Journal
VIRUS RESEARCH
Volume 201, Issue -, Pages 61-66Publisher
ELSEVIER
DOI: 10.1016/j.virusres.2015.02.023
Keywords
Middle East respiratory syndrome coronavirus (MERS); Envelope protein; Ion channel; Purification; Oligomeric state
Categories
Funding
- Singapore National Research Foundation under CRP [NRF-CRP4-2008-02, RG 51/13]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available