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The M Protein of SARS-CoV: Basic Structural and Immunological Properties

Identifieur interne : 001783 ( Pmc/Checkpoint ); précédent : 001782; suivant : 001784

The M Protein of SARS-CoV: Basic Structural and Immunological Properties

Auteurs : Yongwu Hu [République populaire de Chine] ; Jie Wen [République populaire de Chine] ; Lin Tang [République populaire de Chine] ; Haijun Zhang [République populaire de Chine] ; Xiaowei Zhang [République populaire de Chine] ; Yan Li [République populaire de Chine] ; Jing Wang [République populaire de Chine] ; Yujun Han [République populaire de Chine] ; Guoqing Li [République populaire de Chine] ; Jianping Shi [République populaire de Chine] ; Xiangjun Tian [République populaire de Chine] ; Feng Jiang [République populaire de Chine] ; Xiaoqian Zhao [République populaire de Chine] ; Jun Wang [République populaire de Chine] ; Siqi Liu [République populaire de Chine] ; Changqing Zeng [République populaire de Chine] ; Jian Wang [République populaire de Chine] ; Huanming Yang [République populaire de Chine]

Source :

RBID : PMC:5172243

Abstract

We studied structural and immunological properties of the SARS-CoV M (membrane) protein, based on comparative analyses of sequence features, phylogenetic investigation, and experimental results. The M protein is predicted to contain a triple-spanning transmembrane (TM) region, a single N-glycosylation site near its N-terminus that is in the exterior of the virion, and a long C-terminal region in the interior. The M protein harbors a higher substitution rate (0.6% correlated to its size) among viral open reading frames (ORFs) from published data. The four substitutions detected in the M protein, which cause non-synonymous changes, can be classified into three types. One of them results in changes of pI (isoelectric point) and charge, affecting antigenicity. The second changes hydrophobicity of the TM region, and the third one relates to hydrophilicity of the interior structure. Phylogenetic tree building based on the variations of the M protein appears to support the non-human origin of SARS-CoV. To investigate its immunogenicity, we synthesized eight oligopeptides covering 69.2% of the entire ORF and screened them by using ELISA (enzyme-linked immunosorbent assay) with sera from SARS patients. The results confirmed our predictions on antigenic sites.


Url:
DOI: 10.1016/S1672-0229(03)01016-7
PubMed: 15626342
PubMed Central: 5172243


Affiliations:


