Lysophosphatidylcholine reversibly arrests pore expansion during syncytium formation mediated by diverse viral fusogens

Using lysophosphatidylcholine, a curvature-inducing lysolipid, we have isolated a reversible, "stalled pore" phenotype during syncytium formation induced by the p14 fusion-associated small transmembrane (FAST) protein and influenza virus hemagglutinin (HA) fusogens. This is the first evidence that lateral propagation of stable fusion pores leading to syncytiogenesis mediated by diverse viral fusogens is inhibited by promotion of positive membrane curvature in the outer leaflets of the lipid bilayer surrounding intercellular fusion pores.