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The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV

Identifieur interne : 005D49 ( Main/Exploration ); précédent : 005D48; suivant : 005D50

The Structure Analysis and Antigenicity Study of the N Protein of SARS-CoV

Auteurs : Jingqiang Wang [République populaire de Chine] ; Jia Ji [République populaire de Chine] ; Jia Ye [République populaire de Chine] ; Xiaoqian Zhao [République populaire de Chine] ; Jie Wen [République populaire de Chine] ; Wei Li [République populaire de Chine] ; Jianfei Hu [République populaire de Chine] ; Dawei Li [République populaire de Chine] ; Min Sun [République populaire de Chine] ; Haipan Zeng [République populaire de Chine] ; Yongwu Hu [République populaire de Chine] ; Xiangjun Tian [République populaire de Chine] ; Xuehai Tan [République populaire de Chine] ; Ningzhi Xu [République populaire de Chine] ; Changqing Zeng [République populaire de Chine] ; Jian Wang [République populaire de Chine] ; Shengli Bi [République populaire de Chine] ; Huanming Yang [République populaire de Chine]

Source :

RBID : PMC:5172421

Descripteurs français

English descriptors

Abstract

The Coronaviridae family is characterized by a nucleocapsid that is composed of the genome RNA molecule in combination with the nucleoprotein (N protein) within a virion. The most striking physiochemical feature of the N protein of SARS-CoV is that it is a typical basic protein with a high predicted pI and high hydrophilicity, which is consistent with its function of binding to the ribophosphate backbone of the RNA molecule. The predicted high extent of phosphorylation of the N protein on multiple candidate phosphorylation sites demonstrates that it would be related to important functions, such as RNA-binding and localization to the nucleolus of host cells. Subsequent study shows that there is an SR-rich region in the N protein and this region might be involved in the protein-protein interaction. The abundant antigenic sites predicted in the N protein, as well as experimental evidence with synthesized polypeptides, indicate that the N protein is one of the major antigens of the SARS-CoV. Compared with other viral structural proteins, the low variation rate of the N protein with regards to its size suggests its importance to the survival of the virus.


Url:
DOI: 10.1016/S1672-0229(03)01018-0
PubMed: 15626344
PubMed Central: 5172421


Affiliations:


Links toward previous steps (curation, corpus...)


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<wicri:regionArea>James D. Watson Institute of Genome Sciences, Zhijiang Campus, Zhejiang University and Hangzhou Genomics Institute, Hangzhou 310008</wicri:regionArea>
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<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>James D. Watson Institute of Genome Sciences, Zhijiang Campus, Zhejiang University and Hangzhou Genomics Institute, Hangzhou 310008</wicri:regionArea>
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<name sortKey="Bi, Shengli" sort="Bi, Shengli" uniqKey="Bi S" first="Shengli" last="Bi">Shengli Bi</name>
<affiliation wicri:level="1">
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<name sortKey="Yang, Huanming" sort="Yang, Huanming" uniqKey="Yang H" first="Huanming" last="Yang">Huanming Yang</name>
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</analytic>
<series>
<title level="j">Genomics, Proteomics & Bioinformatics</title>
<idno type="ISSN">1672-0229</idno>
<idno type="eISSN">2210-3244</idno>
<imprint>
<date when="2003">2003</date>
</imprint>
</series>
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<keywords scheme="KwdEn" xml:lang="en">
<term>Amino Acid Motifs (genetics)</term>
<term>Amino Acid Sequence</term>
<term>Antigens, Viral (immunology)</term>
<term>Base Composition</term>
<term>Base Sequence</term>
<term>Cluster Analysis</term>
<term>Computational Biology</term>
<term>DNA Primers</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Genetic Variation</term>
<term>Molecular Sequence Data</term>
<term>Nucleocapsid Proteins (genetics)</term>
<term>Nucleocapsid Proteins (immunology)</term>
<term>Nucleocapsid Proteins (metabolism)</term>
<term>Phosphorylation</term>
<term>SARS Virus (genetics)</term>
<term>Sequence Analysis, DNA</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Amorces ADN</term>
<term>Analyse de regroupements</term>
<term>Analyse de séquence d'ADN</term>
<term>Antigènes viraux (immunologie)</term>
<term>Biologie informatique</term>
<term>Composition en bases nucléiques</term>
<term>Données de séquences moléculaires</term>
<term>Motifs d'acides aminés (génétique)</term>
<term>Phosphorylation</term>
<term>Protéines nucléocapside (génétique)</term>
<term>Protéines nucléocapside (immunologie)</term>
<term>Protéines nucléocapside (métabolisme)</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Test ELISA</term>
<term>Variation génétique</term>
<term>Virus du SRAS (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Nucleocapsid Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en">
<term>Antigens, Viral</term>
<term>Nucleocapsid Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Amino Acid Motifs</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Motifs d'acides aminés</term>
<term>Protéines nucléocapside</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr">
<term>Antigènes viraux</term>
<term>Protéines nucléocapside</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Nucleocapsid Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Protéines nucléocapside</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Amino Acid Sequence</term>
<term>Base Composition</term>
<term>Base Sequence</term>
<term>Cluster Analysis</term>
<term>Computational Biology</term>
<term>DNA Primers</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Genetic Variation</term>
<term>Molecular Sequence Data</term>
<term>Phosphorylation</term>
<term>Sequence Analysis, DNA</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Amorces ADN</term>
<term>Analyse de regroupements</term>
<term>Analyse de séquence d'ADN</term>
<term>Biologie informatique</term>
<term>Composition en bases nucléiques</term>
<term>Données de séquences moléculaires</term>
<term>Phosphorylation</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Test ELISA</term>
<term>Variation génétique</term>
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<front>
<div type="abstract" xml:lang="en">
<p>The
<italic>Coronaviridae</italic>
family is characterized by a nucleocapsid that is composed of the genome RNA molecule in combination with the nucleoprotein (N protein) within a virion. The most striking physiochemical feature of the N protein of SARS-CoV is that it is a typical basic protein with a high predicted pI and high hydrophilicity, which is consistent with its function of binding to the ribophosphate backbone of the RNA molecule. The predicted high extent of phosphorylation of the N protein on multiple candidate phosphorylation sites demonstrates that it would be related to important functions, such as RNA-binding and localization to the nucleolus of host cells. Subsequent study shows that there is an SR-rich region in the N protein and this region might be involved in the protein-protein interaction. The abundant antigenic sites predicted in the N protein, as well as experimental evidence with synthesized polypeptides, indicate that the N protein is one of the major antigens of the SARS-CoV. Compared with other viral structural proteins, the low variation rate of the N protein with regards to its size suggests its importance to the survival of the virus.</p>
</div>
</front>
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</TEI>
<affiliations>
<list>
<country>
<li>République populaire de Chine</li>
</country>
<region>
<li>Pékin</li>
<li>Zhejiang</li>
</region>
<settlement>
<li>Hangzhou</li>
<li>Pékin</li>
</settlement>
<orgName>
<li>Université de Pékin</li>
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</country>
</tree>
</affiliations>
</record>

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