Abstract

M2 is a pH-dependent matrix protein from influenza virus widely known for its role in viral uncoating and the target of the amantadine flu drug that prevents proton transport. An additional role played by M2 relies on collective effects where clusters of M2-homotetramer proteins have been hypothesized to induce local membrane curvature effects (Rossman et al., Cell 142, pp. 902-913, 2010).We use molecular dynamics simulations with the MARTINI coarse grained parametrization to study a system comprised by two model membranes linked by an hour-glass shaped structure. We study the role played by M2 homotetramers in the scission step, leading to lipid-bilayer separation. The geometry of the model and the membrane-lipid interaction details are further used to adjust parameters on a Helfrich-like functional in order to propose a minimal model for viral scission at the mesoscopic scale.

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