Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: implications for the functional roles of S2 subunit.
Identifieur interne : 003D58 ( Main/Exploration ); précédent : 003D57; suivant : 003D59Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: implications for the functional roles of S2 subunit.
Auteurs : Fanya Zeng [République populaire de Chine] ; Chung Chau Hon ; Chi Wai Yip ; Ka Man Law ; Yin Shan Yeung ; Kwok Hung Chan ; Joseph S. Malik Peiris ; Frederick Chi Ching LeungSource :
- FEBS letters [ 0014-5793 ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antiviraux (immunologie), Anticorps antiviraux (pharmacologie), Cricetinae, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Liaison aux protéines, Lignée cellulaire, Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Souris, Sous-unités de protéines (immunologie), Sous-unités de protéines (métabolisme), Virus du SRAS (), Virus du SRAS (immunologie), Épitopes (immunologie).
- MESH :
- immunologie : Anticorps antiviraux, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Sous-unités de protéines, Virus du SRAS, Épitopes.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Sous-unités de protéines.
- pharmacologie : Anticorps antiviraux.
- Animaux, Cricetinae, Glycoprotéine de spicule des coronavirus, Liaison aux protéines, Lignée cellulaire, Souris, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Antibodies, Viral (immunology), Antibodies, Viral (pharmacology), Cell Line, Chlorocebus aethiops, Cricetinae, Epitopes (immunology), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Mice, Protein Binding, Protein Subunits (immunology), Protein Subunits (metabolism), SARS Virus (drug effects), SARS Virus (immunology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , immunology : Antibodies, Viral, Epitopes, Membrane Glycoproteins, Protein Subunits, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Protein Subunits, Viral Envelope Proteins.
- chemical , pharmacology : Antibodies, Viral.
- drug effects : SARS Virus.
- immunology : SARS Virus.
- Animals, Cell Line, Chlorocebus aethiops, Cricetinae, Mice, Protein Binding, Spike Glycoprotein, Coronavirus.
Abstract
Neutralizing effects of antibodies targeting the C-terminal stalk (S2) subunit of the spike protein of severe acute respiratory syndrome coronavirus have previously been reported, although its mechanism remained elusive. In this study, high titered mouse antisera against the N-terminal globular (S1) and S2 subunits of the S protein were generated and total immunoglobulin G (IgG) was purified from these antisera. The efficiency of these purified IgGs in virus neutralization and blocking of receptor binding were compared quantitatively using virus neutralization assay and a previously developed cell-based receptor binding assay, respectively. We demonstrated that anti-S1 IgG neutralizes the virus and binds to the membrane associated S protein more efficiently than anti-S2 IgG does. Moreover, both anti-S1 and anti-S2 IgGs were able to abolish the binding between S protein and its cellular receptor(s), although anti-S1 IgG showed a significantly higher blocking efficiency. The unexpected blocking ability of anti-S2 IgG towards the receptor binding implied a possible role of the S2 subunit in virus docking process and argues against the current hypothesis of viral entry. On the other hand, the functional roles of the previously reported neutralizing epitopes within S2 subunit were investigated using an antigen specific antibody depletion assay. Depletion of antibodies against these regions significantly diminished, though not completely abolished, the neutralizing effects of anti-S2 IgG. It suggests the absence of a major neutralizing domain on S2 protein. The possible ways of anti-S2 IgGs to abolish the receptor binding and the factors restricting anti-S2 IgGs to neutralize the virus are discussed.
