Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids
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Altres documents de l'autoria: Aguilella, Vicente; Alcaraz, Antonio; Verdiá Báguena, Carmen; Nieto Torres, José L.; De Diego, Marta L.; Torres, Jaume; Enjuanes, Luis
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Títol
Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipidsAutoria
Data de publicació
2012-10Editor
ElsevierTipus de document
info:eu-repo/semantics/articleVersió de l'editorial
http://www.sciencedirect.com/science/article/pii/S0042682212003352Versió
info:eu-repo/semantics/publishedVersionParaules clau / Matèries
Resum
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. [-]
Publicat a
Virology, Volume 432, Issue 2, October 2012Drets d'accés
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info:eu-repo/semantics/openAccess
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info:eu-repo/semantics/openAccess
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