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

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.

journal_name

Virology

journal_title

Virology

authors

Verdiá-Báguena C,Nieto-Torres JL,Alcaraz A,DeDiego ML,Torres J,Aguilella VM,Enjuanes L

doi

10.1016/j.virol.2012.07.005

subject

Has Abstract

pub_date

2012-10-25 00:00:00

pages

485-94

issue

2

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(12)00335-2

journal_volume

432

pub_type

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