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
Links to Exploration step
pubmed:18926799Le document en format XML
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<term>Nucleocapsid Proteins (isolation & purification)</term>
<term>Peptide Fragments (chemistry)</term>
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<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>
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