title: The role of the target membrane structure in fusion with Sendai virus.
abstract: Fusion between membranes of Sendai virus and liposomes or human erythrocytes ghosts was studied using an assay for lipid mixing based on the relief of self-quenching of octadecylrhodamine (R18) fluorescence. We considered only viral fusion that reflects the biological activity of the viral spike glycoproteins. The liposomes were made of phosphatidylcholine, and the effects of including cholesterol, the sialoglycolipid GD1a, and/or the sialoglycoprotein glycophorin as receptors were tested. Binding of Sendai virus to those liposomes at 37 degrees C was very weak. Fusion with the erythrocyte membranes occurred at a 30-fold faster rate than with the liposomes. Experiments with biological and liposomal targets of different size indicated that size did not account for differences in fusion efficiency.
authors.affiliation: Section on Membrane Structure and Function, National Cancer Institute, Bethesda, MD 20892.
authors.forename: D P
authors.initials: DP
authors.lastname: Sarkar
authors.forename: R
authors.initials: R
authors.lastname: Blumenthal
mesh_terms: D004910:Erythrocyte Membrane / Q000502:physiology; D005732:Gangliosides; D006021:Glycophorins / Q000502:physiology; D006801:Humans; D008081:Liposomes; D008561:Membrane Fusion / Q000502:physiology*; D010222:Parainfluenza Virus 1, Human / Q000502:physiology*; D014760:Viral Fusion Proteins / Q000502:physiology
chemical_list: D005732:Gangliosides; D006021:Glycophorins; D008081:Liposomes; D014760:Viral Fusion Proteins; C021298:ganglioside, GD1a