Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein.
Identifieur interne : 003221 ( PubMed/Corpus ); précédent : 003220; suivant : 003222Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein.
Auteurs : Valérie Campanacci ; Marie-Pierre Egloff ; Sonia Longhi ; François Ferron ; Corinne Rancurel ; Aurelia Salomoni ; Cécile Durousseau ; Fabienne Tocque ; Nicolas Brémond ; Jessika C. Dobbe ; Eric J. Snijder ; Bruno Canard ; Christian CambillauSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2003.
English descriptors
- KwdEn :
- Amino Acid Sequence, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Genomics, RNA-Binding Proteins (chemistry), SARS Virus (chemistry), SARS Virus (genetics), Sequence Alignment, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (isolation & purification), Viral Proteins (chemistry).
- MESH :
- chemical , chemistry : RNA-Binding Proteins, Viral Nonstructural Proteins, Viral Proteins.
- chemistry : SARS Virus.
- genetics : SARS Virus, Viral Nonstructural Proteins.
- chemical , isolation & purification : Viral Nonstructural Proteins.
- Amino Acid Sequence, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Genomics, Sequence Alignment.
Abstract
The aetiologic agent of the recent epidemics of Severe Acute Respiratory Syndrome (SARS) is a positive-stranded RNA virus (SARS-CoV) belonging to the Coronaviridae family and its genome differs substantially from those of other known coronaviruses. SARS-CoV is transmissible mainly by the respiratory route and to date there is no vaccine and no prophylactic or therapeutic treatments against this agent. A SARS-CoV whole-genome approach has been developed aimed at determining the crystal structure of all of its proteins or domains. These studies are expected to greatly facilitate drug design. The genomes of coronaviruses are between 27 and 31.5 kbp in length, the largest of the known RNA viruses, and encode 20-30 mature proteins. The functions of many of these polypeptides, including the Nsp9-Nsp10 replicase-cleavage products, are still unknown. Here, the cloning, Escherichia coli expression, purification and crystallization of the SARS-CoV Nsp9 protein, the first SARS-CoV protein to be crystallized, are reported. Nsp9 crystals diffract to 2.8 A resolution and belong to space group P6(1/5)22, with unit-cell parameters a = b = 89.7, c = 136.7 A. With two molecules in the asymmetric unit, the solvent content is 60% (V(M) = 3.1 A(3) Da(-1)).
DOI: 10.1107/s0907444903016779
PubMed: 12925794
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pubmed:12925794Le document en format XML
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Dobbe</name></author><author><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J" last="Snijder">Eric J. Snijder</name></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name></author><author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="ISSN">0907-4449</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Genomics</term><term>RNA-Binding Proteins (chemistry)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (genetics)</term><term>Sequence Alignment</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (isolation & purification)</term><term>Viral Proteins (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA-Binding Proteins</term><term>Viral Nonstructural Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Genomics</term><term>Sequence Alignment</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The aetiologic agent of the recent epidemics of Severe Acute Respiratory Syndrome (SARS) is a positive-stranded RNA virus (SARS-CoV) belonging to the Coronaviridae family and its genome differs substantially from those of other known coronaviruses. SARS-CoV is transmissible mainly by the respiratory route and to date there is no vaccine and no prophylactic or therapeutic treatments against this agent. A SARS-CoV whole-genome approach has been developed aimed at determining the crystal structure of all of its proteins or domains. These studies are expected to greatly facilitate drug design. The genomes of coronaviruses are between 27 and 31.5 kbp in length, the largest of the known RNA viruses, and encode 20-30 mature proteins. The functions of many of these polypeptides, including the Nsp9-Nsp10 replicase-cleavage products, are still unknown. Here, the cloning, Escherichia coli expression, purification and crystallization of the SARS-CoV Nsp9 protein, the first SARS-CoV protein to be crystallized, are reported. Nsp9 crystals diffract to 2.8 A resolution and belong to space group P6(1/5)22, with unit-cell parameters a = b = 89.7, c = 136.7 A. With two molecules in the asymmetric unit, the solvent content is 60% (V(M) = 3.1 A(3) Da(-1)).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12925794</PMID><DateCompleted><Year>2004</Year><Month>06</Month><Day>01</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>59</Volume><Issue>Pt 9</Issue><PubDate><Year>2003</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr. D Biol. Crystallogr.</ISOAbbreviation></Journal><ArticleTitle>Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein.</ArticleTitle><Pagination><MedlinePgn>1628-31</MedlinePgn></Pagination><Abstract><AbstractText>The aetiologic agent of the recent epidemics of Severe Acute Respiratory Syndrome (SARS) is a positive-stranded RNA virus (SARS-CoV) belonging to the Coronaviridae family and its genome differs substantially from those of other known coronaviruses. SARS-CoV is transmissible mainly by the respiratory route and to date there is no vaccine and no prophylactic or therapeutic treatments against this agent. A SARS-CoV whole-genome approach has been developed aimed at determining the crystal structure of all of its proteins or domains. These studies are expected to greatly facilitate drug design. The genomes of coronaviruses are between 27 and 31.5 kbp in length, the largest of the known RNA viruses, and encode 20-30 mature proteins. The functions of many of these polypeptides, including the Nsp9-Nsp10 replicase-cleavage products, are still unknown. Here, the cloning, Escherichia coli expression, purification and crystallization of the SARS-CoV Nsp9 protein, the first SARS-CoV protein to be crystallized, are reported. Nsp9 crystals diffract to 2.8 A resolution and belong to space group P6(1/5)22, with unit-cell parameters a = b = 89.7, c = 136.7 A. With two molecules in the asymmetric unit, the solvent content is 60% (V(M) = 3.1 A(3) Da(-1)).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Campanacci</LastName><ForeName>Valérie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Egloff</LastName><ForeName>Marie-Pierre</ForeName><Initials>MP</Initials></Author><Author ValidYN="Y"><LastName>Longhi</LastName><ForeName>Sonia</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Ferron</LastName><ForeName>François</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Rancurel</LastName><ForeName>Corinne</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Salomoni</LastName><ForeName>Aurelia</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Durousseau</LastName><ForeName>Cécile</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Tocque</LastName><ForeName>Fabienne</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Brémond</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Dobbe</LastName><ForeName>Jessika C</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Snijder</LastName><ForeName>Eric J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Cambillau</LastName><ForeName>Christian</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2003</Year><Month>08</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA><NlmUniqueID>9305878</NlmUniqueID><ISSNLinking>0907-4449</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C087633">nonstructural protein, coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C483945">nsp9 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UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2003</Year><Month>07</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2003</Year><Month>07</Month><Day>30</Day></PubMedPubDate><PubMedPubDate 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