Expression and purification of N and E proteins from severe acute respiratory syndrome (SARS)-associated coronavirus: a comparative study.
Identifieur interne : 002601 ( PubMed/Corpus ); précédent : 002600; suivant : 002602Expression and purification of N and E proteins from severe acute respiratory syndrome (SARS)-associated coronavirus: a comparative study.
Auteurs : Chia-Wei Lai ; Yao-Chi Chung ; Yiu-Kay Lai ; Margaret Dah-Tsyr Chang ; Yu-Chen HuSource :
- Biotechnology letters [ 0141-5492 ] ; 2005.
English descriptors
- KwdEn :
- Animals, Baculoviridae (genetics), Blotting, Western, Cell Line, Cell Survival (genetics), Chromatography, Affinity (methods), Gene Expression, Microscopy, Confocal, Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Recombinant Fusion Proteins (isolation & purification), Recombinant Fusion Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Spodoptera, Time Factors, Transfection, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , genetics : Nucleocapsid Proteins, Viral Envelope Proteins.
- genetics : Baculoviridae, Cell Survival, SARS Virus.
- chemical , isolation & purification : Recombinant Fusion Proteins.
- chemical , metabolism : Nucleocapsid Proteins, Recombinant Fusion Proteins, SARS Virus, Viral Envelope Proteins.
- methods : Chromatography, Affinity.
- Animals, Blotting, Western, Cell Line, Gene Expression, Microscopy, Confocal, Spodoptera, Time Factors, Transfection.
Abstract
Histidine-tagged N (rNH) and E (rEH) proteins of Severe Acute Respiratory Syndrome (SARS)-coronovirus were expressed in the baculovirus/insect cell system and purified by immobilized metal affinity chromatography. rNH and rEH proteins differed markedly with respect to expression levels, cell death kinetics and subcellular localizations that led to different extraction and purification schemes. The features of both proteins are compared and the potential applications of purified rNH and rEH are discussed.
DOI: 10.1007/s10529-005-7176-6
PubMed: 16091881
Links to Exploration step
pubmed:16091881Le document en format XML
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<author><name sortKey="Lai, Chia Wei" sort="Lai, Chia Wei" uniqKey="Lai C" first="Chia-Wei" last="Lai">Chia-Wei Lai</name>
<affiliation><nlm:affiliation>Department of Chemical Engineering, National Tsing Hua University, 300 Hsinchu, Taiwan.</nlm:affiliation>
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<author><name sortKey="Chung, Yao Chi" sort="Chung, Yao Chi" uniqKey="Chung Y" first="Yao-Chi" last="Chung">Yao-Chi Chung</name>
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<author><name sortKey="Lai, Yiu Kay" sort="Lai, Yiu Kay" uniqKey="Lai Y" first="Yiu-Kay" last="Lai">Yiu-Kay Lai</name>
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<author><name sortKey="Chang, Margaret Dah Tsyr" sort="Chang, Margaret Dah Tsyr" uniqKey="Chang M" first="Margaret Dah-Tsyr" last="Chang">Margaret Dah-Tsyr Chang</name>
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<author><name sortKey="Hu, Yu Chen" sort="Hu, Yu Chen" uniqKey="Hu Y" first="Yu-Chen" last="Hu">Yu-Chen Hu</name>
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<affiliation><nlm:affiliation>Department of Chemical Engineering, National Tsing Hua University, 300 Hsinchu, Taiwan.</nlm:affiliation>
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<term>Cell Survival (genetics)</term>
<term>Chromatography, Affinity (methods)</term>
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<term>Nucleocapsid Proteins (genetics)</term>
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<term>Recombinant Fusion Proteins (metabolism)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
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<term>Time Factors</term>
<term>Transfection</term>
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<front><div type="abstract" xml:lang="en">Histidine-tagged N (rNH) and E (rEH) proteins of Severe Acute Respiratory Syndrome (SARS)-coronovirus were expressed in the baculovirus/insect cell system and purified by immobilized metal affinity chromatography. rNH and rEH proteins differed markedly with respect to expression levels, cell death kinetics and subcellular localizations that led to different extraction and purification schemes. The features of both proteins are compared and the potential applications of purified rNH and rEH are discussed.</div>
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<Abstract><AbstractText>Histidine-tagged N (rNH) and E (rEH) proteins of Severe Acute Respiratory Syndrome (SARS)-coronovirus were expressed in the baculovirus/insect cell system and purified by immobilized metal affinity chromatography. rNH and rEH proteins differed markedly with respect to expression levels, cell death kinetics and subcellular localizations that led to different extraction and purification schemes. The features of both proteins are compared and the potential applications of purified rNH and rEH are discussed.</AbstractText>
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