A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor.
Identifieur interne : 002A14 ( PubMed/Corpus ); précédent : 002A13; suivant : 002A15A 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 ] ; 2005.
English descriptors
- KwdEn :
- Animals, CHO Cells, Chlorocebus aethiops, Cricetinae, Green Fluorescent Proteins (genetics), Green Fluorescent Proteins (metabolism), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Receptors, Virus (metabolism), SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , genetics : Green Fluorescent Proteins, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Green Fluorescent Proteins, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- metabolism : SARS Virus.
- Animals, CHO Cells, Chlorocebus aethiops, Cricetinae, Spike Glycoprotein, Coronavirus, Vero Cells.
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 N-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 (1M 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 Escherichia coli. 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.
DOI: 10.1016/j.jviromet.2004.09.008
PubMed: 15582697
Links to Exploration step
pubmed:15582697Le document en format XML
<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><affiliation><nlm:affiliation>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore. mcbccf@imcb.a-star.edu.sg</nlm:affiliation></affiliation></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">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15582697</idno><idno type="pmid">15582697</idno><idno type="doi">10.1016/j.jviromet.2004.09.008</idno><idno type="wicri:Area/PubMed/Corpus">002A14</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002A14</idno></publicationStmt><sourceDesc><biblStruct><analytic><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><affiliation><nlm:affiliation>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore. mcbccf@imcb.a-star.edu.sg</nlm:affiliation></affiliation></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><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>CHO Cells</term><term>Chlorocebus aethiops</term><term>Cricetinae</term><term>Green Fluorescent Proteins (genetics)</term><term>Green Fluorescent Proteins (metabolism)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Green Fluorescent Proteins</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Green Fluorescent Proteins</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>CHO Cells</term><term>Chlorocebus aethiops</term><term>Cricetinae</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 N-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 (1M 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 Escherichia coli. 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15582697</PMID><DateCompleted><Year>2005</Year><Month>02</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0166-0934</ISSN><JournalIssue CitedMedium="Print"><Volume>123</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Journal of virological methods</Title><ISOAbbreviation>J. Virol. Methods</ISOAbbreviation></Journal><ArticleTitle>A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor.</ArticleTitle><Pagination><MedlinePgn>41-8</MedlinePgn></Pagination><Abstract><AbstractText>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 N-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 (1M 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 Escherichia coli. 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chou</LastName><ForeName>Chih-Fong</ForeName><Initials>CF</Initials><AffiliationInfo><Affiliation>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore. mcbccf@imcb.a-star.edu.sg</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Shuo</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Yee-Joo</ForeName><Initials>YJ</Initials></Author><Author ValidYN="Y"><LastName>Fielding</LastName><ForeName>Burtram C</ForeName><Initials>BC</Initials></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Timothy H P</ForeName><Initials>TH</Initials></Author><Author ValidYN="Y"><LastName>Fu</LastName><ForeName>Jianlin</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Qiurong</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Lim</LastName><ForeName>Seng Gee</ForeName><Initials>SG</Initials></Author><Author ValidYN="Y"><LastName>Hong</LastName><ForeName>Wanjin</ForeName><Initials>W</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D023362">Evaluation Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Virol Methods</MedlineTA><NlmUniqueID>8005839</NlmUniqueID><ISSNLinking>0166-0934</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016466" MajorTopicYN="N">CHO Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006224" MajorTopicYN="N">Cricetinae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000378" 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