="pubmed">12781535</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 Oct 10;302(5643):276-8</Citation><ArticleIdList><ArticleId IdType="pubmed">12958366</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Jan 30;279(5):3197-201</Citation><ArticleIdList><ArticleId IdType="pubmed">14670965</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2004 Apr 1;428(6982):561-4</Citation><ArticleIdList><ArticleId IdType="pubmed">15024391</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 May 14;279(20):20836-49</Citation><ArticleIdList><ArticleId IdType="pubmed">14996844</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8709-14</Citation><ArticleIdList><ArticleId IdType="pubmed">15161975</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Jul;78(13):6938-45</Citation><ArticleIdList><ArticleId IdType="pubmed">15194770</ArticleId></ArticleIdList></Reference><Reference><Citation>AIDS. 1989 Dec;3(12):777-84</Citation><ArticleIdList><ArticleId IdType="pubmed">2483618</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1998 Dec 23;95(7):871-4</Citation><ArticleIdList><ArticleId IdType="pubmed">9875840</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Med. 2004 Dec;10(12 Suppl):S88-97</Citation><ArticleIdList><ArticleId IdType="pubmed">15577937</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2430-5</Citation><ArticleIdList><ArticleId IdType="pubmed">15695582</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Mar;79(6):3289-96</Citation><ArticleIdList><ArticleId IdType="pubmed">15731223</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Mar;79(6):3401-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15731234</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2005 Mar 30;334(1):74-82</Citation><ArticleIdList><ArticleId IdType="pubmed">15749124</ArticleId></ArticleIdList></Reference><Reference><Citation>Hybridoma (Larchmt). 2005 Feb;24(1):36-41</Citation><ArticleIdList><ArticleId IdType="pubmed">15785207</ArticleId></ArticleIdList></Reference><Reference><Citation>J Immunol. 2005 Apr 15;174(8):4908-15</Citation><ArticleIdList><ArticleId IdType="pubmed">15814718</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Jun;79(11):7195-206</Citation><ArticleIdList><ArticleId IdType="pubmed">15890958</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Jul;79(14):9062-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15994800</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):14040-5</Citation><ArticleIdList><ArticleId IdType="pubmed">16169905</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001283 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 001283 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:23185609
|texte= Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:23185609" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |