Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology
Identifieur interne : 002083 ( Ncbi/Merge ); précédent : 002082; suivant : 002084Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology
Auteurs : Jody D. Berry [États-Unis, Canada] ; Kevin Hay [États-Unis] ; James M. Rini [États-Unis] ; Meng Yu ; Linfa Wang ; Francis A. Plummer [États-Unis, Canada] ; Cindi R. Corbett [États-Unis, Canada] ; Anton Andonov [États-Unis, Canada]Source :
- mAbs [ 1942-0862 ] ; 2010.
Descripteurs français
- KwdFr :
- Affinité des anticorps, Animaux, Anticorps monoclonaux (), Anticorps monoclonaux (génétique), Anticorps monoclonaux (immunologie), Anticorps monoclonaux (métabolisme), Anticorps neutralisants (), Anticorps neutralisants (génétique), Anticorps neutralisants (immunologie), Anticorps neutralisants (métabolisme), Cartographie épitopique, Conformation des protéines, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Protéines de fusion recombinantes (), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (immunologie), Protéines de fusion recombinantes (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Récepteur de type 2 à l'angiotensine-II (métabolisme), Récepteurs pour l'antigène des lymphocytes B (immunologie), Souris, Syndrome respiratoire aigu sévère (), Syndrome respiratoire aigu sévère (immunologie), Syndrome respiratoire aigu sévère (virologie), Technologie biomédicale, Test ELISA, Vaccins antiviraux, Virus du SRAS (immunologie), Épitopes immunodominants (immunologie).
- MESH :
- génétique : Anticorps monoclonaux, Anticorps neutralisants, Protéines de fusion recombinantes.
- immunologie : Anticorps monoclonaux, Anticorps neutralisants, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Récepteurs pour l'antigène des lymphocytes B, Syndrome respiratoire aigu sévère, Virus du SRAS, Épitopes immunodominants.
- métabolisme : Anticorps monoclonaux, Anticorps neutralisants, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Récepteur de type 2 à l'angiotensine-II.
- virologie : Syndrome respiratoire aigu sévère.
- Affinité des anticorps, Animaux, Anticorps monoclonaux, Anticorps neutralisants, Cartographie épitopique, Conformation des protéines, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Souris, Syndrome respiratoire aigu sévère, Technologie biomédicale, Test ELISA, Vaccins antiviraux.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (chemistry), Antibodies, Monoclonal (genetics), Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (metabolism), Antibodies, Neutralizing (chemistry), Antibodies, Neutralizing (genetics), Antibodies, Neutralizing (immunology), Antibodies, Neutralizing (metabolism), Antibody Affinity, Biomedical Technology, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Humans, Immunodominant Epitopes (immunology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Mice, Protein Binding, Protein Conformation, Receptor, Angiotensin, Type 2 (metabolism), Receptors, Antigen, B-Cell (immunology), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (immunology), Recombinant Fusion Proteins (metabolism), SARS Virus (immunology), Severe Acute Respiratory Syndrome (immunology), Severe Acute Respiratory Syndrome (prevention & control), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism), Viral Vaccines.
- MESH :
- chemical , chemistry : Antibodies, Monoclonal, Antibodies, Neutralizing, Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , genetics : Antibodies, Monoclonal, Antibodies, Neutralizing, Recombinant Fusion Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Neutralizing, Immunodominant Epitopes, Membrane Glycoproteins, Receptors, Antigen, B-Cell, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , metabolism : Antibodies, Monoclonal, Antibodies, Neutralizing, Membrane Glycoproteins, Receptor, Angiotensin, Type 2, Recombinant Fusion Proteins, Viral Envelope Proteins.
- immunology : SARS Virus, Severe Acute Respiratory Syndrome.
- prevention & control : Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Antibody Affinity, Biomedical Technology, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Humans, Mice, Protein Binding, Protein Conformation, Spike Glycoprotein, Coronavirus, Viral Vaccines.
Abstract
Neutralizing antibody responses to the surface glycoproteins of enveloped viruses play an important role in immunity. Many of these glycoproteins, including the severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) protein form trimeric units in the membrane of the native virion. There is substantial experimental and pre-clinical evidence showing that the S protein is a promising lead for vaccines and therapeutics. Previously we generated a panel of monoclonal antibodies (mAbs) to whole inactivated SARS-CoV which neutralize the virus in vitro.
