The E protein is a multifunctional membrane protein of SARS-CoV |
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Authors: | Wu Qingfa Zhang Yilin Lü Hong Wang Jing He Ximiao Liu Yong Ye Chen Lin Wei Hu Jianfei Ji Jia Xu Jing Ye Jie Hu Yongwu Chen Wenjun Li Songgang Wang Jun Wang Jian Bi Shengli Yang Huanming |
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Affiliation: | Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China. |
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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. |
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Keywords: | SARS SARS-CoV the E protein envelope TM region |
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