Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2.
Identifieur interne : 002B53 ( PubMed/Corpus ); précédent : 002B52; suivant : 002B54Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2.
Auteurs : Michael J. Moore ; Tatyana Dorfman ; Wenhui Li ; Swee Kee Wong ; Yanhan Li ; Jens H. Kuhn ; James Coderre ; Natalya Vasilieva ; Zhongchao Han ; Thomas C. Greenough ; Michael Farzan ; Hyeryun ChoeSource :
- Journal of virology [ 0022-538X ] ; 2004.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Carboxypeptidases (genetics), Carboxypeptidases (metabolism), Cell Line, HIV-1 (genetics), Humans, Leukemia Virus, Murine (genetics), Leukemia Virus, Murine (metabolism), Leukemia Virus, Murine (physiology), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Peptidyl-Dipeptidase A, Receptors, Virus (metabolism), SARS Virus (genetics), Simian Immunodeficiency Virus (genetics), Simian Immunodeficiency Virus (metabolism), Simian Immunodeficiency Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virion (chemistry), Virion (metabolism), Virus Replication.
- MESH :
- chemical , genetics : Carboxypeptidases, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Carboxypeptidases, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemistry : Virion.
- genetics : HIV-1, Leukemia Virus, Murine, SARS Virus, Simian Immunodeficiency Virus.
- metabolism : Leukemia Virus, Murine, Simian Immunodeficiency Virus, Virion.
- physiology : Leukemia Virus, Murine, Simian Immunodeficiency Virus.
- Amino Acid Sequence, Animals, Cell Line, Humans, Molecular Sequence Data, Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus, Virus Replication.
Abstract
Infection of receptor-bearing cells by coronaviruses is mediated by their spike (S) proteins. The coronavirus (SARS-CoV) that causes severe acute respiratory syndrome (SARS) infects cells expressing the receptor angiotensin-converting enzyme 2 (ACE2). Here we show that codon optimization of the SARS-CoV S-protein gene substantially enhanced S-protein expression. We also found that two retroviruses, simian immunodeficiency virus (SIV) and murine leukemia virus, both expressing green fluorescent protein and pseudotyped with SARS-CoV S protein or S-protein variants, efficiently infected HEK293T cells stably expressing ACE2. Infection mediated by an S-protein variant whose cytoplasmic domain had been truncated and altered to include a fragment of the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein was, in both cases, substantially more efficient than that mediated by wild-type S protein. Using S-protein-pseudotyped SIV, we found that the enzymatic activity of ACE2 made no contribution to S-protein-mediated infection. Finally, we show that a soluble and catalytically inactive form of ACE2 potently blocked infection by S-protein-pseudotyped retrovirus and by SARS-CoV. These results permit studies of SARS-CoV entry inhibitors without the use of live virus and suggest a candidate therapy for SARS.
DOI: 10.1128/JVI.78.19.10628-10635.2004
PubMed: 15367630
Links to Exploration step
pubmed:15367630Le document en format XML
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Moore</name><affiliation><nlm:affiliation>Partners AIDS Research Center, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Dorfman, Tatyana" sort="Dorfman, Tatyana" uniqKey="Dorfman T" first="Tatyana" last="Dorfman">Tatyana Dorfman</name></author><author><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></author><author><name sortKey="Wong, Swee Kee" sort="Wong, Swee Kee" uniqKey="Wong S" first="Swee Kee" last="Wong">Swee Kee Wong</name></author><author><name sortKey="Li, Yanhan" sort="Li, Yanhan" uniqKey="Li Y" first="Yanhan" last="Li">Yanhan Li</name></author><author><name sortKey="Kuhn, Jens H" sort="Kuhn, Jens H" uniqKey="Kuhn J" first="Jens H" last="Kuhn">Jens H. 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Moore</name><affiliation><nlm:affiliation>Partners AIDS Research Center, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Dorfman, Tatyana" sort="Dorfman, Tatyana" uniqKey="Dorfman T" first="Tatyana" last="Dorfman">Tatyana Dorfman</name></author><author><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></author><author><name sortKey="Wong, Swee Kee" sort="Wong, Swee Kee" uniqKey="Wong S" first="Swee Kee" last="Wong">Swee Kee Wong</name></author><author><name sortKey="Li, Yanhan" sort="Li, Yanhan" uniqKey="Li Y" first="Yanhan" last="Li">Yanhan Li</name></author><author><name sortKey="Kuhn, Jens H" sort="Kuhn, Jens H" uniqKey="Kuhn J" first="Jens H" last="Kuhn">Jens H. Kuhn</name></author><author><name sortKey="Coderre, James" sort="Coderre, James" uniqKey="Coderre J" first="James" last="Coderre">James Coderre</name></author><author><name sortKey="Vasilieva, Natalya" sort="Vasilieva, Natalya" uniqKey="Vasilieva N" first="Natalya" last="Vasilieva">Natalya Vasilieva</name></author><author><name sortKey="Han, Zhongchao" sort="Han, Zhongchao" uniqKey="Han Z" first="Zhongchao" last="Han">Zhongchao Han</name></author><author><name sortKey="Greenough, Thomas C" sort="Greenough, Thomas C" uniqKey="Greenough T" first="Thomas C" last="Greenough">Thomas C. Greenough</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author><author><name sortKey="Choe, Hyeryun" sort="Choe, Hyeryun" uniqKey="Choe H" first="Hyeryun" last="Choe">Hyeryun Choe</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Carboxypeptidases (genetics)</term><term>Carboxypeptidases (metabolism)</term><term>Cell Line</term><term>HIV-1 (genetics)</term><term>Humans</term><term>Leukemia Virus, Murine (genetics)</term><term>Leukemia Virus, Murine (metabolism)</term><term>Leukemia