Characterization of a torovirus main proteinase
Identifieur interne : 000040 ( PascalFrancis/Checkpoint ); précédent : 000039; suivant : 000041Characterization 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.
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
Pascal:06-0212598Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><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>
</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>
</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>
<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>80</s2>
</fA05>
<fA06><s2>8</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>Characterization of a torovirus main proteinase</s1>
</fA08>
<fA11 i1="01" i2="1"><s1>SMITS (Saskia L.)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>SNIJDER (Eric J.)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>DE GROOT (Raoul J.)</s1>
</fA11>
<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>
</fA14>
<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>
</fA14>
<fA20><s1>4157-4167</s1>
</fA20>
<fA21><s1>2006</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>13592</s2>
<s5>354000142800860460</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2006 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>76 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>06-0212598</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>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.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A05C10</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Torovirus</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Torovirus</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Torovirus</s0>
<s2>NW</s2>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Aspergillopepsin II</s0>
<s2>FE</s2>
<s5>05</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Aspergillopepsin II</s0>
<s2>FE</s2>
<s5>05</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Aspergillopepsin II</s0>
<s2>FE</s2>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Microbiologie</s0>
<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Microbiology</s0>
<s5>06</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Microbiología</s0>
<s5>06</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>Aspartic endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Aspartic endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Aspartic 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>135</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
</inist>
<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)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/CovidV2/Data/PascalFrancis/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000040 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PascalFrancis/Checkpoint/biblio.hfd -nk 000040 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= CovidV2 |flux= PascalFrancis |étape= Checkpoint |type= RBID |clé= Pascal:06-0212598 |texte= Characterization of a torovirus main proteinase }}
This area was generated with Dilib version V0.6.33. |