Url:
PubMed: 20168090
PubMed Central: 2828578
Links toward previous steps (curation, corpus...)
- to stream Pmc, to step Corpus: 000816
- to stream Pmc, to step Curation: 000816
- to stream Pmc, to step Checkpoint: 000C08
- to stream PubMed, to step Corpus: 001746
- to stream PubMed, to step Curation: 001746
- to stream PubMed, to step Checkpoint: 003492
Links to Exploration step
PMC:2828578Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology</title>
<author><name sortKey="Berry, Jody D" sort="Berry, Jody D" uniqKey="Berry J" first="Jody D" last="Berry">Jody D. Berry</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Hay, Kevin" sort="Hay, Kevin" uniqKey="Hay K" first="Kevin" last="Hay">Kevin Hay</name>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Rini, James M" sort="Rini, James M" uniqKey="Rini J" first="James M" last="Rini">James M. Rini</name>
<affiliation wicri:level="2"><nlm:aff id="A4">Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Wang, Linfa" sort="Wang, Linfa" uniqKey="Wang L" first="Linfa" last="Wang">Linfa Wang</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Plummer, Francis A" sort="Plummer, Francis A" uniqKey="Plummer F" first="Francis A" last="Plummer">Francis A. Plummer</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Corbett, Cindi R" sort="Corbett, Cindi R" uniqKey="Corbett C" first="Cindi R" last="Corbett">Cindi R. Corbett</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">20168090</idno>
<idno type="pmc">2828578</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2828578</idno>
<idno type="RBID">PMC:2828578</idno>
<date when="2010">2010</date>
<idno type="wicri:Area/Pmc/Corpus">000816</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000816</idno>
<idno type="wicri:Area/Pmc/Curation">000816</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000816</idno>
<idno type="wicri:Area/Pmc/Checkpoint">000C08</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000C08</idno>
<idno type="wicri:source">PubMed</idno>
<idno type="RBID">pubmed:20168090</idno>
<idno type="wicri:Area/PubMed/Corpus">001746</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001746</idno>
<idno type="wicri:Area/PubMed/Curation">001746</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001746</idno>
<idno type="wicri:Area/PubMed/Checkpoint">003492</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">003492</idno>
<idno type="wicri:Area/Ncbi/Merge">002083</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology</title>
<author><name sortKey="Berry, Jody D" sort="Berry, Jody D" uniqKey="Berry J" first="Jody D" last="Berry">Jody D. Berry</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Hay, Kevin" sort="Hay, Kevin" uniqKey="Hay K" first="Kevin" last="Hay">Kevin Hay</name>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Rini, James M" sort="Rini, James M" uniqKey="Rini J" first="James M" last="Rini">James M. Rini</name>
<affiliation wicri:level="2"><nlm:aff id="A4">Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Wang, Linfa" sort="Wang, Linfa" uniqKey="Wang L" first="Linfa" last="Wang">Linfa Wang</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Plummer, Francis A" sort="Plummer, Francis A" uniqKey="Plummer F" first="Francis A" last="Plummer">Francis A. Plummer</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Corbett, Cindi R" sort="Corbett, Cindi R" uniqKey="Corbett C" first="Cindi R" last="Corbett">Cindi R. Corbett</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
</analytic>
<series><title level="j">mAbs</title>
<idno type="ISSN">1942-0862</idno>
<idno type="eISSN">1942-0870</idno>
<imprint><date when="2010">2010</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 (genetics)</term>
<term>Antibodies, Monoclonal (immunology)</term>
<term>Antibodies, Monoclonal (metabolism)</term>
<term>Antibodies, Neutralizing (chemistry)</term>
<term>Antibodies, Neutralizing (genetics)</term>
<term>Antibodies, Neutralizing (immunology)</term>
<term>Antibodies, Neutralizing (metabolism)</term>
<term>Antibody Affinity</term>
<term>Biomedical Technology</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Epitope Mapping</term>
<term>Humans</term>
<term>Immunodominant Epitopes (immunology)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Mice</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Receptor, Angiotensin, Type 2 (metabolism)</term>
<term>Receptors, Antigen, B-Cell (immunology)</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (immunology)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>SARS Virus (immunology)</term>
<term>Severe Acute Respiratory Syndrome (immunology)</term>
<term>Severe Acute Respiratory Syndrome (prevention & control)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (immunology)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Viral Vaccines</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Affinité des anticorps</term>
<term>Animaux</term>
<term>Anticorps monoclonaux ()</term>
<term>Anticorps monoclonaux (génétique)</term>
<term>Anticorps monoclonaux (immunologie)</term>