Virus, Murine (physiology)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Molecular Sequence Data</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (genetics)</term><term>Simian Immunodeficiency Virus (genetics)</term><term>Simian Immunodeficiency Virus (metabolism)</term><term>Simian Immunodeficiency Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virion (chemistry)</term><term>Virion (metabolism)</term><term>Virus Replication</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carboxypeptidases</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Virion</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>HIV-1</term><term>Leukemia Virus, Murine</term><term>SARS Virus</term><term>Simian Immunodeficiency Virus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Leukemia Virus, Murine</term><term>Simian Immunodeficiency Virus</term><term>Virion</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Leukemia Virus, Murine</term><term>Simian Immunodeficiency Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Molecular Sequence Data</term><term>Peptidyl-Dipeptidase A</term><term>Spike Glycoprotein, Coronavirus</term><term>Virus Replication</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Infection of receptor-bearing cells by coronaviruses is mediated by their spike (S) proteins. The coronavirus (SARS-CoV) that causes severe acute respiratory syndrome (SARS) infects cells expressing the receptor angiotensin-converting enzyme 2 (ACE2). Here we show that codon optimization of the SARS-CoV S-protein gene substantially enhanced S-protein expression. We also found that two retroviruses, simian immunodeficiency virus (SIV) and murine leukemia virus, both expressing green fluorescent protein and pseudotyped with SARS-CoV S protein or S-protein variants, efficiently infected HEK293T cells stably expressing ACE2. Infection mediated by an S-protein variant whose cytoplasmic domain had been truncated and altered to include a fragment of the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein was, in both cases, substantially more efficient than that mediated by wild-type S protein. Using S-protein-pseudotyped SIV, we found that the enzymatic activity of ACE2 made no contribution to S-protein-mediated infection. Finally, we show that a soluble and catalytically inactive form of ACE2 potently blocked infection by S-protein-pseudotyped retrovirus and by SARS-CoV. These results permit studies of SARS-CoV entry inhibitors without the use of live virus and suggest a candidate therapy for SARS.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15367630</PMID><DateCompleted><Year>2004</Year><Month>10</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>78</Volume><Issue>19</Issue><PubDate><Year>2004</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2.</ArticleTitle><Pagination><MedlinePgn>10628-35</MedlinePgn></Pagination><Abstract><AbstractText>Infection of receptor-bearing cells by coronaviruses is mediated by their spike (S) proteins. The coronavirus (SARS-CoV) that causes severe acute respiratory syndrome (SARS) infects cells expressing the receptor angiotensin-converting enzyme 2 (ACE2). Here we show that codon optimization of the SARS-CoV S-protein gene substantially enhanced S-protein expression. We also found that two retroviruses, simian immunodeficiency virus (SIV) and murine leukemia virus, both expressing green fluorescent protein and pseudotyped with SARS-CoV S protein or S-protein variants, efficiently infected HEK293T cells stably expressing ACE2. Infection mediated by an S-protein variant whose cytoplasmic domain had been truncated and altered to include a fragment of the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein was, in both cases, substantially more efficient than that mediated by wild-type S protein. Using S-protein-pseudotyped SIV, we found that the enzymatic activity of ACE2 made no contribution to S-protein-mediated infection. Finally, we show that a soluble and catalytically inactive form of ACE2 potently blocked infection by S-protein-pseudotyped retrovirus and by SARS-CoV. These results permit studies of SARS-CoV entry inhibitors without the use of live virus and suggest a candidate therapy for SARS.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Moore</LastName><ForeName>Michael J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Partners AIDS Research Center, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dorfman</LastName><ForeName>Tatyana</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Wenhui</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Swee Kee</ForeName><Initials>SK</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Yanhan</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Kuhn</LastName><ForeName>Jens H</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Coderre</LastName><ForeName>James</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Vasilieva</LastName><ForeName>Natalya</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Han</LastName><ForeName>Zhongchao</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Greenough</LastName><ForeName>Thomas C</ForeName><Initials>TC</Initials></Author><Author ValidYN="Y"><LastName>Farzan</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Choe</LastName><ForeName>Hyeryun</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J 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MajorTopicYN="N">HIV-1</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009052" MajorTopicYN="N">Leukemia Virus, Murine</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase 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