Expression cloning of functional receptor used by SARS coronavirus.
Identifieur interne : 002F59 ( PubMed/Corpus ); précédent : 002F58; suivant : 002F60Expression cloning of functional receptor used by SARS coronavirus.
Auteurs : Peigang Wang ; Jian Chen ; Aihua Zheng ; Yuchun Nie ; Xuanling Shi ; Wei Wang ; Guangwen Wang ; Min Luo ; Huijun Liu ; Lei Tan ; Xijun Song ; Zai Wang ; Xiaolei Yin ; Xiuxia Qu ; Xiaojing Wang ; Tingting Qing ; Mingxiao Ding ; Hongkui DengSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
English descriptors
- KwdEn :
- Animals, Carboxypeptidases (metabolism), Carrier Proteins, Cell Separation, Chlorocebus aethiops, Cloning, Molecular, DNA, Complementary (metabolism), Flow Cytometry, Gene Library, Glycoproteins (chemistry), HeLa Cells, Humans, Ligands, Membrane Glycoproteins (metabolism), Mice, Models, Genetic, NIH 3T3 Cells, Peptidyl-Dipeptidase A, Polymerase Chain Reaction, Protein Binding, Protein Structure, Tertiary, Receptors, Virus (chemistry), Retroviridae (genetics), Reverse Transcriptase Polymerase Chain Reaction, SARS Virus (metabolism), Terminal Repeat Sequences, Vero Cells, Viral Envelope Proteins.
- MESH :
- chemical , chemistry : Glycoproteins, Receptors, Virus.
- chemical , metabolism : Carboxypeptidases, DNA, Complementary, Membrane Glycoproteins.
- genetics : Retroviridae.
- metabolism : SARS Virus.
- Animals, Carrier Proteins, Cell Separation, Chlorocebus aethiops, Cloning, Molecular, Flow Cytometry, Gene Library, HeLa Cells, Humans, Ligands, Mice, Models, Genetic, NIH 3T3 Cells, Peptidyl-Dipeptidase A, Polymerase Chain Reaction, Protein Binding, Protein Structure, Tertiary, Reverse Transcriptase Polymerase Chain Reaction, Terminal Repeat Sequences, Vero Cells, Viral Envelope Proteins.
Abstract
We have expressed a series of truncated spike (S) glycoproteins of SARS-CoV and found that the N-terminus 14-502 residuals were sufficient to bind to SARS-CoV susceptible Vero E6 cells. With this soluble S protein fragment as an affinity ligand, we screened HeLa cells transduced with retroviral cDNA library from Vero E6 cells and obtained a HeLa cell clone which could bind with the S protein. This cell clone was susceptible to HIV/SARS pseudovirus infection and the presence of a functional receptor for S protein in this cell clone was confirmed by the cell-cell fusion assay. Further studies showed the susceptibility of this cell was due to the expression of endogenous angiotensin-converting enzyme 2 (ACE2) which was activated by inserted LTR from retroviral vector used for expression cloning. When human ACE2 cDNA was transduced into NIH3T3 cells, the ACE2 expressing NIH3T3 cells could be infected with HIV/SARS pseudovirus. These data clearly demonstrated that ACE2 was the functional receptor for SARS-CoV.
