A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor
Identifieur interne : 001230 ( Pmc/Curation ); précédent : 001229; suivant : 001231A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor
Auteurs : Chih-Fong Chou ; Shuo Shen ; Yee-Joo Tan ; Burtram C. Fielding ; Timothy H. P. Tan ; Jianlin Fu ; Qiurong Xu ; Seng Gee Lim ; Wanjin HongSource :
- Journal of Virological Methods [ 0166-0934 ] ; 2004.
Abstract
Severe acute respiratory syndrome (SARS), a life-threatening disease, is caused by the newly identified virus SARS coronavirus (SARS-CoV). In order to study the spike (S) protein of this highly contagious virus, we established a clonal cell-line, CHO-SG, from the Chinese hamster ovary cells that stably expresses C-terminally EGFP-tagged SARS-CoV S protein (S-EGFP). The ectodomain of the S glycoprotein is localized on the surface of CHO-SG cells with
Url:
DOI: 10.1016/j.jviromet.2004.09.008
PubMed: 15582697
PubMed Central: 7112911
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor</title><author><name sortKey="Chou, Chih Fong" sort="Chou, Chih Fong" uniqKey="Chou C" first="Chih-Fong" last="Chou">Chih-Fong Chou</name></author><author><name sortKey="Shen, Shuo" sort="Shen, Shuo" uniqKey="Shen S" first="Shuo" last="Shen">Shuo Shen</name></author><author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name></author><author><name sortKey="Fielding, Burtram C" sort="Fielding, Burtram C" uniqKey="Fielding B" first="Burtram C." last="Fielding">Burtram C. Fielding</name></author><author><name sortKey="Tan, Timothy H P" sort="Tan, Timothy H P" uniqKey="Tan T" first="Timothy H. P." last="Tan">Timothy H. P. Tan</name></author><author><name sortKey="Fu, Jianlin" sort="Fu, Jianlin" uniqKey="Fu J" first="Jianlin" last="Fu">Jianlin Fu</name></author><author><name sortKey="Xu, Qiurong" sort="Xu, Qiurong" uniqKey="Xu Q" first="Qiurong" last="Xu">Qiurong Xu</name></author><author><name sortKey="Lim, Seng Gee" sort="Lim, Seng Gee" uniqKey="Lim S" first="Seng Gee" last="Lim">Seng Gee Lim</name></author><author><name sortKey="Hong, Wanjin" sort="Hong, Wanjin" uniqKey="Hong W" first="Wanjin" last="Hong">Wanjin Hong</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">15582697</idno><idno type="pmc">7112911</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112911</idno><idno type="RBID">PMC:7112911</idno><idno type="doi">10.1016/j.jviromet.2004.09.008</idno><date when="2004">2004</date><idno type="wicri:Area/Pmc/Corpus">001230</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001230</idno><idno type="wicri:Area/Pmc/Curation">001230</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001230</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor</title><author><name sortKey="Chou, Chih Fong" sort="Chou, Chih Fong" uniqKey="Chou C" first="Chih-Fong" last="Chou">Chih-Fong Chou</name></author><author><name sortKey="Shen, Shuo" sort="Shen, Shuo" uniqKey="Shen S" first="Shuo" last="Shen">Shuo Shen</name></author><author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name></author><author><name sortKey="Fielding, Burtram C" sort="Fielding, Burtram C" uniqKey="Fielding B" first="Burtram C." last="Fielding">Burtram C. Fielding</name></author><author><name sortKey="Tan, Timothy H P" sort="Tan, Timothy H P" uniqKey="Tan T" first="Timothy H. P." last="Tan">Timothy H. P. Tan</name></author><author><name sortKey="Fu, Jianlin" sort="Fu, Jianlin" uniqKey="Fu J" first="Jianlin" last="Fu">Jianlin Fu</name></author><author><name sortKey="Xu, Qiurong" sort="Xu, Qiurong" uniqKey="Xu Q" first="Qiurong" last="Xu">Qiurong Xu</name></author><author><name sortKey="Lim, Seng Gee" sort="Lim, Seng Gee" uniqKey="Lim S" first="Seng Gee" last="Lim">Seng Gee Lim</name></author><author><name sortKey="Hong, Wanjin" sort="Hong, Wanjin" uniqKey="Hong W" first="Wanjin" last="Hong">Wanjin Hong</name></author></analytic><series><title level="j">Journal of Virological Methods</title><idno type="ISSN">0166-0934</idno><idno type="eISSN">1879-0984</idno><imprint><date when="2004">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Severe acute respiratory syndrome (SARS), a life-threatening disease, is caused by the newly identified virus SARS coronavirus (SARS-CoV). In order to study the spike (S) protein of this highly contagious virus, we established a clonal cell-line, CHO-SG, from the Chinese hamster ovary cells that stably expresses C-terminally EGFP-tagged SARS-CoV S protein (S-EGFP). The ectodomain of the S glycoprotein is localized on the surface of CHO-SG cells with <italic>N</italic>-acetyl-glucosamine-terminated carbohydrate structure. CHO-SG cells associated tightly with Vero E6 cells, a SARS-CoV receptor (ACE2) expressing cell-line, and the interaction remained stable under highly stringent condition (1 M NaCl). This interaction could be blocked by either the serum from a SARS convalescent patient or a goat anti-ACE2 antibody, indicating that the interaction is specific. A binding epitope with lesser degree of glycosylation and native conformation was localized by using rabbit anti-sera raised against five denatured recombinant S protein fragments expressed in <italic>Escherichia coli</italic>. One of the sera obtained from the fragment encompassing amino acids 48-358 significantly blocked the interaction between CHO-SG and Vero E6 cells. The region is useful for studying neutralizing antibodies in future vaccine development. This paper describes an easy and safe cell-based assay suitable for studying the binding between SARS-CoV S protein and its receptor.