Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids
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Otros documentos de la autoría: Aguilella, Vicente; Alcaraz, Antonio; Verdiá Báguena, Carmen; Nieto Torres, José L.; De Diego, Marta L.; Torres, Jaume; Enjuanes, Luis
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Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
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Título
Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipidsAutoría
Fecha de publicación
2012-10Editor
ElsevierTipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://www.sciencedirect.com/science/article/pii/S0042682212003352Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
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 ... [+]
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. [-]
Publicado en
Virology, Volume 432, Issue 2, October 2012Derechos de acceso
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