DOI: 10.1016/j.bbrc.2004.01.076
PubMed: 14766227
Links to Exploration step
pubmed:14766227Le document en format XML
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uniqKey="Wang W" first="Wei" last="Wang">Wei Wang</name></author><author><name sortKey="Wang, Guangwen" sort="Wang, Guangwen" uniqKey="Wang G" first="Guangwen" last="Wang">Guangwen Wang</name></author><author><name sortKey="Luo, Min" sort="Luo, Min" uniqKey="Luo M" first="Min" last="Luo">Min Luo</name></author><author><name sortKey="Liu, Huijun" sort="Liu, Huijun" uniqKey="Liu H" first="Huijun" last="Liu">Huijun Liu</name></author><author><name sortKey="Tan, Lei" sort="Tan, Lei" uniqKey="Tan L" first="Lei" last="Tan">Lei Tan</name></author><author><name sortKey="Song, Xijun" sort="Song, Xijun" uniqKey="Song X" first="Xijun" last="Song">Xijun Song</name></author><author><name sortKey="Wang, Zai" sort="Wang, Zai" uniqKey="Wang Z" first="Zai" last="Wang">Zai Wang</name></author><author><name sortKey="Yin, Xiaolei" sort="Yin, Xiaolei" uniqKey="Yin X" first="Xiaolei" last="Yin">Xiaolei Yin</name></author><author><name sortKey="Qu, Xiuxia" sort="Qu, Xiuxia" uniqKey="Qu X" first="Xiuxia" last="Qu">Xiuxia Qu</name></author><author><name sortKey="Wang, Xiaojing" sort="Wang, Xiaojing" uniqKey="Wang X" first="Xiaojing" last="Wang">Xiaojing Wang</name></author><author><name sortKey="Qing, Tingting" sort="Qing, Tingting" uniqKey="Qing T" first="Tingting" last="Qing">Tingting Qing</name></author><author><name sortKey="Ding, Mingxiao" sort="Ding, Mingxiao" uniqKey="Ding M" first="Mingxiao" last="Ding">Mingxiao Ding</name></author><author><name sortKey="Deng, Hongkui" sort="Deng, Hongkui" uniqKey="Deng H" first="Hongkui" last="Deng">Hongkui Deng</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:14766227</idno><idno type="pmid">14766227</idno><idno type="doi">10.1016/j.bbrc.2004.01.076</idno><idno type="wicri:Area/PubMed/Corpus">002F59</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002F59</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Expression cloning of functional receptor used by SARS coronavirus.</title><author><name sortKey="Wang, Peigang" sort="Wang, Peigang" uniqKey="Wang P" first="Peigang" last="Wang">Peigang Wang</name><affiliation><nlm:affiliation>Department of Cell Biology and Genetics, College of Life Sciences, Peking University, Beijing 100871, PR China.</nlm:affiliation></affiliation></author><author><name sortKey="Chen, Jian" sort="Chen, Jian" uniqKey="Chen J" first="Jian" last="Chen">Jian Chen</name></author><author><name sortKey="Zheng, Aihua" sort="Zheng, Aihua" uniqKey="Zheng A" first="Aihua" last="Zheng">Aihua Zheng</name></author><author><name sortKey="Nie, Yuchun" sort="Nie, Yuchun" uniqKey="Nie Y" first="Yuchun" last="Nie">Yuchun Nie</name></author><author><name sortKey="Shi, Xuanling" sort="Shi, Xuanling" uniqKey="Shi X" first="Xuanling" last="Shi">Xuanling Shi</name></author><author><name sortKey="Wang, Wei" sort="Wang, Wei" uniqKey="Wang W" first="Wei" last="Wang">Wei Wang</name></author><author><name sortKey="Wang, Guangwen" sort="Wang, Guangwen" uniqKey="Wang G" first="Guangwen" last="Wang">Guangwen Wang</name></author><author><name sortKey="Luo, Min" sort="Luo, Min" uniqKey="Luo M" first="Min" last="Luo">Min Luo</name></author><author><name sortKey="Liu, Huijun" sort="Liu, Huijun" uniqKey="Liu H" first="Huijun" last="Liu">Huijun Liu</name></author><author><name sortKey="Tan, Lei" sort="Tan, Lei" uniqKey="Tan L" first="Lei" last="Tan">Lei Tan</name></author><author><name sortKey="Song, Xijun" sort="Song, Xijun" uniqKey="Song X" first="Xijun" last="Song">Xijun Song</name></author><author><name sortKey="Wang, Zai" sort="Wang, Zai" uniqKey="Wang Z" first="Zai" last="Wang">Zai Wang</name></author><author><name sortKey="Yin, Xiaolei" sort="Yin, Xiaolei" uniqKey="Yin X" first="Xiaolei" last="Yin">Xiaolei Yin</name></author><author><name sortKey="Qu, Xiuxia" sort="Qu, Xiuxia" uniqKey="Qu X" first="Xiuxia" last="Qu">Xiuxia Qu</name></author><author><name sortKey="Wang, Xiaojing" sort="Wang, Xiaojing" uniqKey="Wang X" first="Xiaojing" last="Wang">Xiaojing Wang</name></author><author><name sortKey="Qing, Tingting" sort="Qing, Tingting" uniqKey="Qing T" first="Tingting" last="Qing">Tingting Qing</name></author><author><name sortKey="Ding, Mingxiao" sort="Ding, Mingxiao" uniqKey="Ding M" first="Mingxiao" last="Ding">Mingxiao Ding</name></author><author><name sortKey="Deng, Hongkui" sort="Deng, Hongkui" uniqKey="Deng H" first="Hongkui" last="Deng">Hongkui Deng</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Carboxypeptidases (metabolism)</term><term>Carrier Proteins</term><term>Cell Separation</term><term>Chlorocebus aethiops</term><term>Cloning, Molecular</term><term>DNA, Complementary (metabolism)</term><term>Flow Cytometry</term><term>Gene Library</term><term>Glycoproteins (chemistry)</term><term>HeLa Cells</term><term>Humans</term><term>Ligands</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Models, Genetic</term><term>NIH 3T3 Cells</term><term>Peptidyl-Dipeptidase A</term><term>Polymerase Chain Reaction</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Receptors, Virus (chemistry)</term><term>Retroviridae (genetics)</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>SARS Virus (metabolism)</term><term>Terminal Repeat Sequences</term><term>Vero Cells</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glycoproteins</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term><term>DNA, Complementary</term><term>Membrane Glycoproteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Retroviridae</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>Carrier