<term>Anticorps monoclonaux (métabolisme)</term>
<term>Anticorps neutralisants ()</term>
<term>Anticorps neutralisants (génétique)</term>
<term>Anticorps neutralisants (immunologie)</term>
<term>Anticorps neutralisants (métabolisme)</term>
<term>Cartographie épitopique</term>
<term>Conformation des protéines</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Protéines de fusion recombinantes ()</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (immunologie)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Récepteur de type 2 à l'angiotensine-II (métabolisme)</term>
<term>Récepteurs pour l'antigène des lymphocytes B (immunologie)</term>
<term>Souris</term>
<term>Syndrome respiratoire aigu sévère ()</term>
<term>Syndrome respiratoire aigu sévère (immunologie)</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Technologie biomédicale</term>
<term>Test ELISA</term>
<term>Vaccins antiviraux</term>
<term>Virus du SRAS (immunologie)</term>
<term>Épitopes immunodominants (immunologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Membrane Glycoproteins</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Immunodominant Epitopes</term>
<term>Membrane Glycoproteins</term>
<term>Receptors, Antigen, B-Cell</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Membrane Glycoproteins</term>
<term>Receptor, Angiotensin, Type 2</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Protéines de fusion recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Récepteurs pour l'antigène des lymphocytes B</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Virus du SRAS</term>
<term>Épitopes immunodominants</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="métabolisme" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Récepteur de type 2 à l'angiotensine-II</term>
</keywords>
<keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Antibody Affinity</term>
<term>Biomedical Technology</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Epitope Mapping</term>
<term>Humans</term>
<term>Mice</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Vaccines</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Affinité des anticorps</term>
<term>Animaux</term>
<term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Cartographie épitopique</term>
<term>Conformation des protéines</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Souris</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Technologie biomédicale</term>
<term>Test ELISA</term>
<term>Vaccins antiviraux</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Neutralizing antibody responses to the surface glycoproteins of enveloped viruses play an important role in immunity. Many of these glycoproteins, including the severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) protein form trimeric units in the membrane of the native virion. There is substantial experimental and pre-clinical evidence showing that the S protein is a promising lead for vaccines and therapeutics. Previously we generated a panel of monoclonal antibodies (mAbs) to whole inactivated SARS-CoV which neutralize the virus in vitro.<xref ref-type="bibr" rid="R1">1</xref>
,<xref ref-type="bibr" rid="R2">2</xref>
Here, we define their specificity and affinity, map several of their epitopes and lastly characterise chimeric versions of them. Our data show that the neutralizing mAbs bind to the angiotensin-converting enzyme 2 (ACE2) receptor-binding domain (RBD) of the SARS S protein. Three of the chimeric mAbs retain their binding specificity while one conformational mAb, F26G19, lost its ability to bind the S protein despite high level expression. The affinity for recombinant S is maintained in all of the functional chimeric versions of the parental mAbs. Both parental mAb F26G18 and the chimeric version neutralize the TOR2 strain of SARS-CoV with essentially identical titres (2.07 and 2.47 nM, respectively). Lastly, a comparison with other neutralizing mAbs to SARS-CoV clearly shows that the dominance of a 33 amino acid residue loop of the SARS-CoV RBD is independent of repertoire, species, quaternary structure, and importantly, the technology used to derive the mAbs. In cases like this, the dominance of a compact RBD antigenic domain and the central role of the S protein in pathogenesis may inherently create immunoselection pressure on viruses to evolve more complex evasion strategies or die out of a host species. The apparent simplicity of the mechanism of SARS-CoV neutralization is in stark contrast to the complexity shown by other enveloped viruses.</p>
</div>
</front>
</TEI>
<double pmid="20168090"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology</title>
<author><name sortKey="Berry, Jody D" sort="Berry, Jody D" uniqKey="Berry J" first="Jody D" last="Berry">Jody D. Berry</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Hay, Kevin" sort="Hay, Kevin" uniqKey="Hay K" first="Kevin" last="Hay">Kevin Hay</name>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Rini, James M" sort="Rini, James M" uniqKey="Rini J" first="James M" last="Rini">James M. Rini</name>
