Severe Acute Respiratory Syndrome Coronavirus nspl Suppresses Host Gene Expression, Including That of Type I Interferon, in Infected Cells
Identifieur interne : 003471 ( Main/Exploration ); précédent : 003470; suivant : 003472Severe Acute Respiratory Syndrome Coronavirus nspl Suppresses Host Gene Expression, Including That of Type I Interferon, in Infected Cells
Auteurs : Krishna Narayanan [États-Unis] ; CHENG HUANG [États-Unis] ; Kumari Lokugamage [États-Unis] ; Wataru Kamitani [États-Unis] ; Tetsuro Ikegami [États-Unis] ; Chien-Te K. Tseng [États-Unis] ; Shinji Makino [États-Unis]Source :
- Journal of virology [ 0022-538X ] ; 2008.
Descripteurs français
- KwdFr :
- ARN messager (métabolisme), Biosynthèse des protéines, Humains, Interféron de type I (génétique), Lignée cellulaire, Mutation, Protéines virales non structurales (physiologie), RNA replicase (physiologie), Régulation de l'expression des gènes, Stabilité de l'ARN, Virus du SRAS (pathogénicité), Virus du SRAS (physiologie).
- MESH :
- génétique : Interféron de type I.
- métabolisme : ARN messager.
- pathogénicité : Virus du SRAS.
- physiologie : Protéines virales non structurales, RNA replicase, Virus du SRAS.
- Pascal (Inist)
English descriptors
- KwdEn :
- Cell Line, Coronavirus, Cytokine, Gene Expression Regulation, Gene expression, Humans, Infected cell, Interferon, Interferon Type I (genetics), Mutation, Protein Biosynthesis, RNA Replicase (physiology), RNA Stability, RNA, Messenger (metabolism), SARS Virus (pathogenicity), SARS Virus (physiology), Severe acute respiratory syndrome, Viral Nonstructural Proteins (physiology), Virology.
- MESH :
- chemical , genetics : Interferon Type I.
- chemical , metabolism : RNA, Messenger.
- chemical , physiology : RNA Replicase, Viral Nonstructural Proteins.
- pathogenicity : SARS Virus.
- physiology : SARS Virus.
- Cell Line, Gene Expression Regulation, Humans, Mutation, Protein Biosynthesis, RNA Stability.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) nspl protein has unique biological functions that have not been described in the viral proteins of any RNA viruses; expressed SARS-CoV nspl protein has been found to suppress host gene expression by promoting host mRNA degradation and inhibiting translation. We generated an nspl mutant (nspl-mt) that neither promoted host mRNA degradation nor suppressed host protein synthesis in expressing cells. Both a SARS-CoV mutant virus, encoding the nspl-mt protein (SARS-CoV-mt), and a wild-type virus (SARS-CoV-WT) replicated efficiently and exhibited similar one-step growth kinetics in susceptible cells. Both viruses accumulated similar amounts of virus-specific mRNAs and nspl protein in infected cells, whereas the amounts of endogenous host mRNAs were clearly higher in SARS-CoV-mt-infected cells than in SARS-CoV-WT-infected cells, in both the presence and absence of actinomycin D. Further, SARS-CoV-WT replication strongly inhibited host protein synthesis, whereas host protein synthesis inhibition in SARS-CoV-mt-infected cells was not as efficient as in SARS-CoV-WT-infected cells. These data revealed that nspl indeed promoted host mRNA degradation and contributed to host protein translation inhibition in infected cells. Notably, SARS-CoV-mt infection, but not SARS-CoV-WT infection, induced high levels of beta interferon (IFN) mRNA accumulation and high titers of type I IFN production. These data demonstrated that SARS-CoV nspl suppressed host innate immune functions, including type I IFN expression, in infected cells and suggested that SARS-CoV nspl most probably plays a critical role in SARS-CoV virulence.
