Author: Hu, Yongwu; Wen, Jie; Tang, Lin; Zhang, Haijun; Zhang, Xiaowei; Li, Yan; Wang, Jing; Han, Yujun; Li, Guoqing; Shi, Jianping; Tian, Xiangjun; Jiang, Feng; Zhao, Xiaoqian; Wang, Jun; Liu, Siqi; Zeng, Changqing; Wang, Jian; Yang, Huanming
Title: The M Protein of SARS-CoV: Basic Structural and Immunological Properties Document date: 2016_11_28
ID: xzlcyn3l_27
Snippet: Glycoproteins on the viral surface are known to be generally involved in antigenicity demonstrated by the viral pathogens and immunoreponse by the host. The M protein might be related to the viral infectivity through binding to the viral S protein, and then subsequently binding to the host cellular receptor(s) and helping with the membrane fusion 1., 3., 11.. The N-terminal exterior region of the M protein is postulated to be responsible for its .....
Document: Glycoproteins on the viral surface are known to be generally involved in antigenicity demonstrated by the viral pathogens and immunoreponse by the host. The M protein might be related to the viral infectivity through binding to the viral S protein, and then subsequently binding to the host cellular receptor(s) and helping with the membrane fusion 1., 3., 11.. The N-terminal exterior region of the M protein is postulated to be responsible for its important roles in the pathogen-host interaction and membrane fusion with the host cell. The predicted presence of a single putative N-glycosylation site at the N-terminus (Codon 4) is highly conserved in other coronaviruses at similar positions and surroundings. The glycosylation site is classified as Type N-glycosylation (linked with Asn). As with other coronaviruses in Group I and II, no O-linked oligosaccharide site has been identified (12).
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