Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63
Identifieur interne : 000368 ( PascalFrancis/Corpus ); précédent : 000367; suivant : 000369Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63
Auteurs : ZHONGBIN CHEN ; YANHUA WANG ; Kiira Ratia ; Andrew D. Mesecar ; Keith D. Wilkinson ; Susan C. BakerSource :
- Journal of virology [ 0022-538X ] ; 2007.
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Abstract
Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nspl, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV.
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Format Inist (serveur)
| NO : | PASCAL 07-0279094 INIST |
|---|---|
| ET : | Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63 |
| AU : | ZHONGBIN CHEN; YANHUA WANG; RATIA (Kiira); MESECAR (Andrew D.); WILKINSON (Keith D.); BAKER (Susan C.) |
| AF : | Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine/Maywood, Illinois/Etats-Unis (1 aut., 2 aut., 6 aut.); Department of Biochemistry and Molecular Biology, Beijing Institute of Radiation Medicine/Beijing/Chine (1 aut.); Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago/Chicago, Illinois/Etats-Unis (3 aut., 4 aut.); Department of Biochemistry, Emory University School of Medicine/Atlanta, Georgia/Etats-Unis (5 aut.) |
| DT : | Publication en série; Niveau analytique |
| SO : | Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 11; Pp. 6007-6018; Bibl. 71 ref. |
| LA : | Anglais |
| EA : | Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nspl, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV. |
| CC : | 002A05C10 |
| FD : | Homme; Coronavirus; Papain; Virologie |
| FG : | Coronaviridae; Nidovirales; Virus; Cysteine endopeptidases; Peptidases; Hydrolases; Enzyme |
| ED : | Human; Coronavirus; Papain; Virology |
| EG : | Coronaviridae; Nidovirales; Virus; Cysteine endopeptidases; Peptidases; Hydrolases; Enzyme |
| SD : | Hombre; Coronavirus; Papain; Virología |
| LO : | INIST-13592.354000146868860550 |
| ID : | 07-0279094 |
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Mesecar</name><affiliation><inist:fA14 i1="03"><s1>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago</s1><s2>Chicago, Illinois</s2><s3>USA</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Wilkinson, Keith D" sort="Wilkinson, Keith D" uniqKey="Wilkinson K" first="Keith D." last="Wilkinson">Keith D. Wilkinson</name><affiliation><inist:fA14 i1="04"><s1>Department of Biochemistry, Emory University School of Medicine</s1><s2>Atlanta, Georgia</s2><s3>USA</s3><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><affiliation><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine</s1><s2>Maywood, Illinois</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">INIST</idno><idno type="inist">07-0279094</idno><date when="2007">2007</date><idno type="stanalyst">PASCAL 07-0279094 INIST</idno><idno type="RBID">Pascal:07-0279094</idno><idno type="wicri:Area/PascalFrancis/Corpus">000368</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63</title><author><name sortKey="Zhongbin Chen" sort="Zhongbin Chen" uniqKey="Zhongbin Chen" last="Zhongbin Chen">ZHONGBIN CHEN</name><affiliation><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine</s1><s2>Maywood, Illinois</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14></affiliation><affiliation><inist:fA14 i1="02"><s1>Department of Biochemistry and Molecular Biology, Beijing Institute of Radiation Medicine</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Yanhua Wang" sort="Yanhua Wang" uniqKey="Yanhua Wang" last="Yanhua Wang">YANHUA WANG</name><affiliation><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine</s1><s2>Maywood, Illinois</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name><affiliation><inist:fA14 i1="03"><s1>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago</s1><s2>Chicago, Illinois</s2><s3>USA</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name><affiliation><inist:fA14 i1="03"><s1>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago</s1><s2>Chicago, Illinois</s2><s3>USA</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Wilkinson, Keith D" sort="Wilkinson, Keith D" uniqKey="Wilkinson K" first="Keith D." last="Wilkinson">Keith D. Wilkinson</name><affiliation><inist:fA14 i1="04"><s1>Department of Biochemistry, Emory University School of Medicine</s1><s2>Atlanta, Georgia</s2><s3>USA</s3><sZ>5 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><affiliation><inist:fA14 i1="01"><s1>Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine</s1><s2>Maywood, Illinois</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14></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="2007">2007</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>Coronavirus</term><term>Human</term><term>Papain</term><term>Virology</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Homme</term><term>Coronavirus</term><term>Papain</term><term>Virologie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nspl, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV.