Reconstitution of the fusogenic activity of vesicular stomatitis virus.
Enveloped virus glycoproteins exhibit membrane fusion activity. We have analysed whether the G protein of vesicular stomatitis virus, reconstituted into liposomes, is able to fuse nucleated cells in a pH-dependent fashion. Proteoliposomes produced by octylglucoside dialysis did not exhibit cell fusion activity of the G protein. However, by making use of n-dodecyl octaethylene monoether (C12E8) as the solubilizing agent and by removal of the detergent in two steps, we were able to produce fusogenic G protein liposomes. These G protein liposomes fuse to the BHK-21 cell surface at pH 5.7-6.0 with an efficiency of fusion comparable with that of the parent virus. Physical and chemical analysis revealed that the fusogenic liposomes exhibited a protein to lipid weight ratio of 0.67 and showed an average diameter of 130 nm.
D000818:Animals; D002459:Cell Fusion; D002460:Cell Line; D002462:Cell Membrane / Q000648:ultrastructure; D003902:Detergents; D006863:Hydrogen-Ion Concentration; D008562:Membrane Glycoproteins; D014721:Vesicular stomatitis Indiana virus / Q000502:physiology*; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000502:physiology*
D003902:Detergents; C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins