CovidV2, PascalFrancis, Curation, bibRecord, 000017

Characterization of a torovirus main proteinase

Identifieur interne : 000017 ( PascalFrancis/Curation ); précédent : 000016; suivant : 000018

Characterization 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.

RBID : Pascal:06-0212598

Descripteurs français

Pascal (Inist)
- Torovirus, Aspergillopepsin II, Microbiologie, Virologie.

English descriptors

KwdEn :
- Aspergillopepsin II, Microbiology, Torovirus, Virology.

Abstract

Viruses of the order Nidovirales encode huge replicase polyproteins. These are processed primarily by the chymotrypsin-like main proteinases (M^pros). So far, M^pros have been studied only for corona-, arteri-, and roniviruses. Here, we report the characterization of the M^pro 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^pro 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^pro 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^pros, which prefer P1-Glu. Surprisingly, in contrast to the M^pros of corona- and roniviruses, but like that of arterivirus, the torovirus M^pro uses serine instead of cysteine as its principal nucleophile. Under the premise that the M^pros 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^pro with a Ser¹⁶⁵→Cys substitution retained partial enzymatic activity.

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A03		`1`		`@0 J. virol.`
A05				`@2 80`
A06				`@2 8`
A08	`01`	`1`	`ENG`	`@1 Characterization of a torovirus main proteinase`
A11	`01`	`1`		`@1 SMITS (Saskia L.)`
A11	`02`	`1`		`@1 SNIJDER (Eric J.)`
A11	`03`	`1`		`@1 DE GROOT (Raoul J.)`
A14	`01`			`@1 Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University @2 Utrecht @3 NLD @Z 1 aut. @Z 3 aut.`
A14	`02`			`@1 Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center @2 Leiden @3 NLD @Z 2 aut.`
A20				`@1 4157-4167`
A21				`@1 2006`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 13592 @5 354000142800860460`
A44				`@0 0000 @1 © 2006 INIST-CNRS. All rights reserved.`
A45				`@0 76 ref.`
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A64	`01`	`1`		`@0 Journal of virology`
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C01	`01`		`ENG`	@0 Viruses of the order Nidovirales encode huge replicase polyproteins. These are processed primarily by the chymotrypsin-like main proteinases (M^pros). So far, M^pros have been studied only for corona-, arteri-, and roniviruses. Here, we report the characterization of the M^pro 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^pro 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^pro 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^pros, which prefer P1-Glu. Surprisingly, in contrast to the M^pros of corona- and roniviruses, but like that of arterivirus, the torovirus M^pro uses serine instead of cysteine as its principal nucleophile. Under the premise that the M^pros 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^pro with a Ser¹⁶⁵→Cys substitution retained partial enzymatic activity.
C02	`01`	`X`		`@0 002A05C10`
C03	`01`	`X`	`FRE`	`@0 Torovirus @2 NW @5 01`
C03	`01`	`X`	`ENG`	`@0 Torovirus @2 NW @5 01`
C03	`01`	`X`	`SPA`	`@0 Torovirus @2 NW @5 01`
C03	`02`	`X`	`FRE`	`@0 Aspergillopepsin II @2 FE @5 05`
C03	`02`	`X`	`ENG`	`@0 Aspergillopepsin II @2 FE @5 05`
C03	`02`	`X`	`SPA`	`@0 Aspergillopepsin II @2 FE @5 05`
C03	`03`	`X`	`FRE`	`@0 Microbiologie @5 06`
C03	`03`	`X`	`ENG`	`@0 Microbiology @5 06`
C03	`03`	`X`	`SPA`	`@0 Microbiología @5 06`
C03	`04`	`X`	`FRE`	`@0 Virologie @5 07`
C03	`04`	`X`	`ENG`	`@0 Virology @5 07`
C03	`04`	`X`	`SPA`	`@0 Virología @5 07`
C07	`01`	`X`	`FRE`	`@0 Coronaviridae @2 NW`
C07	`01`	`X`	`ENG`	`@0 Coronaviridae @2 NW`
C07	`01`	`X`	`SPA`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`FRE`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`ENG`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`SPA`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`03`	`X`	`ENG`	`@0 Virus @2 NW`
C07	`03`	`X`	`SPA`	`@0 Virus @2 NW`
C07	`04`	`X`	`FRE`	`@0 Aspartic endopeptidases @2 FE`
C07	`04`	`X`	`ENG`	`@0 Aspartic endopeptidases @2 FE`
C07	`04`	`X`	`SPA`	`@0 Aspartic endopeptidases @2 FE`
C07	`05`	`X`	`FRE`	`@0 Peptidases @2 FE`
C07	`05`	`X`	`ENG`	`@0 Peptidases @2 FE`
C07	`05`	`X`	`SPA`	`@0 Peptidases @2 FE`
C07	`06`	`X`	`FRE`	`@0 Hydrolases @2 FE`
C07	`06`	`X`	`ENG`	`@0 Hydrolases @2 FE`
C07	`06`	`X`	`SPA`	`@0 Hydrolases @2 FE`
C07	`07`	`X`	`FRE`	`@0 Enzyme @2 FE`
C07	`07`	`X`	`ENG`	`@0 Enzyme @2 FE`
C07	`07`	`X`	`SPA`	`@0 Enzima @2 FE`
N21				`@1 135`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

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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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<fC01 i1="01" l="ENG"><s0>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>
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<s2>FE</s2>
<s5>05</s5>
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<fC03 i1="02" i2="X" l="SPA"><s0>Aspergillopepsin II</s0>
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   |étape=   Curation
   |type=    RBID
   |clé=     Pascal:06-0212598
   |texte=   Characterization of a torovirus main proteinase
}}

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	Serveur d'exploration Covid (26 mars)
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Serveur d'exploration Covid (26 mars)

Characterization of a torovirus main proteinase

Characterization of a torovirus main proteinase

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