期刊
VIRUS RESEARCH
卷 201, 期 -, 页码 61-66出版社
ELSEVIER
DOI: 10.1016/j.virusres.2015.02.023
关键词
Middle East respiratory syndrome coronavirus (MERS); Envelope protein; Ion channel; Purification; Oligomeric state
类别
资金
- Singapore National Research Foundation under CRP [NRF-CRP4-2008-02, RG 51/13]
The Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified pathogen able of human transmission that causes a mortality of almost 40%. As in the case of SARS-CoV, MERS virus lacking E protein represents a potential vaccine. In both cases, abolishment of channel activity may be a contributor to the attenuation observed in E-deleted viruses. Herein, we report that purified MERS-CoV E protein, like SARS-CoV E protein, is almost fully alpha-helical, has a single alpha-helical transmembrane domain, and forms pentameric ion channels in lipid bilayers. Based on these similarities, and the proposed involvement of channel activity as virulence factor in SARS-CoV E protein, MERS-CoV E protein may constitute a potential drug target. (C) 2015 Elsevier B.V. All rights reserved.
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