Identification and characterization of novel neutralizing epitopes in the receptor-binding domain of SARS-CoV spike protein: revealing the critical antigenic determinants in inactivated SARS-CoV vaccine.
Identifieur interne : 003E69 ( Main/Exploration ); précédent : 003E68; suivant : 003E70Identification and characterization of novel neutralizing epitopes in the receptor-binding domain of SARS-CoV spike protein: revealing the critical antigenic determinants in inactivated SARS-CoV vaccine.
Auteurs : Yuxian He [États-Unis] ; Jingjing Li ; Lanying Du ; Xuxia Yan ; Guangan Hu ; Yusen Zhou ; Shibo JiangSource :
- Vaccine [ 0264-410X ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antiviraux (sang), Anticorps monoclonaux (immunologie), Antigènes viraux (), Antigènes viraux (immunologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (immunologie), Liaison aux protéines, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (immunologie), Souris, Structure tertiaire des protéines, Tests de neutralisation, Vaccins antiviraux (immunologie), Virus du SRAS (), Virus du SRAS (immunologie), Épitopes (), Épitopes (immunologie).
- MESH :
- immunologie : Anticorps monoclonaux, Antigènes viraux, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Vaccins antiviraux, Virus du SRAS, Épitopes.
- sang : Anticorps antiviraux.
- Animaux, Antigènes viraux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Liaison aux protéines, Protéines de l'enveloppe virale, Souris, Structure tertiaire des protéines, Tests de neutralisation, Virus du SRAS, Épitopes.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antibodies, Viral (blood), Antigens, Viral (chemistry), Antigens, Viral (immunology), Epitopes (chemistry), Epitopes (immunology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Mice, Neutralization Tests, Protein Binding, Protein Structure, Tertiary, SARS Virus (chemistry), SARS Virus (immunology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology), Viral Vaccines (immunology).
- MESH :
- chemical , blood : Antibodies, Viral.
- chemical , chemistry : Antigens, Viral, Epitopes, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antigens, Viral, Epitopes, Membrane Glycoproteins, Viral Envelope Proteins, Viral Vaccines.
- chemistry : SARS Virus.
- immunology : SARS Virus.
- Animals, Mice, Neutralization Tests, Protein Binding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus.
Abstract
The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) is considered as a major antigen for vaccine design. We previously demonstrated that the receptor-binding domain (RBD: residues 318-510) of S protein contains multiple conformation-dependent neutralizing epitopes (Conf I to VI) and serves as a major target of SARS-CoV neutralization. Here, we further characterized the antigenic structure in the RBD by a panel of novel mAbs isolated from the mice immunized with an inactivated SARS-CoV vaccine. Ten of the RBD-specific mAbs were mapped to four distinct groups of conformational epitopes (designated Group A to D), and all of which had potent neutralizing activity against S protein-pseudotyped SARS viruses. Group A, B, C mAbs target the epitopes that may overlap with the previously characterized Conf I, III, and VI respectively, but they display different capacity to block the receptor binding. Group D mAb (S25) was directed against a unique epitope by its competitive binding. Two anti-RBD mAbs recognizing the linear epitopes (Group E) were mapped to the RBD residues 335-352 and 442-458, respectively, and none of them inhibited the receptor binding and virus entry. Surprisingly, most neutralizing epitopes (Groups A to C) could be completely disrupted by single amino acid substitutions (e.g., D429A, R441A or D454A) or by deletions of several amino acids at the N-terminal or C-terminal region of the RBD; however, the Group D epitope was not sensitive to the mutations, highlighting its importance for vaccine development. These data provide important information for understanding the antigenicity and immunogenicity of SARS-CoV, and this panel of novel mAbs can be used as tools for studying the structure of S protein and for guiding SARS vaccine design.
DOI: 10.1016/j.vaccine.2006.04.054
PubMed: 16725238
Affiliations:
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Le document en format XML
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<term>Antigens, Viral (chemistry)</term>
<term>Antigens, Viral (immunology)</term>
<term>Epitopes (chemistry)</term>
<term>Epitopes (immunology)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Mice</term>
<term>Neutralization Tests</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (immunology)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (immunology)</term>
<term>Viral Vaccines (immunology)</term>
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<term>Anticorps monoclonaux (immunologie)</term>
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<term>Antigènes viraux (immunologie)</term>
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<term>Protéines de l'enveloppe virale (immunologie)</term>
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<term>Structure tertiaire des protéines</term>
<term>Tests de neutralisation</term>
<term>Vaccins antiviraux (immunologie)</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (immunologie)</term>
<term>Épitopes ()</term>
<term>Épitopes (immunologie)</term>
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<term>Epitopes</term>
<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<term>Epitopes</term>
<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Vaccines</term>
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<front><div type="abstract" xml:lang="en">The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) is considered as a major antigen for vaccine design. We previously demonstrated that the receptor-binding domain (RBD: residues 318-510) of S protein contains multiple conformation-dependent neutralizing epitopes (Conf I to VI) and serves as a major target of SARS-CoV neutralization. Here, we further characterized the antigenic structure in the RBD by a panel of novel mAbs isolated from the mice immunized with an inactivated SARS-CoV vaccine. Ten of the RBD-specific mAbs were mapped to four distinct groups of conformational epitopes (designated Group A to D), and all of which had potent neutralizing activity against S protein-pseudotyped SARS viruses. Group A, B, C mAbs target the epitopes that may overlap with the previously characterized Conf I, III, and VI respectively, but they display different capacity to block the receptor binding. Group D mAb (S25) was directed against a unique epitope by its competitive binding. Two anti-RBD mAbs recognizing the linear epitopes (Group E) were mapped to the RBD residues 335-352 and 442-458, respectively, and none of them inhibited the receptor binding and virus entry. Surprisingly, most neutralizing epitopes (Groups A to C) could be completely disrupted by single amino acid substitutions (e.g., D429A, R441A or D454A) or by deletions of several amino acids at the N-terminal or C-terminal region of the RBD; however, the Group D epitope was not sensitive to the mutations, highlighting its importance for vaccine development. These data provide important information for understanding the antigenicity and immunogenicity of SARS-CoV, and this panel of novel mAbs can be used as tools for studying the structure of S protein and for guiding SARS vaccine design.</div>
</front>
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<name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name>
<name sortKey="Li, Jingjing" sort="Li, Jingjing" uniqKey="Li J" first="Jingjing" last="Li">Jingjing Li</name>
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