Serveur d'exploration SRAS

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Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus : Insight into the humoral immunity of SARS

Identifieur interne : 000358 ( PascalFrancis/Curation ); précédent : 000357; suivant : 000359

Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus : Insight into the humoral immunity of SARS

Auteurs : YUNFEI LIANG [République populaire de Chine] ; YING WAN [République populaire de Chine] ; Li-Wen Qiu [République populaire de Chine] ; JINGRAN ZHOU [République populaire de Chine] ; BING NI [République populaire de Chine] ; BO GUO [République populaire de Chine] ; QIANG ZOU [République populaire de Chine] ; LIYUN ZOU [République populaire de Chine] ; WEI ZHOU [République populaire de Chine] ; ZHENGCAI JIA [République populaire de Chine] ; Xiao-Yan Che [République populaire de Chine] ; YUZHANG WU [République populaire de Chine]

Source :

RBID : Pascal:05-0347652

Descripteurs français

English descriptors

Abstract

Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.
pA  
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A11 02  1    @1 YING WAN
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A11 05  1    @1 BING NI
A11 06  1    @1 BO GUO
A11 07  1    @1 QIANG ZOU
A11 08  1    @1 LIYUN ZOU
A11 09  1    @1 WEI ZHOU
A11 10  1    @1 ZHENGCAI JIA
A11 11  1    @1 CHE (Xiao-Yan)
A11 12  1    @1 YUZHANG WU
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C01 01    ENG  @0 Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.
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C03 03  X  FRE  @0 Cartographie @5 05
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C03 04  X  FRE  @0 Nucléocapside @5 06
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N21       @1 241
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Le document en format XML

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<name sortKey="Liyun Zou" sort="Liyun Zou" uniqKey="Liyun Zou" last="Liyun Zou">LIYUN ZOU</name>
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<name sortKey="Wei Zhou" sort="Wei Zhou" uniqKey="Wei Zhou" last="Wei Zhou">WEI ZHOU</name>
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<name sortKey="Zhengcai Jia" sort="Zhengcai Jia" uniqKey="Zhengcai Jia" last="Zhengcai Jia">ZHENGCAI JIA</name>
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<name sortKey="Che, Xiao Yan" sort="Che, Xiao Yan" uniqKey="Che X" first="Xiao-Yan" last="Che">Xiao-Yan Che</name>
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<s1>Central Laboratory, Zhujiang Hospital, The Southern Medical University</s1>
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<name sortKey="Yuzhang Wu" sort="Yuzhang Wu" uniqKey="Yuzhang Wu" last="Yuzhang Wu">YUZHANG WU</name>
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<title level="j" type="main">Clinical chemistry : (Baltimore, Md.)</title>
<title level="j" type="abbreviated">Clin. chem. : (Baltim. Md.)</title>
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<idno type="ISSN">0009-9147</idno>
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<term>Antibody</term>
<term>Antigenic determinant</term>
<term>Biochemistry</term>
<term>Cartography</term>
<term>Clinical biology</term>
<term>Coronavirus</term>
<term>Humoral immunity</term>
<term>Molecular biology</term>
<term>Nucleocapsid</term>
<term>Protein</term>
<term>Severe acute respiratory syndrome</term>
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<term>Anticorps</term>
<term>Déterminant antigénique</term>
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<term>Nucléocapside</term>
<term>Protéine</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Coronavirus</term>
<term>Immunité humorale</term>
<term>Biochimie</term>
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<div type="abstract" xml:lang="en">Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.</div>
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<s0>Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.</s0>
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