The role of the envelope protein in the stability of a coronavirus model membrane against an ethanolic disinfectant

Ethanol is highly effective against various enveloped viruses and can disable the virus by disintegrating the protective envelope surrounding it. The interactions between the coronavirus envelope (E) protein and its membrane environment play key roles in the stability and function of the viral envelope. By using molecular dynamics simulation, we explore the underlying mechanism of ethanol-induced disruption of a model coronavirus membrane and, in detail, interactions of the E-protein and lipids. We model the membrane bilayer as N-palmitoyl-sphingomyelin and 1-palmitoyl-2-oleoylphosphatidylcholine lipids and the coronavirus E-protein. The study reveals that ethanol causes an increase in the lateral area of the bilayer along with thinning of the bilayer membrane and orientational disordering of lipid tails. Ethanol resides at the head-tail region of the membrane and enhances bilayer permeability. We found an envelope-protein-mediated increase in the ordering of lipid tails. Our simulations also provide important insights into the orientation of the envelope protein in a model membrane environment. At similar to 25 mol.% of ethanol in the surrounding ethanol-water phase, we observe disintegration of the lipid bilayer and dislocation of the E-protein from the membrane environment. Published under an exclusive license by AIP Publishing.

Automated summary

Ethanol is highly effective against enveloped viruses by disintegrating the protective envelope, with interactions between coronavirus envelope protein and membrane environment playing key roles. Ethanol disrupts model coronavirus membrane by increasing lateral area, thinning the membrane, and disordering lipid tails, enhancing bilayer permeability. The study reveals ordering of lipid tails facilitated by envelope protein and disintegration of lipid bilayer at around 25 mol.% ethanol.