Conductance and amantadine binding of a pore formed by a lysine‐flanked transmembrane domain of SARS coronavirus envelope protein

• DOI: 10.1110/ps.062730007
• Publication Date: 2007-08-31T21:28:11Z
• Authors: Jaume Torres; Uma Maheswari; Krupakar Parthasa...; Lifang Ng; Ding Xiang Liu; Xiandi Gong
• Keywords: Coronavirus; Helix (gastropod); Helix bundle

The coronavirus responsible for the severe acute respiratory syndrome (SARS-CoV) contains a small envelope protein, E, with putative involvement in host cell apoptosis and virus morphogenesis. It has been suggested that E protein can form membrane destabilizing transmembrane (TM) hairpin, or homooligomerize to regular TM alpha-helical bundle. We have shown previously topology of domain (ETM), flanked by two lysine residues at C N termini improve solubility, is consistent alpha-helix, orientational parameters lipid bilayers are homopentameric model. Herein, we show this peptide, reconstituted bilayers, shows sodium conductance. Channel activity inhibited anti-influenza drug amantadine, which was found bind our preparation moderate affinity. Results obtained from single double mutants indicate organization pore reported pentameric bundle