<affiliation wicri:level="2"><nlm:aff id="A4">Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Wang, Linfa" sort="Wang, Linfa" uniqKey="Wang L" first="Linfa" last="Wang">Linfa Wang</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Plummer, Francis A" sort="Plummer, Francis A" uniqKey="Plummer F" first="Francis A" last="Plummer">Francis A. Plummer</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Corbett, Cindi R" sort="Corbett, Cindi R" uniqKey="Corbett C" first="Cindi R" last="Corbett">Cindi R. Corbett</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">20168090</idno>
<idno type="pmc">2828578</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2828578</idno>
<idno type="RBID">PMC:2828578</idno>
<date when="2010">2010</date>
<idno type="wicri:Area/Pmc/Corpus">000816</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000816</idno>
<idno type="wicri:Area/Pmc/Curation">000816</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000816</idno>
<idno type="wicri:Area/Pmc/Checkpoint">000C08</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000C08</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology</title>
<author><name sortKey="Berry, Jody D" sort="Berry, Jody D" uniqKey="Berry J" first="Jody D" last="Berry">Jody D. Berry</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Hay, Kevin" sort="Hay, Kevin" uniqKey="Hay K" first="Kevin" last="Hay">Kevin Hay</name>
<affiliation wicri:level="2"><nlm:aff id="A3">Department of Immunology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Immunology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Rini, James M" sort="Rini, James M" uniqKey="Rini J" first="James M" last="Rini">James M. Rini</name>
<affiliation wicri:level="2"><nlm:aff id="A4">Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Departments of Molecular Genetics and Biochemistry; University of Toronto; Toronto</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Wang, Linfa" sort="Wang, Linfa" uniqKey="Wang L" first="Linfa" last="Wang">Linfa Wang</name>
<affiliation><nlm:aff id="A5">CSIRO Livestock Industries; Australian Animal Health Laboratory; Geelong, Victoria Australia</nlm:aff>
<wicri:noCountry code="subfield">Victoria Australia</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Plummer, Francis A" sort="Plummer, Francis A" uniqKey="Plummer F" first="Francis A" last="Plummer">Francis A. Plummer</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Corbett, Cindi R" sort="Corbett, Cindi R" uniqKey="Corbett C" first="Cindi R" last="Corbett">Cindi R. Corbett</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name>
<affiliation wicri:level="2"><nlm:aff id="A1">Department of Medical Microbiology; University of Manitoba; Winnipeg, CA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Department of Medical Microbiology; University of Manitoba; Winnipeg</wicri:cityArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="A2">National Microbiology Laboratory; Health Canada; Winnipeg, Canada</nlm:aff>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>National Microbiology Laboratory; Health Canada; Winnipeg</wicri:regionArea>
</affiliation>
</author>
</analytic>
<series><title level="j">mAbs</title>
<idno type="ISSN">1942-0862</idno>
<idno type="eISSN">1942-0870</idno>
<imprint><date when="2010">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Neutralizing antibody responses to the surface glycoproteins of enveloped viruses play an important role in immunity. Many of these glycoproteins, including the severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) protein form trimeric units in the membrane of the native virion. There is substantial experimental and pre-clinical evidence showing that the S protein is a promising lead for vaccines and therapeutics. Previously we generated a panel of monoclonal antibodies (mAbs) to whole inactivated SARS-CoV which neutralize the virus in vitro.<xref ref-type="bibr" rid="R1">1</xref>
,<xref ref-type="bibr" rid="R2">2</xref>
Here, we define their specificity and affinity, map several of their epitopes and lastly characterise chimeric versions of them. Our data show that the neutralizing mAbs bind to the angiotensin-converting enzyme 2 (ACE2) receptor-binding domain (RBD) of the SARS S protein. Three of the chimeric mAbs retain their binding specificity while one conformational mAb, F26G19, lost its ability to bind the S protein despite high level expression. The affinity for recombinant S is maintained in all of the functional chimeric versions of the parental mAbs. Both parental mAb F26G18 and the chimeric version neutralize the TOR2 strain of SARS-CoV with essentially identical titres (2.07 and 2.47 nM, respectively). Lastly, a comparison with other neutralizing mAbs to SARS-CoV clearly shows that the dominance of a 33 amino acid residue loop of the SARS-CoV RBD is independent of repertoire, species, quaternary structure, and importantly, the technology used to derive the mAbs. In cases like this, the dominance of a compact RBD antigenic domain and the central role of the S protein in pathogenesis may inherently create immunoselection pressure on viruses to evolve more complex evasion strategies or die out of a host species. The apparent simplicity of the mechanism of SARS-CoV neutralization is in stark contrast to the complexity shown by other enveloped viruses.</p>
