Sendai virus-mediated lysis of liposomes requires cholesterol.
Vesicles were constituted with glycophorin, the Sendai virus receptor of human erythrocytes, and loaded with calcein, a polar derivative of fluorescein, at self-quenching concentrations. On exposure to Sendai virus and mild hypo-osmotic stress, vesicles of the appropriate composition released a significant portion of their internal contents, as indicated by an increase in calcein fluorescence. Susceptible liposomes were not induced to leak by heat-inactivated virus or by trypsin-treated virus. The response of the vesicles to virus attachment is thus analogous to virus-induced hemolysis and presumably involves fusion of the vesicle and virus membranes. In addition to glycophorin and phosphatidylcholine, cholesterol was absolutely required for the lytic response to the virus. The need for cholesterol was not attributable to inactivation of the virus by liposomes without cholesterol. The presence of gangliosides increased the encapsulated volume of the liposomes, but gangliosides did not effectively substitute for glycophorin. Thin-layer chromatography of lipid extracted from incubated virus and liposomes containing a small amount of a fluorescent phosphatidylcholine indicated that phosphatidylcholine in the vesicle is not chemically altered by functional interaction with the virus.
D002449:Cell Aggregation; D002784:Cholesterol / Q000502:physiology*; D006021:Glycophorins / Q000502:physiology; D008081:Liposomes; D008561:Membrane Fusion; D008563:Membrane Lipids / Q000502:physiology; D010222:Parainfluenza Virus 1, Human / Q000502:physiology*; D010743:Phospholipids / Q000502:physiology; D011991:Receptors, Virus / Q000502:physiology; D014764:Viral Proteins / Q000502:physiology
D006021:Glycophorins; D008081:Liposomes; D008563:Membrane Lipids; D010743:Phospholipids; D011991:Receptors, Virus; D014764:Viral Proteins; D002784:Cholesterol