Abstract
The influenza A M2 protein is a homotetrameric membrane protein that is vital to the viral life cycle. M2 has been shown to interact with cholesterol to induce cell membrane curvature and scission in the production of new virus particles. Previous work from our group used site-directed spin labeling electron paramagnetic resonance spectroscopy (SDSL-EPR) to probe the conformation and dynamics of M2 constructs consisting of the transmembrane and C-terminal domains, revealing multiple conformational states in a cholesterol-modulated equilibrium. The observed conformational changes were proposed to arise from both a direct M2-cholesterol interaction through an amino acid consensus region in the C-terminal domain and indirectly through cholesterol-induced changes to the bilayer environment.We present work using lipid bicelles, which spontaneously orient in a magnetic field, as a membrane alternative to detergent micelles and bilayered vesicles. Nuclear magnetic resonance (NMR) and EPR were used to obtain new information describing the specific M2-cholesterol interaction.
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