Characterization of a torovirus main proteinase
Identifieur interne : 000042 ( PascalFrancis/Corpus ); précédent : 000041; suivant : 000043Characterization of a torovirus main proteinase
Auteurs : Saskia L. Smits ; Eric J. Snijder ; Raoul J. De GrootSource :
- 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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Format Inist (serveur)
NO : | PASCAL 06-0212598 INIST |
---|---|
ET : | Characterization of a torovirus main proteinase |
AU : | SMITS (Saskia L.); SNIJDER (Eric J.); DE GROOT (Raoul J.) |
AF : | Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University/Utrecht/Pays-Bas (1 aut., 3 aut.); Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center/Leiden/Pays-Bas (2 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 8; Pp. 4157-4167; Bibl. 76 ref. |
LA : | Anglais |
EA : | 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. |
CC : | 002A05C10 |
FD : | Torovirus; Aspergillopepsin II; Microbiologie; Virologie |
FG : | Coronaviridae; Nidovirales; Virus; Aspartic endopeptidases; Peptidases; Hydrolases; Enzyme |
ED : | Torovirus; Aspergillopepsin II; Microbiology; Virology |
EG : | Coronaviridae; Nidovirales; Virus; Aspartic endopeptidases; Peptidases; Hydrolases; Enzyme |
SD : | Torovirus; Aspergillopepsin II; Microbiología; Virología |
LO : | INIST-13592.354000142800860460 |
ID : | 06-0212598 |
Links to Exploration step
Pascal:06-0212598Le document en format XML
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<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>
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<server><NO>PASCAL 06-0212598 INIST</NO>
<ET>Characterization of a torovirus main proteinase</ET>
<AU>SMITS (Saskia L.); SNIJDER (Eric J.); DE GROOT (Raoul J.)</AU>
<AF>Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University/Utrecht/Pays-Bas (1 aut., 3 aut.); Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center/Leiden/Pays-Bas (2 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 8; Pp. 4157-4167; Bibl. 76 ref.</SO>
<LA>Anglais</LA>
<EA>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.</EA>
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