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PMC:5172243

Le document en format XML

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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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<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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<p>We studied structural and immunological properties of the SARS-CoV M (membrane) protein, based on comparative analyses of sequence features, phylogenetic investigation, and experimental results. The M protein is predicted to contain a triple-spanning transmembrane (TM) region, a single N-glycosylation site near its N-terminus that is in the exterior of the virion, and a long C-terminal region in the interior. The M protein harbors a higher substitution rate (0.6% correlated to its size) among viral open reading frames (ORFs) from published data. The four substitutions detected in the M protein, which cause non-synonymous changes, can be classified into three types. One of them results in changes of pI (isoelectric point) and charge, affecting antigenicity. The second changes hydrophobicity of the TM region, and the third one relates to hydrophilicity of the interior structure. Phylogenetic tree building based on the variations of the M protein appears to support the non-human origin of SARS-CoV. To investigate its immunogenicity, we synthesized eight oligopeptides covering 69.2% of the entire ORF and screened them by using ELISA (enzyme-linked immunosorbent assay) with sera from SARS patients. The results confirmed our predictions on antigenic sites.</p>
</div>
</front>
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<journal-id journal-id-type="nlm-ta">Genomics Proteomics Bioinformatics</journal-id>
<journal-id journal-id-type="iso-abbrev">Genomics Proteomics Bioinformatics</journal-id>
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<issn pub-type="epub">2210-3244</issn>
<publisher>
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<article-title>The M Protein of SARS-CoV: Basic Structural and Immunological Properties</article-title>
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<name>
<surname>Hu</surname>
<given-names>Yongwu</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="aff0010" ref-type="aff">2</xref>
<xref rid="fn1" ref-type="fn">*</xref>
</contrib>
<contrib contrib-type="author" id="au0010">
<name>
<surname>Wen</surname>
<given-names>Jie</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="fn1" ref-type="fn">*</xref>
</contrib>
<contrib contrib-type="author" id="au0015">
<name>
<surname>Tang</surname>
<given-names>Lin</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="fn1" ref-type="fn">*</xref>
</contrib>
<contrib contrib-type="author" id="au0020">
<name>
<surname>Zhang</surname>
<given-names>Haijun</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="fn1" ref-type="fn">*</xref>
</contrib>
<contrib contrib-type="author" id="au0025">
<name>
<surname>Zhang</surname>
<given-names>Xiaowei</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0030">
<name>
<surname>Li</surname>
<given-names>Yan</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0035">
<name>
<surname>Wang</surname>
<given-names>Jing</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="aff0015" ref-type="aff">3</xref>
</contrib>
<contrib contrib-type="author" id="au0040">
<name>
<surname>Han</surname>
<given-names>Yujun</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0045">
<name>
<surname>Li</surname>
<given-names>Guoqing</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0050">
<name>
<surname>Shi</surname>
<given-names>Jianping</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0055">
<name>
<surname>Tian</surname>
<given-names>Xiangjun</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="aff0010" ref-type="aff">2</xref>
</contrib>
<contrib contrib-type="author" id="au0060">
<name>
<surname>Jiang</surname>
<given-names>Feng</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0065">
<name>
<surname>Zhao</surname>
<given-names>Xiaoqian</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0070">
<name>
<surname>Wang</surname>
<given-names>Jun</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0075">
<name>
<surname>Liu</surname>
<given-names>Siqi</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0080">
<name>
<surname>Zeng</surname>
<given-names>Changqing</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
</contrib>
<contrib contrib-type="author" id="au0085">
<name>
<surname>Wang</surname>
<given-names>Jian</given-names>
</name>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="aff0010" ref-type="aff">2</xref>
</contrib>
<contrib contrib-type="author" id="au0090">
<name>
<surname>Yang</surname>
<given-names>Huanming</given-names>
</name>
<email>yanghm@genomics.org.cn</email>
<xref rid="aff0005" ref-type="aff">1</xref>
<xref rid="aff0010" ref-type="aff">2</xref>
<xref rid="cor1" ref-type="corresp">#</xref>
</contrib>
</contrib-group>
<aff id="aff0005">
<label>1</label>
Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China</aff>
<aff id="aff0010">
<label>2</label>
James D. Watson Institute of Genome Sciences, Zhijiang Campus, Zhejiang University and Hangzhou Genomics Institute, Hangzhou 310008, China</aff>
<aff id="aff0015">
<label>3</label>
College of Life Sciences, Peking University, Beijing 100871, China</aff>
<author-notes>
<corresp id="cor1">
<label>#</label>
Corresponding author.
<email>yanghm@genomics.org.cn</email>
</corresp>
<fn id="fn1">
<label>*</label>
<p id="ntp0005">These authors contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release">
<day>28</day>
<month>11</month>
<year>2016</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub">
<month>5</month>
<year>2003</year>
</pub-date>
<pub-date pub-type="epub">
<day>28</day>
<month>11</month>
<year>2016</year>
</pub-date>
<volume>1</volume>
<issue>2</issue>
<fpage>118</fpage>
<lpage>130</lpage>
<permissions>
<copyright-statement>Copyright © 2003 Beijing Institute of Genomics, the Chinese Academy of Sciences and the Genetics Society of China. Production and hosting by Elsevier B.V.</copyright-statement>
<copyright-year>2003</copyright-year>
<copyright-holder>Beijing Institute of Genomics, the Chinese Academy of Sciences and the Genetics Society of China</copyright-holder>
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<license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p>
</license>
</permissions>
<abstract id="ab0005">
<p>We studied structural and immunological properties of the SARS-CoV M (membrane) protein, based on comparative analyses of sequence features, phylogenetic investigation, and experimental results. The M protein is predicted to contain a triple-spanning transmembrane (TM) region, a single N-glycosylation site near its N-terminus that is in the exterior of the virion, and a long C-terminal region in the interior. The M protein harbors a higher substitution rate (0.6% correlated to its size) among viral open reading frames (ORFs) from published data. The four substitutions detected in the M protein, which cause non-synonymous changes, can be classified into three types. One of them results in changes of pI (isoelectric point) and charge, affecting antigenicity. The second changes hydrophobicity of the TM region, and the third one relates to hydrophilicity of the interior structure. Phylogenetic tree building based on the variations of the M protein appears to support the non-human origin of SARS-CoV. To investigate its immunogenicity, we synthesized eight oligopeptides covering 69.2% of the entire ORF and screened them by using ELISA (enzyme-linked immunosorbent assay) with sera from SARS patients. The results confirmed our predictions on antigenic sites.</p>
</abstract>
<kwd-group id="keys0005">
<title>Key words</title>
<kwd>SARS-CoV</kwd>
<kwd>the M protein</kwd>
<kwd>enzyme immunoassay</kwd>
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