SARS coronavirus: unusual lability of the nucleocapsid protein.
Identifieur interne : 001A50 ( PubMed/Corpus ); précédent : 001A49; suivant : 001A51SARS coronavirus: unusual lability of the nucleocapsid protein.
Auteurs : John Mark ; Xuguang Li ; Terry Cyr ; Sylvie Fournier ; Bozena Jaentschke ; Mary Alice HeffordSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2008.
English descriptors
- KwdEn :
- Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Nucleocapsid Proteins (biosynthesis), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (isolation & purification), Peptide Fragments (chemistry), Peptide Fragments (metabolism), Peptide Hydrolases (chemistry), Peptide Hydrolases (metabolism), Protein Folding, SARS Virus (metabolism), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
- MESH :
- chemical , biosynthesis : Nucleocapsid Proteins.
- chemical , chemistry : Nucleocapsid Proteins, Peptide Fragments, Peptide Hydrolases.
- chemical , isolation & purification : Nucleocapsid Proteins.
- chemical , metabolism : Peptide Fragments, Peptide Hydrolases.
- metabolism : SARS Virus.
- Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Protein Folding, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
Abstract
The severe acute respiratory syndrome (SARS) is a contagious disease that killed hundreds and sickened thousands of people worldwide between November 2002 and July 2003. The nucleocapsid (N) protein of the coronavirus responsible for this disease plays a critical role in viral assembly and maturation and is of particular interest because of its potential as an antiviral target or vaccine candidate. Refolding of SARS N-protein during production and purification showed the presence of two additional protein bands by SDS-PAGE. Mass spectroscopy (MALDI, SELDI, and LC/MS) confirmed that the bands are proteolytic products of N-protein and the cleavage sites are four SR motifs in the serine-arginine-rich region-sites not suggestive of any known protease. Furthermore, results of subsequent testing for contaminating protease(s) were negative: cleavage appears to be due to inherent instability and/or autolysis. The importance of N-protein proteolysis to viral life cycle and thus to possible treatment directions are discussed.
DOI: 10.1016/j.bbrc.2008.09.153
PubMed: 18926799
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Electronic address: Mary_Hefford@hc-sc.gc.ca.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Liquid</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Nucleocapsid Proteins (biosynthesis)</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (isolation & purification)</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (metabolism)</term><term>Peptide Hydrolases (chemistry)</term><term>Peptide Hydrolases (metabolism)</term><term>Protein Folding</term><term>SARS Virus (metabolism)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Peptide Fragments</term><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Fragments</term><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Liquid</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Protein Folding</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome (SARS) is a contagious disease that killed hundreds and sickened thousands of people worldwide between November 2002 and July 2003. The nucleocapsid (N) protein of the coronavirus responsible for this disease plays a critical role in viral assembly and maturation and is of particular interest because of its potential as an antiviral target or vaccine candidate. Refolding of SARS N-protein during production and purification showed the presence of two additional protein bands by SDS-PAGE. Mass spectroscopy (MALDI, SELDI, and LC/MS) confirmed that the bands are proteolytic products of N-protein and the cleavage sites are four SR motifs in the serine-arginine-rich region-sites not suggestive of any known protease. Furthermore, results of subsequent testing for contaminating protease(s) were negative: cleavage appears to be due to inherent instability and/or autolysis. The importance of N-protein proteolysis to viral life cycle and thus to possible treatment directions are discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18926799</PMID><DateCompleted><Year>2008</Year><Month>12</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>04</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>377</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Dec</Month><Day>12</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>SARS coronavirus: unusual lability of the nucleocapsid protein.</ArticleTitle><Pagination><MedlinePgn>429-433</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(08)01940-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2008.09.153</ELocationID><Abstract><AbstractText>The severe acute respiratory syndrome (SARS) is a contagious disease that killed hundreds and sickened thousands of people worldwide between November 2002 and July 2003. The nucleocapsid (N) protein of the coronavirus responsible for this disease plays a critical role in viral assembly and maturation and is of particular interest because of its potential as an antiviral target or vaccine candidate. Refolding of SARS N-protein during production and purification showed the presence of two additional protein bands by SDS-PAGE. Mass spectroscopy (MALDI, SELDI, and LC/MS) confirmed that the bands are proteolytic products of N-protein and the cleavage sites are four SR motifs in the serine-arginine-rich region-sites not suggestive of any known protease. Furthermore, results of subsequent testing for contaminating protease(s) were negative: cleavage appears to be due to inherent instability and/or autolysis. The importance of N-protein proteolysis to viral life cycle and thus to possible treatment directions are discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mark</LastName><ForeName>John</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, AL:2201E, Ottawa, Ont., Canada K1A 0L2.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xuguang</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, AL:2201E, Ottawa, Ont., Canada K1A 0L2.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cyr</LastName><ForeName>Terry</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, AL:2201E, Ottawa, Ont., Canada K1A 0L2.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fournier</LastName><ForeName>Sylvie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, AL:2201E, Ottawa, Ont., Canada K1A 0L2.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jaentschke</LastName><ForeName>Bozena</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, AL:2201E, Ottawa, Ont., Canada K1A 0L2.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hefford</LastName><ForeName>Mary Alice</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, 251 Sir Frederick Banting Driveway, AL:2201E, Ottawa, Ont., Canada K1A 0L2. 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