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A human neutralizing antibody against a conformational epitope shared by oligomeric SARS S1 protein.

Identifieur interne : 004009 ( Main/Exploration ); précédent : 004008; suivant : 004010

A human neutralizing antibody against a conformational epitope shared by oligomeric SARS S1 protein.

Auteurs : Jinzhu Duan [République populaire de Chine] ; Xin Ji ; Jing Feng ; Wei Han ; Panhe Zhang ; Wuchun Cao ; Xueming Guo ; Cai Qi ; Dongling Yang ; Gang Jin ; Guangxia Gao ; Xiyun Yan

Source :

RBID : pubmed:16518967

Descripteurs français

English descriptors

Abstract

An antibody phage-display library was constructed from the B cells of convalescent severe acute respiratory syndrome (SARS) patients and screened using inactivated SARS coronavirus (CoV) virions as antigens. More than 80 positive clones were isolated from the library and one of them, scFv H12, was extensively characterized. scFv H12 bound to SARS-CoV with high affinity (equilibrium dissociation constant, Kd=73.5 nM), and neutralized SARS virions in vitro. The facts that scFv H12 bound to the SARS-S1 protein under non-reducing conditions and that it did not bind to monomeric S1 protein under reducing conditions strongly suggest that scFv H12 recognizes a conformational epitope shared by oligomeric S1 proteins. This study should aid in the manufacture of neutralizing antibody, provide a better understanding the immunological characteristics of SARS protein and facilitate the design of a SARS vaccine.

PubMed: 16518967


Affiliations:


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Le document en format XML

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<term>Antibodies, Viral (immunology)</term>
<term>Chlorocebus aethiops</term>
<term>Dimerization</term>
<term>Epitopes (chemistry)</term>
<term>Epitopes (immunology)</term>
<term>Humans</term>
<term>Immunoglobulin Fragments (chemistry)</term>
<term>Immunoglobulin Fragments (immunology)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Molecular Sequence Data</term>
<term>Neutralization Tests</term>
<term>Peptide Library</term>
<term>Protein Conformation</term>
<term>SARS Virus (immunology)</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (immunology)</term>
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<term>Animaux</term>
<term>Anticorps antiviraux (immunologie)</term>
<term>Banque de peptides</term>
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<term>Conformation des protéines</term>
<term>Dimérisation</term>
<term>Données de séquences moléculaires</term>
<term>Fragments d'immunoglobuline ()</term>
<term>Fragments d'immunoglobuline (immunologie)</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Humains</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
<term>Séquence d'acides aminés</term>
<term>Tests de neutralisation</term>
<term>Virus du SRAS (immunologie)</term>
<term>Épitopes ()</term>
<term>Épitopes (immunologie)</term>
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<term>Immunoglobulin Fragments</term>
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<term>Epitopes</term>
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<term>Fragments d'immunoglobuline</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus du SRAS</term>
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<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Dimerization</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Neutralization Tests</term>
<term>Peptide Library</term>
<term>Protein Conformation</term>
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<term>Banque de peptides</term>
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<term>Données de séquences moléculaires</term>
<term>Fragments d'immunoglobuline</term>
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<front>
<div type="abstract" xml:lang="en">An antibody phage-display library was constructed from the B cells of convalescent severe acute respiratory syndrome (SARS) patients and screened using inactivated SARS coronavirus (CoV) virions as antigens. More than 80 positive clones were isolated from the library and one of them, scFv H12, was extensively characterized. scFv H12 bound to SARS-CoV with high affinity (equilibrium dissociation constant, Kd=73.5 nM), and neutralized SARS virions in vitro. The facts that scFv H12 bound to the SARS-S1 protein under non-reducing conditions and that it did not bind to monomeric S1 protein under reducing conditions strongly suggest that scFv H12 recognizes a conformational epitope shared by oligomeric S1 proteins. This study should aid in the manufacture of neutralizing antibody, provide a better understanding the immunological characteristics of SARS protein and facilitate the design of a SARS vaccine.</div>
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