Characterization of a torovirus main proteinase
Identifieur interne : 001742 ( Main/Exploration ); précédent : 001741; suivant : 001743Characterization of a torovirus main proteinase
Auteurs : Saskia L. Smits [Pays-Bas] ; Eric J. Snijder [Pays-Bas] ; Raoul J. De Groot [Pays-Bas]Source :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
Viruses of the order Nidovirales encode huge replicase polyproteins. These are processed primarily by the chymotrypsin-like main proteinases (Mpros). So far, Mpros have been studied only for corona-, arteri-, and roniviruses. Here, we report the characterization of the Mpro of toroviruses, the fourth main Nidovirus branch. Comparative sequence analysis of polyprotein la of equine torovirus (EToV) strain Berne, identified a serine proteinase domain, flanked by hydrophobic regions. Heterologous expression of this domain resulted in autoprocessing at flanking cleavage sites. N-terminal sequence analysis of cleavage products tentatively identified FxxQ ↓ (S, A) as the substrate consensus sequence. EToV Mpro combines several traits of its closest relatives. It has a predicted three-domain structure, with two catalytic β-barrel domains and an additional C-terminal domain of unknown function. With respect to substrate specificity, the EToV Mpro resembles its coronavirus homologue in its preference for P1-Gln, but its substrate-binding subsite, S1, more closely resembles that of arteri- and ronivirus Mpros, which prefer P1-Glu. Surprisingly, in contrast to the Mpros of corona- and roniviruses, but like that of arterivirus, the torovirus Mpro uses serine instead of cysteine as its principal nucleophile. Under the premise that the Mpros of corona- and toroviruses are more closely related to each other than to those of arteri- and roniviruses, the transition from serine- to cysteine-based proteolytic catalysis (or vice versa) must have happened more than once in the course of nidovirus evolution. In this respect, it is of interest that a mutant EToV Mpro with a Ser165→Cys substitution retained partial enzymatic activity.
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De Groot</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University</s1><s2>Utrecht</s2><s3>NLD</s3><sZ>1 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Utrecht</settlement><region nuts="2" type="province">Utrecht (province)</region></placeName><orgName type="university">Université d'Utrecht</orgName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">INIST</idno><idno type="inist">06-0212598</idno><date when="2006">2006</date><idno type="stanalyst">PASCAL 06-0212598 INIST</idno><idno type="RBID">Pascal:06-0212598</idno><idno type="wicri:Area/PascalFrancis/Corpus">000042</idno><idno type="wicri:Area/PascalFrancis/Curation">000017</idno><idno type="wicri:Area/PascalFrancis/Checkpoint">000040</idno><idno type="wicri:explorRef" wicri:stream="PascalFrancis" wicri:step="Checkpoint">000040</idno><idno type="wicri:doubleKey">0022-538X:2006:Smits S:characterization:of:a</idno><idno type="wicri:Area/Main/Merge">001749</idno><idno type="wicri:Area/Main/Curation">001742</idno><idno type="wicri:Area/Main/Exploration">001742</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Characterization of a torovirus main proteinase</title><author><name sortKey="Smits, Saskia L" sort="Smits, Saskia L" uniqKey="Smits S" first="Saskia L." last="Smits">Saskia L. Smits</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University</s1><s2>Utrecht</s2><s3>NLD</s3><sZ>1 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Utrecht</settlement><region nuts="2" type="province">Utrecht (province)</region></placeName><orgName type="university">Université d'Utrecht</orgName></affiliation></author><author><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J." last="Snijder">Eric J. Snijder</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center</s1><s2>Leiden</s2><s3>NLD</s3><sZ>2 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation></author><author><name sortKey="De Groot, Raoul J" sort="De Groot, Raoul J" uniqKey="De Groot R" first="Raoul J." last="De Groot">Raoul J. De Groot</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University</s1><s2>Utrecht</s2><s3>NLD</s3><sZ>1 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Utrecht</settlement><region nuts="2" type="province">Utrecht (province)</region></placeName><orgName type="university">Université d'Utrecht</orgName></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="2006">2006</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>Aspergillopepsin II</term><term>Microbiology</term><term>Torovirus</term><term>Virology</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Torovirus</term><term>Aspergillopepsin II</term><term>Microbiologie</term><term>Virologie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Viruses of the order Nidovirales encode huge replicase polyproteins. These are processed primarily by the chymotrypsin-like main proteinases (M<sup>pro</sup>s). So far, M<sup>pro</sup>s have been studied only for corona-, arteri-, and roniviruses. Here, we report the characterization of the M<sup>pro</sup> of toroviruses, the fourth main Nidovirus branch. Comparative sequence analysis of polyprotein la of equine torovirus (EToV) strain Berne, identified a serine proteinase domain, flanked by hydrophobic regions. Heterologous expression of this domain resulted in autoprocessing at flanking cleavage sites. N-terminal sequence analysis of cleavage products tentatively identified FxxQ ↓ (S, A) as the substrate consensus sequence. EToV M<sup>pro</sup> combines several traits of its closest relatives. It has a predicted three-domain structure, with two catalytic β-barrel domains and an additional C-terminal domain of unknown function. With respect to substrate specificity, the EToV M<sup>pro</sup> resembles its coronavirus homologue in its preference for P1-Gln, but its substrate-binding subsite, S1, more closely resembles that of arteri- and ronivirus M<sup>pro</sup>s, which prefer P1-Glu. Surprisingly, in contrast to the M<sup>pro</sup>s of corona- and roniviruses, but like that of arterivirus, the torovirus M<sup>pro</sup> uses serine instead of cysteine as its principal nucleophile. Under the premise that the M<sup>pro</sup>s of corona- and toroviruses are more closely related to each other than to those of arteri- and roniviruses, the transition from serine- to cysteine-based proteolytic catalysis (or vice versa) must have happened more than once in the course of nidovirus evolution. In this respect, it is of interest that a mutant EToV M<sup>pro</sup> with a Ser<sup>165</sup>→Cys substitution retained partial enzymatic activity.</div></front></TEI><affiliations><list><country><li>Pays-Bas</li></country><region><li>Hollande-Méridionale</li><li>Utrecht (province)</li></region><settlement><li>Leyde</li><li>Utrecht</li></settlement><orgName><li>Université d'Utrecht</li></orgName></list><tree><country name="Pays-Bas"><region name="Utrecht (province)"><name sortKey="Smits, Saskia L" sort="Smits, Saskia L" uniqKey="Smits S" first="Saskia L." last="Smits">Saskia L. Smits</name></region><name sortKey="De Groot, Raoul J" sort="De Groot, Raoul J" uniqKey="De Groot R" first="Raoul J." last="De Groot">Raoul J. De Groot</name><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J." last="Snijder">Eric J. Snijder</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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