Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/97217
Title: Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids
Authors: Nieto-Torres, Jose L.
DeDiego, Marta L.
Aguilella, Vicente M.
Verdiá-Báguena, Carmina
Alcaraz, Antonio
Torres, Jaume
Enjuanes, Luis
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2012
Source: Verdiá-Báguena, C., Nieto-Torres, J. L., Alcaraz, A., DeDiego, M. L., Torres, J., Aguilella, V. M., et al. (2012). Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids. Virology, 432(2), 485-494.
Series/Report no.: Virology
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.
URI: https://hdl.handle.net/10356/97217
http://hdl.handle.net/10220/11767
ISSN: 0042-6822
DOI: 10.1016/j.virol.2012.07.005
Rights: © 2012 Elsevier Inc.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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