Low Stability of Nucleocapsid Protein in SARS Virus†
Identifieur interne : 005555 ( Main/Exploration ); précédent : 005554; suivant : 005556Low Stability of Nucleocapsid Protein in SARS Virus†
Auteurs : Yulong Wang [République populaire de Chine] ; Xiaoyu Wu [République populaire de Chine] ; Yihua Wang [République populaire de Chine] ; Bing Li [République populaire de Chine] ; Hao Zhou [République populaire de Chine] ; Guiyong Yuan [République populaire de Chine] ; Yan Fu [République populaire de Chine] ; Yongzhang Luo [République populaire de Chine]Source :
- Biochemistry [ 0006-2960 ] ; 2004.
Descripteurs français
- KwdFr :
- Cations monovalents, Chlorure de sodium (), Concentration en ions d'hydrogène, Dénaturation des protéines, Guanidine (), Humains, Inactivation virale, Pliage des protéines, Protéines nucléocapside (), Protéines nucléocapside (biosynthèse), Protéines nucléocapside (génétique), Protéines nucléocapside (isolement et purification), Syndrome respiratoire aigu sévère (virologie), Température élevée, Thermodynamique, Urée (), Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (physiologie).
- MESH :
- biosynthèse : Protéines nucléocapside.
- génétique : Protéines nucléocapside, Virus du SRAS.
- isolement et purification : Protéines nucléocapside.
- physiologie : Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Cations monovalents, Chlorure de sodium, Concentration en ions d'hydrogène, Dénaturation des protéines, Guanidine, Humains, Inactivation virale, Pliage des protéines, Protéines nucléocapside, Température élevée, Thermodynamique, Urée, Virus du SRAS.
English descriptors
- KwdEn :
- Cations, Monovalent, Guanidine (chemistry), Hot Temperature, Humans, Hydrogen-Ion Concentration, Nucleocapsid Proteins (biosynthesis), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (isolation & purification), Protein Denaturation, Protein Folding, SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (physiology), Severe Acute Respiratory Syndrome (virology), Sodium Chloride (chemistry), Thermodynamics, Urea (chemistry), Virus Inactivation.
- MESH :
- chemical , biosynthesis : Nucleocapsid Proteins.
- chemical , chemistry : Guanidine, Nucleocapsid Proteins, Sodium Chloride, Urea.
- chemical , genetics : Nucleocapsid Proteins.
- chemical , isolation & purification : Nucleocapsid Proteins.
- chemical : Cations, Monovalent.
- chemistry : SARS Virus.
- genetics : SARS Virus.
- physiology : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Hot Temperature, Humans, Hydrogen-Ion Concentration, Protein Denaturation, Protein Folding, Thermodynamics, Virus Inactivation.
Abstract
The nucleocapsid protein (N protein) is one of the major virion structural proteins of a newly identified coronavirus, which has been confirmed as the causative agent of severe acute respiratory syndrome (SARS). The major function of N protein is to assemble the RNA of coronavirus. In the present study, the gene encoding the N protein was cloned and the protein was expressed, purified, and refolded as shown by 1H NMR measurement. The maximal Trp emission wavelength occurs near 331 nm, suggesting substantial burial of Trp residues. Circular dichroism measurements indicate that N protein contains little α-helical structure. Acid titration shows that N protein begins to unfold near pH 5 and is fully denatured near pH 2.7, and the acid unfolding process is reversible. The physical and chemical properties of N protein indicate that its stability is low. N protein is denatured reversibly at pH 7.4 either by urea (with Cm of 2.77 M and m value of 2.74 kcal mol-1 M-1) or GdmCl (with Cm of 1.46 M and m value of 4.50 kcal mol-1 M-1). In the heat-induced denaturation in phosphate-buffered saline buffer, N-protein starts to unfold at 35 °C and is completely denatured at 55 °C, where SARS virus was also reported to be inactivated. We propose that the low stability of N protein may be critical for the stability and function of SARS virus.