Proteins</term><term>Cell Separation</term><term>Chlorocebus aethiops</term><term>Cloning, Molecular</term><term>Flow Cytometry</term><term>Gene Library</term><term>HeLa Cells</term><term>Humans</term><term>Ligands</term><term>Mice</term><term>Models, Genetic</term><term>NIH 3T3 Cells</term><term>Peptidyl-Dipeptidase A</term><term>Polymerase Chain Reaction</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Terminal Repeat Sequences</term><term>Vero Cells</term><term>Viral Envelope Proteins</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have expressed a series of truncated spike (S) glycoproteins of SARS-CoV and found that the N-terminus 14-502 residuals were sufficient to bind to SARS-CoV susceptible Vero E6 cells. With this soluble S protein fragment as an affinity ligand, we screened HeLa cells transduced with retroviral cDNA library from Vero E6 cells and obtained a HeLa cell clone which could bind with the S protein. This cell clone was susceptible to HIV/SARS pseudovirus infection and the presence of a functional receptor for S protein in this cell clone was confirmed by the cell-cell fusion assay. Further studies showed the susceptibility of this cell was due to the expression of endogenous angiotensin-converting enzyme 2 (ACE2) which was activated by inserted LTR from retroviral vector used for expression cloning. When human ACE2 cDNA was transduced into NIH3T3 cells, the ACE2 expressing NIH3T3 cells could be infected with HIV/SARS pseudovirus. These data clearly demonstrated that ACE2 was the functional receptor for SARS-CoV.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14766227</PMID><DateCompleted><Year>2004</Year><Month>04</Month><Day>20</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>315</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Mar</Month><Day>05</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>Expression cloning of functional receptor used by SARS coronavirus.</ArticleTitle><Pagination><MedlinePgn>439-44</MedlinePgn></Pagination><Abstract><AbstractText>We have expressed a series of truncated spike (S) glycoproteins of SARS-CoV and found that the N-terminus 14-502 residuals were sufficient to bind to SARS-CoV susceptible Vero E6 cells. With this soluble S protein fragment as an affinity ligand, we screened HeLa cells transduced with retroviral cDNA library from Vero E6 cells and obtained a HeLa cell clone which could bind with the S protein. This cell clone was susceptible to HIV/SARS pseudovirus infection and the presence of a functional receptor for S protein in this cell clone was confirmed by the cell-cell fusion assay. Further studies showed the susceptibility of this cell was due to the expression of endogenous angiotensin-converting enzyme 2 (ACE2) which was activated by inserted LTR from retroviral vector used for expression cloning. When human ACE2 cDNA was transduced into NIH3T3 cells, the ACE2 expressing NIH3T3 cells could be infected with HIV/SARS pseudovirus. These data clearly demonstrated that ACE2 was the functional receptor for SARS-CoV.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Peigang</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Cell Biology and Genetics, College of Life Sciences, Peking University, Beijing 100871, PR China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Jian</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Aihua</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Nie</LastName><ForeName>Yuchun</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Shi</LastName><ForeName>Xuanling</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Wei</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Guangwen</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Min</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Huijun</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Lei</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Xijun</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Zai</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Yin</LastName><ForeName>Xiaolei</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Qu</LastName><ForeName>Xiuxia</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Xiaojing</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Qing</LastName><ForeName>Tingting</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Ding</LastName><ForeName>Mingxiao</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Deng</LastName><ForeName>Hongkui</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006023">Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008024">Ligands</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="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D002268">Carboxypeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber><NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002268" MajorTopicYN="N">Carboxypeptidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002469" MajorTopicYN="N">Cell Separation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005434" MajorTopicYN="N">Flow Cytometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015723" MajorTopicYN="N">Gene Library</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006023" MajorTopicYN="N">Glycoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008957" MajorTopicYN="N">Models, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D041681" MajorTopicYN="N">NIH 3T3 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012190" MajorTopicYN="N">Retroviridae</DescriptorName><QualifierName UI="Q000235" 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