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

• Published in: Virology (New York, N.Y.) Vol. 432; no. 2; pp. 485 - 494
• Main Authors: Verdiá-Báguena, Carmina, Nieto-Torres, Jose L, Alcaraz, Antonio, DeDiego, Marta L, Torres, Jaume, Aguilella, Vicente M, Enjuanes, Luis
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25.10.2012
• Subjects: Amino Acid Sequence; Cations; Channel pores; Conductance; Coronavirus; Coronavirus 229E, Human - metabolism; Envelope protein; Envelopes; HCoV-229E; Humans; Infectious Disease; Ion channel; Ion channels; Ion Channels - metabolism; Lipid bilayers; Lipid composition; Lipid membranes; Membrane Lipids - metabolism; Molecular Sequence Data; Mutation; SARS; SARS coronavirus; SARS Virus - metabolism; Severe acute respiratory syndrome; Transmembrane domains; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - genetics; Viral Envelope Proteins - metabolism; Viroporin Proteins; Envelope protein; Lipid membranes; SARS; Coronavirus; HCoV-229E; Ion channel

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...