Low stability of nucleocapsid protein in SARS virus.
Identifieur interne : 000A14 ( Ncbi/Merge ); précédent : 000A13; suivant : 000A15Low stability of nucleocapsid protein in SARS virus.
Auteurs : Yulong Wang [République populaire de Chine] ; Xiaoyu Wu ; Yihua Wang ; Bing Li ; Hao Zhou ; Guiyong Yuan ; Yan Fu ; Yongzhang LuoSource :
- 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 (1)H 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 alpha-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 C(m) of 2.77 M and m value of 2.74 kcal mol(-1) M(-1)) or GdmCl (with C(m) 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 degrees C and is completely denatured at 55 degrees 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.
DOI: 10.1021/bi049194b
PubMed: 15323569
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élevée</term><term>Thermodynamique</term><term>Urée</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 (1)H 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 alpha-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 C(m) of 2.77 M and m value of 2.74 kcal mol(-1) M(-1)) or GdmCl (with C(m) 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 degrees C and is completely denatured at 55 degrees 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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15323569</PMID><DateCompleted><Year>2004</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>43</Volume><Issue>34</Issue><PubDate><Year>2004</Year><Month>Aug</Month><Day>31</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Low stability of nucleocapsid protein in SARS virus.</ArticleTitle><Pagination><MedlinePgn>11103-8</MedlinePgn></Pagination><Abstract><AbstractText>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 (1)H 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 alpha-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 C(m) of 2.77 M and m value of 2.74 kcal mol(-1) M(-1)) or GdmCl (with C(m) 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 degrees C and is completely denatured at 55 degrees 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yulong</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences and Biotechnology, MOE Laboratory of Protein Science, Tsinghua University, Beijing 100084, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Xiaoyu</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yihua</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Bing</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Hao</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Yuan</LastName><ForeName>Guiyong</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Fu</LastName><ForeName>Yan</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Yongzhang</ForeName><Initials>Y</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002414">Cations, Monovalent</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>451W47IQ8X</RegistryNumber><NameOfSubstance UI="D012965">Sodium 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MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><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="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory 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PubStatus="entrez"><Year>2004</Year><Month>8</Month><Day>25</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15323569</ArticleId><ArticleId IdType="doi">10.1021/bi049194b</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><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="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></noCountry><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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