</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0022-538X</s0></fA01><fA03 i2="1"><s0>J. virol.</s0></fA03><fA05><s2>81</s2></fA05><fA06><s2>11</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63</s1></fA08><fA11 i1="01" i2="1"><s1>ZHONGBIN CHEN</s1></fA11><fA11 i1="02" i2="1"><s1>YANHUA WANG</s1></fA11><fA11 i1="03" i2="1"><s1>RATIA (Kiira)</s1></fA11><fA11 i1="04" i2="1"><s1>MESECAR (Andrew D.)</s1></fA11><fA11 i1="05" i2="1"><s1>WILKINSON (Keith D.)</s1></fA11><fA11 i1="06" i2="1"><s1>BAKER (Susan C.)</s1></fA11><fA14 i1="01"><s1>Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine</s1><s2>Maywood, Illinois</s2><s3>USA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></fA14><fA14 i1="02"><s1>Department of Biochemistry and Molecular Biology, Beijing Institute of Radiation Medicine</s1><s2>Beijing</s2><s3>CHN</s3><sZ>1 aut.</sZ></fA14><fA14 i1="03"><s1>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago</s1><s2>Chicago, Illinois</s2><s3>USA</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ></fA14><fA14 i1="04"><s1>Department of Biochemistry, Emory University School of Medicine</s1><s2>Atlanta, Georgia</s2><s3>USA</s3><sZ>5 aut.</sZ></fA14><fA20><s1>6007-6018</s1></fA20><fA21><s1>2007</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>13592</s2><s5>354000146868860550</s5></fA43><fA44><s0>0000</s0><s1>© 2007 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>71 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>07-0279094</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of virology</s0></fA64><fA66 i1="01"><s0>USA</s0></fA66><fC01 i1="01" l="ENG"><s0>Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nspl, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV.</s0></fC01><fC02 i1="01" i2="X"><s0>002A05C10</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Homme</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Human</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Hombre</s0><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Coronavirus</s0><s2>NW</s2><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Coronavirus</s0><s2>NW</s2><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Coronavirus</s0><s2>NW</s2><s5>02</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Papain</s0><s2>FE</s2><s5>05</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Papain</s0><s2>FE</s2><s5>05</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Papain</s0><s2>FE</s2><s5>05</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Virologie</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Virology</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Virología</s0><s5>07</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Cysteine endopeptidases</s0><s2>FE</s2></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Cysteine endopeptidases</s0><s2>FE</s2></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Cysteine endopeptidases</s0><s2>FE</s2></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Peptidases</s0><s2>FE</s2></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Peptidases</s0><s2>FE</s2></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Peptidases</s0><s2>FE</s2></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Hydrolases</s0><s2>FE</s2></fC07><fC07 i1="07" i2="X" l="FRE"><s0>Enzyme</s0><s2>FE</s2></fC07><fC07 i1="07" i2="X" l="ENG"><s0>Enzyme</s0><s2>FE</s2></fC07><fC07 i1="07" i2="X" l="SPA"><s0>Enzima</s0><s2>FE</s2></fC07><fN21><s1>183</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard><server><NO>PASCAL 07-0279094 INIST</NO><ET>Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63</ET><AU>ZHONGBIN CHEN; YANHUA WANG; RATIA (Kiira); MESECAR (Andrew D.); WILKINSON (Keith D.); BAKER (Susan C.)</AU><AF>Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine/Maywood, Illinois/Etats-Unis (1 aut., 2 aut., 6 aut.); Department of Biochemistry and Molecular Biology, Beijing Institute of Radiation Medicine/Beijing/Chine (1 aut.); Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago/Chicago, Illinois/Etats-Unis (3 aut., 4 aut.); Department of Biochemistry, Emory University School of Medicine/Atlanta, Georgia/Etats-Unis (5 aut.)</AF><DT>Publication en série; Niveau analytique</DT><SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2007; Vol. 81; No. 11; Pp. 6007-6018; Bibl. 71 ref.</SO><LA>Anglais</LA><EA>Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nspl, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV.</EA><CC>002A05C10</CC><FD>Homme; Coronavirus; Papain; Virologie</FD><FG>Coronaviridae; Nidovirales; Virus; Cysteine endopeptidases; Peptidases; Hydrolases; Enzyme</FG><ED>Human; Coronavirus; Papain; Virology</ED><EG>Coronaviridae; Nidovirales; Virus; Cysteine endopeptidases; Peptidases; Hydrolases; Enzyme</EG><SD>Hombre; Coronavirus; Papain; Virología</SD><LO>INIST-13592.354000146868860550</LO><ID>07-0279094</ID></server></inist></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63
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