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

Virus Res. 2015 Apr 2;201:61-6. doi: 10.1016/j.virusres.2015.02.023. Epub 2015 Feb 27.

Abstract

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.

Keywords: Envelope protein; Ion channel; Middle East respiratory syndrome coronavirus (MERS); Oligomeric state; Purification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Ion Channels / chemistry*
  • Ion Channels / metabolism*
  • Middle East Respiratory Syndrome Coronavirus / chemistry*
  • Middle East Respiratory Syndrome Coronavirus / physiology*
  • Protein Conformation
  • Protein Multimerization*
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / metabolism*

Substances

  • Ion Channels
  • Viral Envelope Proteins