Permeability properties of the membrane of vesicular stomatitis virions.
Observations of the light-scattering properties of several enveloped viruses indicate that virions (vesicular stomatitis, SV5 and influenza), in common with other membrane systems, are osmotically active, responding to NaCl gradients by swelling in hypo-osmolar solutions and shrinking in hyperosmolar solutions. The permeability barrier responsible for this osmotic response in vesicular stomatitis virions was modified both by protease treatment to remove the viral glycoprotein and by treatment with the polyene antibiotic filipin, an agent known to interact with cholesterol in liposomes and membranes. Filipin altered the kinetic and equilibrium permeability behavior of virions but the extent of leakage of osmotic shocking agent was less than that in lecithin/cholesterol and lecithin/ergosterol liposomes and in ergosterol-containing ciliary membranes. Negative-staining electron microscopy revealed that filipin treatment caused structural changes in the viral membrane. Intact virions exhibited appreciably larger responses to osmotic change than did protease-treated virus particles. Thus, the osmotic barrier in intact vesicular stomatitis virions may not be exclusively lipid in nature.
D007700:Kinetics; D008027:Light; D008433:Mathematics; D008566:Membranes / Q000378:metabolism* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009995:Osmosis; D010539:Permeability; D012542:Scattering, Radiation; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism* / Q000648:ultrastructure; D014764:Viral Proteins / Q000378:metabolism; D014867:Water / Q000378:metabolism
D014764:Viral Proteins; D014867:Water