Expression and Purification of N and E Proteins from Severe Acute Respiratory Syndrome (SARS)-Associated Coronavirus: a Comparative Study
Identifieur interne : 004C07 ( Main/Curation ); précédent : 004C06; suivant : 004C08Expression and Purification of N and E Proteins from Severe Acute Respiratory Syndrome (SARS)-Associated Coronavirus: a Comparative Study
Auteurs : Chia-Wei Lai [Taïwan] ; Yao-Chi Chung [Taïwan] ; Yiu-Kay Lai [Taïwan] ; Margaret Dah-Tsyr Chang [Taïwan] ; Yu-Chen Hu [Taïwan]Source :
- Biotechnology Letters [ 0141-5492 ] ; 2005-07-01.
Descripteurs français
- KwdFr :
- Animaux, Baculoviridae (génétique), Chromatographie d'affinité (), Expression des gènes, Facteurs temps, Lignée cellulaire, Microscopie confocale, Protéines de fusion recombinantes (isolement et purification), Protéines de fusion recombinantes (métabolisme), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Spodoptera, Survie cellulaire (génétique), Technique de Western, Transfection, Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Baculoviridae, Protéines de l'enveloppe virale, Protéines nucléocapside, Survie cellulaire, Virus du SRAS.
- isolement et purification : Protéines de fusion recombinantes.
- métabolisme : Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Protéines nucléocapside, Virus du SRAS.
- Animaux, Chromatographie d'affinité, Expression des gènes, Facteurs temps, Lignée cellulaire, Microscopie confocale, Spodoptera, Technique de Western, Transfection.
- Pascal (Inist)
English descriptors
- KwdEn :
- Animals, Baculoviridae, Baculoviridae (genetics), Blotting, Western, Cell Line, Cell Survival (genetics), Chromatography, Affinity (methods), Comparative study, Coronavirus, Gene Expression, Immobilized metal affinity chromatography, Microscopy, Confocal, Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein, Purification, Recombinant Fusion Proteins (isolation & purification), Recombinant Fusion Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome virus, Severe acute respiratory syndrome virus, Spodoptera, Syndrome, Time Factors, Transfection, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), baculovirus, coronavirus, immobilized metal affinity chromatography.
- 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
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.
Url:
DOI: 10.1007/s10529-005-7176-6
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<front><div type="abstract" xml:lang="en">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.</div>
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<front><div type="abstract" xml:lang="en">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.</div>
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