The E protein is a multifunctional membrane protein of SARS-CoV.
Identifieur interne : 002983 ( PubMed/Curation ); précédent : 002982; suivant : 002984The E protein is a multifunctional membrane protein of SARS-CoV.
Auteurs : Qingfa Wu [République populaire de Chine] ; Yilin Zhang ; Hong Lü ; Jing Wang ; Ximiao He ; Yong Liu ; Chen Ye ; Wei Lin ; Jianfei Hu ; Jia Ji ; Jing Xu ; Jie Ye ; Yongwu Hu ; Wenjun Chen ; Songgang Li ; Jun Wang ; Jian Wang ; Shengli Bi ; Huanming YangSource :
- Genomics, proteomics & bioinformatics [ 1672-0229 ] ; 2003.
Descripteurs français
- KwdFr :
- Alignement de séquences, Analyse de regroupements, Analyse de séquence d'ADN, Codon (génétique), Composants de gène, Conformation des protéines, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Génome viral, Phylogénie, Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines membranaires (génétique), Protéines membranaires (métabolisme), Similitude de séquences, Séquence d'acides aminés, Séquence nucléotidique, Virus du SRAS (génétique).
- MESH :
- génétique : Codon, Protéines de l'enveloppe virale, Protéines membranaires, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines membranaires.
- Alignement de séquences, Analyse de regroupements, Analyse de séquence d'ADN, Composants de gène, Conformation des protéines, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Génome viral, Phylogénie, Similitude de séquences, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Base Sequence, Cluster Analysis, Codon (genetics), Gene Components, Genome, Viral, Membrane Glycoproteins (metabolism), Membrane Proteins (genetics), Membrane Proteins (metabolism), Molecular Sequence Data, Phylogeny, Protein Conformation, SARS Virus (genetics), Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , genetics : Codon, Membrane Proteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Membrane Proteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- Amino Acid Sequence, Base Sequence, Cluster Analysis, Gene Components, Genome, Viral, Molecular Sequence Data, Phylogeny, Protein Conformation, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Spike Glycoprotein, Coronavirus.
Abstract
The E (envelope) protein is the smallest structural protein in all coronaviruses and is the only viral structural protein in which no variation has been detected. We conducted genome sequencing and phylogenetic analyses of SARS-CoV. Based on genome sequencing, we predicted the E protein is a transmembrane (TM) protein characterized by a TM region with strong hydrophobicity and alpha-helix conformation. We identified a segment (NH2-_L-Cys-A-Y-Cys-Cys-N_-COOH) in the carboxyl-terminal region of the E protein that appears to form three disulfide bonds with another segment of corresponding cysteines in the carboxyl-terminus of the S (spike) protein. These bonds point to a possible structural association between the E and S proteins. Our phylogenetic analyses of the E protein sequences in all published coronaviruses place SARS-CoV in an independent group in Coronaviridae and suggest a non-human animal origin.
DOI: 10.1016/s1672-0229(03)01017-9
PubMed: 15626343
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pubmed:15626343Le document en format XML
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<front><div type="abstract" xml:lang="en">The E (envelope) protein is the smallest structural protein in all coronaviruses and is the only viral structural protein in which no variation has been detected. We conducted genome sequencing and phylogenetic analyses of SARS-CoV. Based on genome sequencing, we predicted the E protein is a transmembrane (TM) protein characterized by a TM region with strong hydrophobicity and alpha-helix conformation. We identified a segment (NH2-_L-Cys-A-Y-Cys-Cys-N_-COOH) in the carboxyl-terminal region of the E protein that appears to form three disulfide bonds with another segment of corresponding cysteines in the carboxyl-terminus of the S (spike) protein. These bonds point to a possible structural association between the E and S proteins. Our phylogenetic analyses of the E protein sequences in all published coronaviruses place SARS-CoV in an independent group in Coronaviridae and suggest a non-human animal origin.</div>
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<Abstract><AbstractText>The E (envelope) protein is the smallest structural protein in all coronaviruses and is the only viral structural protein in which no variation has been detected. We conducted genome sequencing and phylogenetic analyses of SARS-CoV. Based on genome sequencing, we predicted the E protein is a transmembrane (TM) protein characterized by a TM region with strong hydrophobicity and alpha-helix conformation. We identified a segment (NH2-_L-Cys-A-Y-Cys-Cys-N_-COOH) in the carboxyl-terminal region of the E protein that appears to form three disulfide bonds with another segment of corresponding cysteines in the carboxyl-terminus of the S (spike) protein. These bonds point to a possible structural association between the E and S proteins. Our phylogenetic analyses of the E protein sequences in all published coronaviruses place SARS-CoV in an independent group in Coronaviridae and suggest a non-human animal origin.</AbstractText>
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