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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 : 002785 ( PubMed/Checkpoint ); précédent : 002784; suivant : 002786

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 ; Li-Wen Qiu ; Jingran Zhou ; Bing Ni ; Bo Guo ; Qiang Zou ; Liyun Zou ; Wei Zhou ; Zhengcai Jia ; Xiao-Yan Che ; Yuzhang Wu

Source :

RBID : pubmed:15976093

Descripteurs français

English descriptors

Abstract

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.

DOI: 10.1373/clinchem.2005.051045
PubMed: 15976093


Affiliations:


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pubmed:15976093

Le document en format XML

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<term>Cell Line</term>
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<term>Epitope Mapping</term>
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<term>Humans</term>
<term>Male</term>
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<term>Nucleocapsid Proteins (genetics)</term>
<term>Nucleocapsid Proteins (metabolism)</term>
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<term>Severe Acute Respiratory Syndrome (immunology)</term>
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<term>Anticorps monoclonaux</term>
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<term>Femelle</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Mâle</term>
<term>Production d'anticorps</term>
<term>Protéines nucléocapside (génétique)</term>
<term>Protéines nucléocapside (métabolisme)</term>
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<term>Souris de lignée BALB C</term>
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<term>Nucleocapsid Proteins</term>
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<term>Nucleocapsid Proteins</term>
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<term>Protéines nucléocapside</term>
<term>Saccharomyces cerevisiae</term>
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<term>Syndrome respiratoire aigu sévère</term>
<term>Virus du SRAS</term>
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<term>SARS Virus</term>
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<term>Chlorocebus aethiops</term>
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<term>Humans</term>
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<term>Mice, Inbred BALB C</term>
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<term>Anticorps monoclonaux</term>
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<term>Lignée cellulaire</term>
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<div type="abstract" xml:lang="en">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.</div>
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<Year>2020</Year>
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<Year>2005</Year>
<Month>Aug</Month>
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<Title>Clinical chemistry</Title>
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<ArticleTitle>Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus: insight into the humoral immunity of SARS.</ArticleTitle>
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<AbstractText Label="BACKGROUND" NlmCategory="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.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="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.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="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).</AbstractText>
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