Membrane vesicles containing the Sendai virus binding glycoprotein, but not the viral fusion protein, fuse with phosphatidylserine liposomes at low pH.

Membrane vesicles containing the Sendai virus hemagglutinin/neuraminidase (HN) glycoprotein were able to induce carboxyfluorescein (CF) release from loaded phosphatidylserine (PS) but not loaded phosphatidylcholine (PC) liposomes. Similarly, fluorescence dequenching was observed only when HN vesicles, bearing self-quenched N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylethanolamine (N-NBD-PE), were incubated with PS but not PC liposomes. Thus, fusion between Sendai virus HN glycoprotein vesicles and the negatively charged PS liposomes is suggested.

Fusion of Sendai virus with negatively charged liposomes as studied by pyrene-labelled phospholipid liposomes.

Sendai virus particles fuse with negatively charged liposomes but not with vesicles made of zwitterionic phospholipids. The liposome-virus fusion process was studied by dilution of the concentration-dependent excimer-forming fluorophore 2-pyrenyldodecanoylphosphatidylcholine contained in the liposomes by the viral lipids. The data were analyzed in the framework of a mass action kinetic model.

The interaction of Sendai virus with negatively charged liposomes: virus-induced lysis of carboxyfluorescein-loaded small unilamellar vesicles.

The interaction of Sendai virus with small, unilamellar vesicles, lacking virus receptors and loaded with self-quenched 6-carboxyfluorescein, was studied. Sendai virions induced release of carboxyfluorescein from vesicles composed of negative charged phospholipids, despite the fact that they did not contain virus receptors. Preliminary experiments indicate that the carboxyfluorescein release is accompanied by mixing of the virus and liposome lipids and their entrapped contents, suggesting liposome-virus fusion.

Dependence of the conformation of the polar head groups of phosphatidylcholine on its packing in bilayers. Nuclear magnetic resonance studies on the effect of the binding of lanthanide ions.

Proton magnetic resonance spectra of vesicles of various sizes composed of egg phosphatidylcholine (PC) with varying concentrations of cholesterol differed in the apparent line width of the signal of the methylene protons of PC (delta v1/2). They also varied in the extent of lanthanide-induced shifts of the 31P and 1H NMR signals of the corresponding nuclei of the polar head groups located on the outer surface of the vesicles (delta delta). The differences in the lanthanide-induced shifts of the 31P signals are fully accounted for by the ratio between the externally added lanthanide and the number of PC head groups available for interaction with the lanthanide ions.