title: Lysophosphatidylcholine reversibly arrests pore expansion during syncytium formation mediated by diverse viral fusogens.
abstract: 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.
authors.affiliation: Department of Microbiology & Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.
authors.forename: Marta
authors.initials: M
authors.lastname: Ciechonska
authors.forename: Roy
authors.initials: R
authors.lastname: Duncan
mesh_terms: D000818:Animals; D002522:Chlorocebus aethiops; D015726:Giant Cells / Q000502:physiology* / Q000821:virology*; D006389:Hemagglutinins, Viral / Q000378:metabolism*; D008244:Lysophosphatidylcholines / Q000378:metabolism*; D008561:Membrane Fusion / Q000502:physiology*; D008856:Microscopy, Fluorescence; D008954:Models, Biological; D014709:Vero Cells; D014760:Viral Fusion Proteins / Q000378:metabolism*
chemical_list: D006389:Hemagglutinins, Viral; D008244:Lysophosphatidylcholines; D014760:Viral Fusion Proteins; C458881:hemagglutinin fusogenic peptide, influenza virus