</div>
</front>
</TEI>
</pmc>
<pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology.</title>
<author><name sortKey="Berry, Jody D" sort="Berry, Jody D" uniqKey="Berry J" first="Jody D" last="Berry">Jody D. Berry</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Medical Microbiology, University of Manitoba, Winnipeg, Canada. jberry@cangene.com</nlm:affiliation>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>Department of Medical Microbiology, University of Manitoba, Winnipeg</wicri:regionArea>
<orgName type="university">Université du Manitoba</orgName>
<placeName><settlement type="city">Winnipeg</settlement>
<region type="state">Manitoba</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Hay, Kevin" sort="Hay, Kevin" uniqKey="Hay K" first="Kevin" last="Hay">Kevin Hay</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>
<author><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name>
</author>
<author><name sortKey="Wang, Linfa" sort="Wang, Linfa" uniqKey="Wang L" first="Linfa" last="Wang">Linfa Wang</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="Corbett, Cindi R" sort="Corbett, Cindi R" uniqKey="Corbett C" first="Cindi R" last="Corbett">Cindi R. Corbett</name>
</author>
<author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="????"><PubDate><MedlineDate>2010 Jan-Feb</MedlineDate>
</PubDate>
</date>
<idno type="RBID">pubmed:20168090</idno>
<idno type="pmid">20168090</idno>
<idno type="doi">10.4161/mabs.2.1.10788</idno>
<idno type="wicri:Area/PubMed/Corpus">001746</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001746</idno>
<idno type="wicri:Area/PubMed/Curation">001746</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001746</idno>
<idno type="wicri:Area/PubMed/Checkpoint">003492</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">003492</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology.</title>
<author><name sortKey="Berry, Jody D" sort="Berry, Jody D" uniqKey="Berry J" first="Jody D" last="Berry">Jody D. Berry</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Medical Microbiology, University of Manitoba, Winnipeg, Canada. jberry@cangene.com</nlm:affiliation>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>Department of Medical Microbiology, University of Manitoba, Winnipeg</wicri:regionArea>
<orgName type="university">Université du Manitoba</orgName>
<placeName><settlement type="city">Winnipeg</settlement>
<region type="state">Manitoba</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Hay, Kevin" sort="Hay, Kevin" uniqKey="Hay K" first="Kevin" last="Hay">Kevin Hay</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>
<author><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name>
</author>
<author><name sortKey="Wang, Linfa" sort="Wang, Linfa" uniqKey="Wang L" first="Linfa" last="Wang">Linfa Wang</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="Corbett, Cindi R" sort="Corbett, Cindi R" uniqKey="Corbett C" first="Cindi R" last="Corbett">Cindi R. Corbett</name>
</author>
<author><name sortKey="Andonov, Anton" sort="Andonov, Anton" uniqKey="Andonov A" first="Anton" last="Andonov">Anton Andonov</name>
</author>
</analytic>
<series><title level="j">mAbs</title>
<idno type="eISSN">1942-0870</idno>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Antibodies, Monoclonal (chemistry)</term>
<term>Antibodies, Monoclonal (genetics)</term>
<term>Antibodies, Monoclonal (immunology)</term>
<term>Antibodies, Monoclonal (metabolism)</term>
<term>Antibodies, Neutralizing (chemistry)</term>
<term>Antibodies, Neutralizing (genetics)</term>
<term>Antibodies, Neutralizing (immunology)</term>
<term>Antibodies, Neutralizing (metabolism)</term>
<term>Antibody Affinity</term>
<term>Biomedical Technology</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Epitope Mapping</term>
<term>Humans</term>
<term>Immunodominant Epitopes (immunology)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Mice</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Receptor, Angiotensin, Type 2 (metabolism)</term>
<term>Receptors, Antigen, B-Cell (immunology)</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (immunology)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>SARS Virus (immunology)</term>
<term>Severe Acute Respiratory Syndrome (immunology)</term>
<term>Severe Acute Respiratory Syndrome (prevention & control)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (immunology)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Viral Vaccines</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Affinité des anticorps</term>
<term>Animaux</term>
<term>Anticorps monoclonaux ()</term>
