Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids

Virology. 2012 Oct 25;432(2):485-94. doi: 10.1016/j.virol.2012.07.005. Epub 2012 Jul 24.

Abstract

Coronavirus (CoV) envelope (E) protein ion channel activity was determined in channels formed in planar lipid bilayers by peptides representing either the transmembrane domain of severe acute respiratory syndrome CoV (SARS-CoV) E protein, or the full-length E protein. Both of them formed a voltage independent ion conductive pore with symmetric ion transport properties. Mutations N15A and V25F located in the transmembrane domain prevented the ion conductivity. E protein derived channels showed no cation preference in non-charged lipid membranes, whereas they behaved as pores with mild cation selectivity in negatively-charged lipid membranes. The ion conductance was also controlled by the lipid composition of the membrane. Lipid charge also regulated the selectivity of a HCoV-229E E protein derived peptide. These results suggested that the lipids are functionally involved in E protein ion channel activity, forming a protein-lipid pore, a novel concept for CoV E protein ion channel entity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Coronavirus 229E, Human / metabolism*
  • Humans
  • Ion Channels / metabolism*
  • Membrane Lipids / metabolism*
  • Molecular Sequence Data
  • SARS Virus / metabolism*
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism

Substances

  • E protein, SARS coronavirus
  • Ion Channels
  • Membrane Lipids
  • Viral Envelope Proteins