Url:
DOI: 10.1021/bi049194b
Affiliations:
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Respiratory Syndrome (virology)</term><term>Sodium Chloride (chemistry)</term><term>Thermodynamics</term><term>Urea (chemistry)</term><term>Virus Inactivation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cations monovalents</term><term>Chlorure de sodium ()</term><term>Concentration en ions d'hydrogène</term><term>Dénaturation des protéines</term><term>Guanidine ()</term><term>Humains</term><term>Inactivation virale</term><term>Pliage des protéines</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (biosynthèse)</term><term>Protéines nucléocapside (génétique)</term><term>Protéines nucléocapside (isolement et purification)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Température élevée</term><term>Thermodynamique</term><term>Urée ()</term><term>Virus du SRAS ()</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (physiologie)</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>Guanidine</term><term>Nucleocapsid Proteins</term><term>Sodium Chloride</term><term>Urea</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cations, Monovalent</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines nucléocapside</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></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hot Temperature</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Thermodynamics</term><term>Virus Inactivation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cations monovalents</term><term>Chlorure de sodium</term><term>Concentration en ions d'hydrogène</term><term>Dénaturation des protéines</term><term>Guanidine</term><term>Humains</term><term>Inactivation virale</term><term>Pliage des protéines</term><term>Protéines nucléocapside</term><term>Température élevée</term><term>Thermodynamique</term><term>Urée</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract">The nucleocapsid protein (N protein) is one of the major virion structural proteins of a newly identified coronavirus, which has been confirmed as the causative agent of severe acute respiratory syndrome (SARS). The major function of N protein is to assemble the RNA of coronavirus. In the present study, the gene encoding the N protein was cloned and the protein was expressed, purified, and refolded as shown by 1H NMR measurement. The maximal Trp emission wavelength occurs near 331 nm, suggesting substantial burial of Trp residues. Circular dichroism measurements indicate that N protein contains little α-helical structure. Acid titration shows that N protein begins to unfold near pH 5 and is fully denatured near pH 2.7, and the acid unfolding process is reversible. The physical and chemical properties of N protein indicate that its stability is low. N protein is denatured reversibly at pH 7.4 either by urea (with Cm of 2.77 M and m value of 2.74 kcal mol-1 M-1) or GdmCl (with Cm of 1.46 M and m value of 4.50 kcal mol-1 M-1). In the heat-induced denaturation in phosphate-buffered saline buffer, N-protein starts to unfold at 35 °C and is completely denatured at 55 °C, where SARS virus was also reported to be inactivated. We propose that the low stability of N protein may be critical for the stability and function of SARS virus.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Wang, Yulong" sort="Wang, Yulong" uniqKey="Wang Y" first="Yulong" last="Wang">Yulong Wang</name></noRegion><name sortKey="Fu, Yan" sort="Fu, Yan" uniqKey="Fu Y" first="Yan" last="Fu">Yan Fu</name><name sortKey="Li, Bing" sort="Li, Bing" uniqKey="Li B" first="Bing" last="Li">Bing Li</name><name sortKey="Luo, Yongzhang" sort="Luo, Yongzhang" uniqKey="Luo Y" first="Yongzhang" last="Luo">Yongzhang Luo</name><name sortKey="Luo, Yongzhang" sort="Luo, Yongzhang" uniqKey="Luo Y" first="Yongzhang" last="Luo">Yongzhang Luo</name><name sortKey="Wang, Yihua" sort="Wang, Yihua" uniqKey="Wang Y" first="Yihua" last="Wang">Yihua Wang</name><name sortKey="Wu, Xiaoyu" sort="Wu, Xiaoyu" uniqKey="Wu X" first="Xiaoyu" last="Wu">Xiaoyu Wu</name><name sortKey="Yuan, Guiyong" sort="Yuan, Guiyong" uniqKey="Yuan G" first="Guiyong" last="Yuan">Guiyong Yuan</name><name sortKey="Zhou, Hao" sort="Zhou, Hao" uniqKey="Zhou H" first="Hao" last="Zhou">Hao Zhou</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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