MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels

作者：Surya Wahyu; Li Yan; Verdia Baguena Carmina; Aguilella Vicente M; Torres Jaume^*

来源：Virus Research, 2015, 201: 61-66.

DOI：10.1016/j.virusres.2015.02.023

• Middle East respiratory syndrome coronavirus (MERS)
• Envelope protein
• Ion channel
• Purification
• Oligomeric state

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.

• 出版日期2015-4-2
• 单位南阳理工学院