SrasV1, Hal, Checkpoint, bibRecord, 000169

Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.

Identifieur interne : 000169 ( Hal/Checkpoint ); précédent : 000168; suivant : 000170

Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.

Auteurs : Yiu Wing Kam [Hong Kong] ; François Kien [Hong Kong] ; Anjeanette Roberts [États-Unis] ; Yan Chung Cheung [République populaire de Chine] ; Elaine W. Lamirande [États-Unis] ; Leatrice Vogel [États-Unis] ; Shui Ling Chu [Hong Kong] ; Jane Tse [Hong Kong] ; Jeannette Guarner [États-Unis] ; Sherif R. Zaki [États-Unis] ; Kanta Subbarao [États-Unis] ; Malik Peiris [République populaire de Chine] ; Béatrice Nal [Hong Kong] ; Ralf Altmeyer [Singapour]

Source :

Vaccine [ 0264-410X ] ; 2007-01-08.

RBID : Hal:pasteur-00589034

Abstract

Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory syndrome coronavirus (SARS-CoV) was able to elicit a neutralizing and protective immune response in animals and analyzed the capacity of anti-S antibodies to mediate antibody-dependent enhancement (ADE) of virus entry in vitro and enhancement of replication in vivo. SARS-CoV-specific serum and mucosal immunoglobulins were readily detected in immunized animals. Serum IgG blocked binding of the S-protein to the ACE2 receptor and neutralized SARS-CoV infection in vitro. Entry into human B cell lines occurred in a FcgammaRII-dependent and ACE2-independent fashion indicating that ADE of virus entry is a novel cell entry mechanism of SARS-CoV. Vaccinated animals showed no signs of enhanced lung pathology or hepatitis and viral load was undetectable or greatly reduced in lungs following challenge with SARS-CoV. Altogether our results indicate that a recombinant trimeric S protein was able to elicit an efficacious protective immune response in vivo and warrant concern in the safety evaluation of a human vaccine against SARS-CoV.

Url:

https://hal-riip.archives-ouvertes.fr/pasteur-00589034

DOI: 10.1016/j.vaccine.2006.08.011

Links toward previous steps (curation, corpus...)