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77555-1019</wicri:noRegion></affiliation></author><author><name sortKey="Cheng Huang" sort="Cheng Huang" uniqKey="Cheng Huang" last="Cheng Huang">CHENG HUANG</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, The University of Texas Medical Branch at Galveston</s1><s2>Galveston, Texas 77555-1019</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Galveston, Texas 77555-1019</wicri:noRegion></affiliation></author><author><name sortKey="Lokugamage, Kumari" sort="Lokugamage, Kumari" uniqKey="Lokugamage K" first="Kumari" last="Lokugamage">Kumari Lokugamage</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, The University of Texas Medical Branch at Galveston</s1><s2>Galveston, Texas 77555-1019</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 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Texas Medical Branch at Galveston</s1><s2>Galveston, Texas 77555-1019</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Galveston, Texas 77555-1019</wicri:noRegion></affiliation></author><author><name sortKey="Tseng, Chien Te K" sort="Tseng, Chien Te K" uniqKey="Tseng C" first="Chien-Te K." last="Tseng">Chien-Te K. Tseng</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, The University of Texas Medical Branch at Galveston</s1><s2>Galveston, Texas 77555-1019</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Galveston, Texas 77555-1019</wicri:noRegion></affiliation></author><author><name sortKey="Makino, Shinji" sort="Makino, Shinji" uniqKey="Makino S" first="Shinji" last="Makino">Shinji Makino</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, The University of Texas Medical Branch at Galveston</s1><s2>Galveston, Texas 77555-1019</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>Galveston, Texas 77555-1019</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno><imprint><date when="2008">2008</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Coronavirus</term><term>Cytokine</term><term>Gene Expression Regulation</term><term>Gene expression</term><term>Humans</term><term>Infected cell</term><term>Interferon</term><term>Interferon Type I (genetics)</term><term>Mutation</term><term>Protein Biosynthesis</term><term>RNA Replicase (physiology)</term><term>RNA Stability</term><term>RNA, Messenger (metabolism)</term><term>SARS Virus (pathogenicity)</term><term>SARS Virus (physiology)</term><term>Severe acute respiratory syndrome</term><term>Viral Nonstructural Proteins (physiology)</term><term>Virology</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (métabolisme)</term><term>Biosynthèse des protéines</term><term>Humains</term><term>Interféron de type I (génétique)</term><term>Lignée cellulaire</term><term>Mutation</term><term>Protéines virales non structurales (physiologie)</term><term>RNA replicase (physiologie)</term><term>Régulation de l'expression des gènes</term><term>Stabilité de l'ARN</term><term>Virus du SRAS (pathogénicité)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Interferon Type I</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Interféron de type I</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines virales non structurales</term><term>RNA replicase</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Gene Expression Regulation</term><term>Humans</term><term>Mutation</term><term>Protein Biosynthesis</term><term>RNA Stability</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Coronavirus</term><term>Expression génique</term><term>Humains</term><term>Interféron</term><term>Cytokine</term><term>Cellule infectée</term><term>Lignée cellulaire</term><term>Mutation</term><term>Régulation de l'expression des gènes</term><term>Stabilité de l'ARN</term><term>Virologie</term><term>Syndrome respiratoire aigu sévère</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) nspl protein has unique biological functions that have not been described in the viral proteins of any RNA viruses; expressed SARS-CoV nspl protein has been found to suppress host gene expression by promoting host mRNA degradation and inhibiting translation. We generated an nspl mutant (nspl-mt) that neither promoted host mRNA degradation nor suppressed host protein synthesis in expressing cells. Both a SARS-CoV mutant virus, encoding the nspl-mt protein (SARS-CoV-mt), and a wild-type virus (SARS-CoV-WT) replicated efficiently and exhibited similar one-step growth kinetics in susceptible cells. Both viruses accumulated similar amounts of virus-specific mRNAs and nspl protein in infected cells, whereas the amounts of endogenous host mRNAs were clearly higher in SARS-CoV-mt-infected cells than in SARS-CoV-WT-infected cells, in both the presence and absence of actinomycin D. Further, SARS-CoV-WT replication strongly inhibited host protein synthesis, whereas host protein synthesis inhibition in SARS-CoV-mt-infected cells was not as efficient as in SARS-CoV-WT-infected cells. These data revealed that nspl indeed promoted host mRNA degradation and contributed to host protein translation inhibition in infected cells. Notably, SARS-CoV-mt infection, but not SARS-CoV-WT infection, induced high levels of beta interferon (IFN) mRNA accumulation and high titers of type I IFN production. These data demonstrated that SARS-CoV nspl suppressed host innate immune functions, including type I IFN expression, in infected cells and suggested that SARS-CoV nspl most probably plays a critical role in SARS-CoV virulence.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Narayanan, Krishna" sort="Narayanan, Krishna" uniqKey="Narayanan K" first="Krishna" last="Narayanan">Krishna Narayanan</name></noRegion><name sortKey="Cheng Huang" sort="Cheng Huang" uniqKey="Cheng Huang" last="Cheng Huang">CHENG HUANG</name><name sortKey="Ikegami, Tetsuro" sort="Ikegami, Tetsuro" uniqKey="Ikegami T" first="Tetsuro" last="Ikegami">Tetsuro Ikegami</name><name sortKey="Kamitani, Wataru" sort="Kamitani, Wataru" uniqKey="Kamitani W" first="Wataru" last="Kamitani">Wataru Kamitani</name><name sortKey="Lokugamage, Kumari" sort="Lokugamage, Kumari" uniqKey="Lokugamage K" first="Kumari" last="Lokugamage">Kumari Lokugamage</name><name sortKey="Makino, Shinji" sort="Makino, Shinji" uniqKey="Makino S" first="Shinji" last="Makino">Shinji Makino</name><name sortKey="Tseng, Chien Te K" sort="Tseng, Chien Te K" uniqKey="Tseng C" first="Chien-Te K." last="Tseng">Chien-Te K. 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