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Babcock, G J" uniqKey="Babcock G">G.J. Babcock</name></author><author><name sortKey="Esshaki, D J" uniqKey="Esshaki D">D.J. Esshaki</name></author><author><name sortKey="Thomas, W D" uniqKey="Thomas W">W.D. Thomas</name></author><author><name sortKey="Ambrosino, D M" uniqKey="Ambrosino D">D.M. Ambrosino</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Brenner, S" uniqKey="Brenner S">S. Brenner</name></author><author><name sortKey="Venkatesh, B" uniqKey="Venkatesh B">B. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol Methods</journal-id><journal-id journal-id-type="iso-abbrev">J. Virol. Methods</journal-id><journal-title-group><journal-title>Journal of Virological Methods</journal-title></journal-title-group><issn pub-type="ppub">0166-0934</issn><issn pub-type="epub">1879-0984</issn><publisher><publisher-name>Elsevier B.V.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">15582697</article-id><article-id pub-id-type="pmc">7112911</article-id><article-id pub-id-type="publisher-id">S0166-0934(04)00265-4</article-id><article-id pub-id-type="doi">10.1016/j.jviromet.2004.09.008</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Chou</surname><given-names>Chih-Fong</given-names></name><email>mcbccf@imcb.a-star.edu.sg</email><xref rid="cor1" ref-type="corresp">*</xref></contrib><contrib contrib-type="author"><name><surname>Shen</surname><given-names>Shuo</given-names></name></contrib><contrib contrib-type="author"><name><surname>Tan</surname><given-names>Yee-Joo</given-names></name></contrib><contrib contrib-type="author"><name><surname>Fielding</surname><given-names>Burtram C.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Tan</surname><given-names>Timothy H.P.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Fu</surname><given-names>Jianlin</given-names></name></contrib><contrib contrib-type="author"><name><surname>Xu</surname><given-names>Qiurong</given-names></name></contrib><contrib contrib-type="author"><name><surname>Lim</surname><given-names>Seng Gee</given-names></name></contrib><contrib contrib-type="author"><name><surname>Hong</surname><given-names>Wanjin</given-names></name></contrib></contrib-group><aff>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore</aff><author-notes><corresp id="cor1"><label>*</label>Corresponding author. Tel.: +65 6586 9623; fax: +65 6779 1117. <email>mcbccf@imcb.a-star.edu.sg</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>5</day><month>11</month><year>2004</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>1</month><year>2005</year></pub-date><pub-date pub-type="epub"><day>5</day><month>11</month><year>2004</year></pub-date><volume>123</volume><issue>1</issue><fpage>41</fpage><lpage>48</lpage><history><date date-type="received"><day>12</day><month>7</month><year>2004</year></date><date date-type="rev-recd"><day>26</day><month>8</month><year>2004</year></date><date date-type="accepted"><day>7</day><month>9</month><year>2004</year></date></history><permissions><copyright-statement>Copyright © 2004 Elsevier B.V. All rights reserved.</copyright-statement><copyright-year>2004</copyright-year><copyright-holder>Elsevier B.V.</copyright-holder><license><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><p>Severe acute respiratory syndrome (SARS), a life-threatening disease, is caused by the newly identified virus SARS coronavirus (SARS-CoV). In order to study the spike (S) protein of this highly contagious virus, we established a clonal cell-line, CHO-SG, from the Chinese hamster ovary cells that stably expresses C-terminally EGFP-tagged SARS-CoV S protein (S-EGFP). The ectodomain of the S glycoprotein is localized on the surface of CHO-SG cells with <italic>N</italic>-acetyl-glucosamine-terminated carbohydrate structure. CHO-SG cells associated tightly with Vero E6 cells, a SARS-CoV receptor (ACE2) expressing cell-line, and the interaction remained stable under highly stringent condition (1 M NaCl). This interaction could be blocked by either the serum from a SARS convalescent patient or a goat anti-ACE2 antibody, indicating that the interaction is specific. A binding epitope with lesser degree of glycosylation and native conformation was localized by using rabbit anti-sera raised against five denatured recombinant S protein fragments expressed in <italic>Escherichia coli</italic>. One of the sera obtained from the fragment encompassing amino acids 48-358 significantly blocked the interaction between CHO-SG and Vero E6 cells. The region is useful for studying neutralizing antibodies in future vaccine development. This paper describes an easy and safe cell-based assay suitable for studying the binding between SARS-CoV S protein and its receptor.</p></abstract><kwd-group><title>Keywords</title><kwd>SARS-CoV</kwd><kwd>Ectodomain</kwd><kwd>CHO</kwd><kwd>EGFP-tagged</kwd><kwd>ACE2</kwd><kwd>Cell-based assay</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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