DOI: 10.1016/j.febslet.2006.08.085
PubMed: 16989815
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002084
- to stream PubMed, to step Curation: 002084
- to stream PubMed, to step Checkpoint: 002046
- to stream Ncbi, to step Merge: 001665
- to stream Ncbi, to step Curation: 001665
- to stream Ncbi, to step Checkpoint: 001665
- to stream Main, to step Merge: 003F31
- to stream Main, to step Curation: 003D58
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: implications for the functional roles of S2 subunit.</title><author><name sortKey="Zeng, Fanya" sort="Zeng, Fanya" uniqKey="Zeng F" first="Fanya" last="Zeng">Fanya Zeng</name><affiliation wicri:level="1"><nlm:affiliation>Department of Zoology, Kadoorie Biological Science Building, The University of Hong Kong, Pokfulam Road, Hong Kong, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Zoology, Kadoorie Biological Science Building, The University of Hong Kong, Pokfulam Road, Hong Kong</wicri:regionArea><wicri:noRegion>Hong Kong</wicri:noRegion></affiliation></author><author><name sortKey="Hon, Chung Chau" sort="Hon, Chung Chau" uniqKey="Hon C" first="Chung Chau" last="Hon">Chung Chau Hon</name></author><author><name sortKey="Yip, Chi Wai" sort="Yip, Chi Wai" uniqKey="Yip C" first="Chi Wai" last="Yip">Chi Wai Yip</name></author><author><name sortKey="Law, Ka Man" sort="Law, Ka Man" uniqKey="Law K" first="Ka Man" last="Law">Ka Man Law</name></author><author><name sortKey="Yeung, Yin Shan" sort="Yeung, Yin Shan" uniqKey="Yeung Y" first="Yin Shan" last="Yeung">Yin Shan Yeung</name></author><author><name sortKey="Chan, Kwok Hung" sort="Chan, Kwok Hung" uniqKey="Chan K" first="Kwok Hung" last="Chan">Kwok Hung Chan</name></author><author><name sortKey="Malik Peiris, Joseph S" sort="Malik Peiris, Joseph S" uniqKey="Malik Peiris J" first="Joseph S" last="Malik Peiris">Joseph S. Malik Peiris</name></author><author><name sortKey="Leung, Frederick Chi Ching" sort="Leung, Frederick Chi Ching" uniqKey="Leung F" first="Frederick Chi Ching" last="Leung">Frederick Chi Ching Leung</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16989815</idno><idno type="pmid">16989815</idno><idno type="doi">10.1016/j.febslet.2006.08.085</idno><idno type="wicri:Area/PubMed/Corpus">002084</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002084</idno><idno type="wicri:Area/PubMed/Curation">002084</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002084</idno><idno type="wicri:Area/PubMed/Checkpoint">002046</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002046</idno><idno type="wicri:Area/Ncbi/Merge">001665</idno><idno type="wicri:Area/Ncbi/Curation">001665</idno><idno type="wicri:Area/Ncbi/Checkpoint">001665</idno><idno type="wicri:doubleKey">0014-5793:2006:Zeng F:quantitative:comparison:of</idno><idno type="wicri:Area/Main/Merge">003F31</idno><idno type="wicri:Area/Main/Curation">003D58</idno><idno type="wicri:Area/Main/Exploration">003D58</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: implications for the functional roles of S2 subunit.</title><author><name sortKey="Zeng, Fanya" sort="Zeng, Fanya" uniqKey="Zeng F" first="Fanya" last="Zeng">Fanya Zeng</name><affiliation wicri:level="1"><nlm:affiliation>Department of Zoology, Kadoorie Biological Science Building, The University of Hong Kong, Pokfulam Road, Hong Kong, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Zoology, Kadoorie Biological Science Building, The University of Hong Kong, Pokfulam Road, Hong Kong</wicri:regionArea><wicri:noRegion>Hong Kong</wicri:noRegion></affiliation></author><author><name sortKey="Hon, Chung Chau" sort="Hon, Chung Chau" uniqKey="Hon C" first="Chung Chau" last="Hon">Chung Chau Hon</name></author><author><name sortKey="Yip, Chi Wai" sort="Yip, Chi Wai" uniqKey="Yip C" first="Chi Wai" last="Yip">Chi Wai Yip</name></author><author><name sortKey="Law, Ka Man" sort="Law, Ka Man" uniqKey="Law K" first="Ka Man" last="Law">Ka Man Law</name></author><author><name sortKey="Yeung, Yin Shan" sort="Yeung, Yin Shan" uniqKey="Yeung Y" first="Yin Shan" last="Yeung">Yin Shan Yeung</name></author><author><name sortKey="Chan, Kwok Hung" sort="Chan, Kwok Hung" uniqKey="Chan K" first="Kwok Hung" last="Chan">Kwok Hung Chan</name></author><author><name sortKey="Malik Peiris, Joseph S" sort="Malik Peiris, Joseph S" uniqKey="Malik Peiris J" first="Joseph S" last="Malik Peiris">Joseph S. Malik Peiris</name></author><author><name sortKey="Leung, Frederick Chi Ching" sort="Leung, Frederick Chi Ching" uniqKey="Leung F" first="Frederick Chi Ching" last="Leung">Frederick Chi Ching Leung</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Viral (immunology)</term><term>Antibodies, Viral (pharmacology)</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Cricetinae</term><term>Epitopes (immunology)</term><term>Membrane Glycoproteins (immunology)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Protein Binding</term><term>Protein Subunits (immunology)</term><term>Protein Subunits (metabolism)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (immunology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (immunology)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps antiviraux (immunologie)</term><term>Anticorps antiviraux (pharmacologie)</term><term>Cricetinae</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (immunologie)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines de l'enveloppe virale (immunologie)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Souris</term><term>Sous-unités de protéines (immunologie)</term><term>Sous-unités de protéines (métabolisme)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (immunologie)</term><term>Épitopes (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Viral</term><term>Epitopes</term><term>Membrane Glycoproteins</term><term>Protein Subunits</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Protein Subunits</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Sous-unités de protéines</term><term>Virus du SRAS</term><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Anticorps antiviraux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Cricetinae</term><term>Mice</term><term>Protein Binding</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cricetinae</term><term>Glycoprotéine de spicule des coronavirus</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Souris</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Neutralizing effects of antibodies targeting the C-terminal stalk (S2) subunit of the spike protein of severe acute respiratory syndrome coronavirus have previously been reported, although its mechanism remained elusive. In this study, high titered mouse antisera against the N-terminal globular (S1) and S2 subunits of the S protein were generated and total immunoglobulin G (IgG) was purified from these antisera. The efficiency of these purified IgGs in virus neutralization and blocking of receptor binding were compared quantitatively using virus neutralization assay and a previously developed cell-based receptor binding assay, respectively. We demonstrated that anti-S1 IgG neutralizes the virus and binds to the membrane associated S protein more efficiently than anti-S2 IgG does. Moreover, both anti-S1 and anti-S2 IgGs were able to abolish the binding between S protein and its cellular receptor(s), although anti-S1 IgG showed a significantly higher blocking efficiency. The unexpected blocking ability of anti-S2 IgG towards the receptor binding implied a possible role of the S2 subunit in virus docking process and argues against the current hypothesis of viral entry. On the other hand, the functional roles of the previously reported neutralizing epitopes within S2 subunit were investigated using an antigen specific antibody depletion assay. Depletion of antibodies against these regions significantly diminished, though not completely abolished, the neutralizing effects of anti-S2 IgG. It suggests the absence of a major neutralizing domain on S2 protein. The possible ways of anti-S2 IgGs to abolish the receptor binding and the factors restricting anti-S2 IgGs to neutralize the virus are discussed.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Chan, Kwok Hung" sort="Chan, Kwok Hung" uniqKey="Chan K" first="Kwok Hung" last="Chan">Kwok Hung Chan</name><name sortKey="Hon, Chung Chau" sort="Hon, Chung Chau" uniqKey="Hon C" first="Chung Chau" last="Hon">Chung Chau Hon</name><name sortKey="Law, Ka Man" sort="Law, Ka Man" uniqKey="Law K" first="Ka Man" last="Law">Ka Man Law</name><name sortKey="Leung, Frederick Chi Ching" sort="Leung, Frederick Chi Ching" uniqKey="Leung F" first="Frederick Chi Ching" last="Leung">Frederick Chi Ching Leung</name><name sortKey="Malik Peiris, Joseph S" sort="Malik Peiris, Joseph S" uniqKey="Malik Peiris J" first="Joseph S" last="Malik Peiris">Joseph S. Malik Peiris</name><name sortKey="Yeung, Yin Shan" sort="Yeung, Yin Shan" uniqKey="Yeung Y" first="Yin Shan" last="Yeung">Yin Shan Yeung</name><name sortKey="Yip, Chi Wai" sort="Yip, Chi Wai" uniqKey="Yip C" first="Chi Wai" last="Yip">Chi Wai Yip</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Zeng, Fanya" sort="Zeng, Fanya" uniqKey="Zeng F" first="Fanya" last="Zeng">Fanya Zeng</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003D58 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003D58 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:16989815
|texte= Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: implications for the functional roles of S2 subunit.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:16989815" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |