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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<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>
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<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>
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