SrasV1, Main, Merge, bibRecord, 002526

Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology

Identifieur interne : 002526 ( Main/Merge ); précédent : 002525; suivant : 002527

Neutralizing 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.

RBID : PMC:2828578

Descripteurs français

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.1,2 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.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2828578

PubMed: 20168090
PubMed Central: 2828578

Links to Exploration step

PMC:2828578

Le document en format XML

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<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>
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Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology

Neutralizing epitopes of the SARS-CoV S-protein cluster independent of repertoire, antigen structure or mAb technology

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