<term>Anticorps monoclonaux (génétique)</term>
<term>Anticorps monoclonaux (immunologie)</term>
<term>Anticorps monoclonaux (métabolisme)</term>
<term>Anticorps neutralisants ()</term>
<term>Anticorps neutralisants (génétique)</term>
<term>Anticorps neutralisants (immunologie)</term>
<term>Anticorps neutralisants (métabolisme)</term>
<term>Cartographie épitopique</term>
<term>Conformation des protéines</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Protéines de fusion recombinantes ()</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (immunologie)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Récepteur de type 2 à l'angiotensine-II (métabolisme)</term>
<term>Récepteurs pour l'antigène des lymphocytes B (immunologie)</term>
<term>Souris</term>
<term>Syndrome respiratoire aigu sévère ()</term>
<term>Syndrome respiratoire aigu sévère (immunologie)</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Technologie biomédicale</term>
<term>Test ELISA</term>
<term>Vaccins antiviraux</term>
<term>Virus du SRAS (immunologie)</term>
<term>Épitopes immunodominants (immunologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Membrane Glycoproteins</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Immunodominant Epitopes</term>
<term>Membrane Glycoproteins</term>
<term>Receptors, Antigen, B-Cell</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Antibodies, Neutralizing</term>
<term>Membrane Glycoproteins</term>
<term>Receptor, Angiotensin, Type 2</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Protéines de fusion recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Récepteurs pour l'antigène des lymphocytes B</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Virus du SRAS</term>
<term>Épitopes immunodominants</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="métabolisme" xml:lang="fr"><term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Récepteur de type 2 à l'angiotensine-II</term>
</keywords>
<keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Antibody Affinity</term>
<term>Biomedical Technology</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Epitope Mapping</term>
<term>Humans</term>
<term>Mice</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Vaccines</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Affinité des anticorps</term>
<term>Animaux</term>
<term>Anticorps monoclonaux</term>
<term>Anticorps neutralisants</term>
<term>Cartographie épitopique</term>
<term>Conformation des protéines</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Souris</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Technologie biomédicale</term>
<term>Test ELISA</term>
<term>Vaccins antiviraux</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Neutralizing antibody responses to the surface glycoproteins of enveloped viruses play an important role in immunity. Many of these glycoproteins, including the severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) protein form trimeric units in the membrane of the native virion. There is substantial experimental and pre-clinical evidence showing that the S protein is a promising lead for vaccines and therapeutics. Previously we generated a panel of monoclonal antibodies (mAbs) to whole inactivated SARS-CoV which neutralize the virus in vitro. Here, we define their specificity and affinity, map several of their epitopes and lastly characterise chimeric versions of them. Our data show that the neutralizing mAbs bind to the angiotensin-converting enzyme 2 (ACE2) receptor-binding domain (RBD) of the SARS S protein. Three of the chimeric mAbs retain their binding specificity while one conformational mAb, F26G19, lost its ability to bind the S protein despite high level expression. The affinity for recombinant S is maintained in all of the functional chimeric versions of the parental mAbs. Both parental mAb F26G18 and the chimeric version neutralize the TO R2 strain of SARS-CoV with essentially identical titres (2.07 and 2.47 nM, respectively). Lastly, a comparison with other neutralizing mAbs to SARS-CoV clearly shows that the dominance of a 33 amino acid residue loop of the SARS-CoV RBD is independent of repertoire, species, quaternary structure, and importantly, the technology used to derive the mAbs. In cases like this, the dominance of a compact RBD antigenic domain and the central role of the S protein in pathogenesis may inherently create immunoselection pressure on viruses to evolve more complex evasion strategies or die out of a host species. The apparent simplicity of the mechanism of SARS-CoV neutralization is in stark contrast to the complexity shown by other enveloped viruses.</div>
</front>
</TEI>
</pubmed>
</double>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002083 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 002083 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= Ncbi |étape= Merge |type= RBID |clé= PMC:2828578 |texte= Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i -Sk "pubmed:20168090" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |