The E protein is a multifunctional membrane protein of SARS-CoV.
- Author:
Qingfa WU
1
;
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 YANG
Author Information
1. Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Base Sequence;
Cluster Analysis;
Codon;
genetics;
Gene Components;
Genome, Viral;
Membrane Glycoproteins;
metabolism;
Membrane Proteins;
genetics;
metabolism;
Molecular Sequence Data;
Phylogeny;
Protein Conformation;
SARS Virus;
genetics;
Sequence Alignment;
Sequence Analysis, DNA;
Sequence Homology;
Spike Glycoprotein, Coronavirus;
Viral Envelope Proteins;
genetics;
metabolism
- From:
Genomics, Proteomics & Bioinformatics
2003;1(2):131-144
- CountryChina
- Language:English
-
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.