to stream Hal, to step Corpus: 000017
to stream Hal, to step Curation: 000017

Links to Exploration step

Hal:pasteur-00589034

Le document en format XML

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</analytic>
<idno type="DOI">10.1016/j.vaccine.2006.08.011</idno>
<series><title level="j">Vaccine</title>
<idno type="ISSN">0264-410X</idno>
<imprint><date type="datePub">2007-01-08</date>
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<front><div type="abstract" xml:lang="en">              <p>Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory syndrome coronavirus (SARS-CoV) was able to elicit a neutralizing and protective immune response in animals and analyzed the capacity of anti-S antibodies to mediate antibody-dependent enhancement (ADE) of virus entry in vitro and enhancement of replication in vivo. SARS-CoV-specific serum and mucosal immunoglobulins were readily detected in immunized animals. Serum IgG blocked binding of the S-protein to the ACE2 receptor and neutralized SARS-CoV infection in vitro. Entry into human B cell lines occurred in a FcgammaRII-dependent and ACE2-independent fashion indicating that ADE of virus entry is a novel cell entry mechanism of SARS-CoV. Vaccinated animals showed no signs of enhanced lung pathology or hepatitis and viral load was undetectable or greatly reduced in lungs following challenge with SARS-CoV. Altogether our results indicate that a recombinant trimeric S protein was able to elicit an efficacious protective immune response in vivo and warrant concern in the safety evaluation of a human vaccine against SARS-CoV.</p>
            </div>
</front>
</TEI>
<hal api="V3">          <titleStmt>            <title xml:lang="en">Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.</title>
            <author role="crp">              <persName>                <forename type="first">Yiu Wing</forename>
                <surname>Kam</surname>
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            <author role="aut">              <persName>                <forename type="first">François</forename>
                <surname>Kien</surname>
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            <author role="aut">              <persName>                <forename type="first">Yan Chung</forename>
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            <author role="aut">              <persName>                <forename type="first">Sherif R</forename>
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          </titleStmt>
          <editionStmt>            <edition n="v1" type="current">              <date type="whenSubmitted">2011-04-27 11:42:08</date>
              <date type="whenModified">2019-12-04 11:14:05</date>
              <date type="whenReleased">2011-07-07 15:13:49</date>
              <date type="whenProduced">2007-01-08</date>
              <date type="whenEndEmbargoed">9999-12-31</date>
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              <name key="157033">                <persName>                  <forename>Francois</forename>
                  <surname>Kien</surname>
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            <idno type="halRefHtml">Vaccine, Elsevier, 2007, 25 (4), pp.729-40. ⟨10.1016/j.vaccine.2006.08.011⟩</idno>
            <idno type="halRef">Vaccine, Elsevier, 2007, 25 (4), pp.729-40. ⟨10.1016/j.vaccine.2006.08.011⟩</idno>
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            <idno type="stamp" n="RIIP_HONGKONG" corresp="RIIP">Centre de Recherche Université de Hong-Kong-Pasteur</idno>
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          <notesStmt>            <note type="audience" n="2">International</note>
            <note type="popular" n="0">No</note>
            <note type="peer" n="1">Yes</note>
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          <sourceDesc>            <biblStruct>              <analytic>                <title xml:lang="en">Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.</title>
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                <author role="aut">                  <persName>                    <forename type="first">Yan Chung</forename>
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                  </persName>
                  <idno type="halauthorid">603764</idno>
                  <affiliation ref="#struct-215584"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Sherif R</forename>
                    <surname>Zaki</surname>
                  </persName>
                  <idno type="halauthorid">603765</idno>
                  <affiliation ref="#struct-215584"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Kanta</forename>
                    <surname>Subbarao</surname>
                  </persName>
                  <idno type="halauthorid">603766</idno>
                  <affiliation ref="#struct-161188"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Malik</forename>
                    <surname>Peiris</surname>
                  </persName>
                  <idno type="halauthorid">400952</idno>
                  <affiliation ref="#struct-136023"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Béatrice</forename>
                    <surname>Nal</surname>
                  </persName>
                  <idno type="halauthorid">170857</idno>
                  <affiliation ref="#struct-55925"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Ralf</forename>
                    <surname>Altmeyer</surname>
                  </persName>
                  <idno type="halauthorid">201745</idno>
                  <affiliation ref="#struct-161190"></affiliation>
                </author>
              </analytic>
              <monogr>                <idno type="halJournalId" status="VALID">19820</idno>
                <idno type="issn">0264-410X</idno>
                <idno type="eissn">0264-410X</idno>
                <title level="j">Vaccine</title>
                <imprint>                  <publisher>Elsevier</publisher>
                  <biblScope unit="volume">25</biblScope>
                  <biblScope unit="issue">4</biblScope>
                  <biblScope unit="pp">729-40</biblScope>
                  <date type="datePub">2007-01-08</date>
                  <date type="dateEpub">2006-08-22</date>
                </imprint>
              </monogr>
              <idno type="doi">10.1016/j.vaccine.2006.08.011</idno>
              <idno type="pubmed">17049691</idno>
            </biblStruct>
          </sourceDesc>
          <profileDesc>            <langUsage>              <language ident="en">English</language>
            </langUsage>
            <textClass>              <classCode scheme="mesh">Animals</classCode>
              <classCode scheme="mesh">Antibodies, Viral</classCode>
              <classCode scheme="mesh">Receptors, IgG</classCode>
              <classCode scheme="mesh">SARS Virus</classCode>
              <classCode scheme="mesh">Severe Acute Respiratory Syndrome</classCode>
              <classCode scheme="mesh">Viral Envelope Proteins</classCode>
              <classCode scheme="mesh">B-Lymphocytes</classCode>
              <classCode scheme="mesh">Cricetinae</classCode>
              <classCode scheme="mesh">Dose-Response Relationship, Drug</classCode>
              <classCode scheme="mesh">Immunity, Mucosal</classCode>
              <classCode scheme="mesh">Immunoglobulin A</classCode>
              <classCode scheme="mesh">Immunoglobulin G</classCode>
              <classCode scheme="mesh">Membrane Glycoproteins</classCode>
              <classCode scheme="mesh">Mice</classCode>
              <classCode scheme="halDomain" n="sdv.mp.vir">Life Sciences [q-bio]/Microbiology and Parasitology/Virology</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
            </textClass>
            <abstract xml:lang="en">              <p>Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory syndrome coronavirus (SARS-CoV) was able to elicit a neutralizing and protective immune response in animals and analyzed the capacity of anti-S antibodies to mediate antibody-dependent enhancement (ADE) of virus entry in vitro and enhancement of replication in vivo. SARS-CoV-specific serum and mucosal immunoglobulins were readily detected in immunized animals. Serum IgG blocked binding of the S-protein to the ACE2 receptor and neutralized SARS-CoV infection in vitro. Entry into human B cell lines occurred in a FcgammaRII-dependent and ACE2-independent fashion indicating that ADE of virus entry is a novel cell entry mechanism of SARS-CoV. Vaccinated animals showed no signs of enhanced lung pathology or hepatitis and viral load was undetectable or greatly reduced in lungs following challenge with SARS-CoV. Altogether our results indicate that a recombinant trimeric S protein was able to elicit an efficacious protective immune response in vivo and warrant concern in the safety evaluation of a human vaccine against SARS-CoV.</p>
            </abstract>
          </profileDesc>
        </hal>
</record>

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Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.

Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.

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