MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels.
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 α-helical, has a single α-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.
School of Biological Sciences, Nanyang Technological University, Singapore.
Wahyu
W
Surya
School of Biological Sciences, Nanyang Technological University, Singapore.
Yan
Y
Li
Department of Physics, Laboratory of Molecular Biophysics, Universitat Jaume I, 12071 Castellón, Spain.
Carmina
C
Verdià-Bàguena
Department of Physics, Laboratory of Molecular Biophysics, Universitat Jaume I, 12071 Castellón, Spain.
Vicente M
VM
Aguilella
School of Biological Sciences, Nanyang Technological University, Singapore. Electronic address: jtorres@ntu.edu.sg.
Jaume
J
Torres
D006801:Humans; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism*; D065207:Middle East Respiratory Syndrome Coronavirus / Q000737:chemistry* / Q000502:physiology*; D011487:Protein Conformation; D055503:Protein Multimerization; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism*
D007473:Ion Channels; D014759:Viral Envelope Proteins
Envelope protein; Ion channel; Middle East respiratory syndrome coronavirus (MERS); Oligomeric state; Purification