title: Sendai virus envelope glycoproteins become laterally mobile on the surface of human erythrocytes following fusion.
abstract: Fluorescence photobleaching recovery has been employed to study the lateral mobility of the Sendai virus envelope glycoproteins (HN, neuraminidase/hemagglutinin protein (HN) fusion protein (F) on the surface of human erythrocytes. Our results indicate that the two viral glycoproteins are laterally immobile on the cell surface prior to fusion, and become mobile during the fusion process. The two fused glycoproteins are mobilized to the same extent (diffusion coefficients of 3.1-3.3 X 10(-10) cm2/sec with mobile fractions of 0.53-0.57 for both HN and F). Their mobilization is blocked under conditions that allow virus adsorption and hemagglutination, but not virus-cell or cell-cell fusion. These findings suggest a possible role for the lateral diffusion of the viral glycoproteins in the mechanism of cell-cell fusion, enabling them to perturb the membranes of adjacent cells and lead to cell-cell fusion.
mesh_terms: D002459:Cell Fusion; D004229:Dithiothreitol / Q000494:pharmacology; D004912:Erythrocytes / Q000166:cytology / Q000382:microbiology*; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins; D015707:HN Protein; D006801:Humans; D008856:Microscopy, Fluorescence; D010222:Parainfluenza Virus 1, Human / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D013499:Surface Properties; D013861:Thiocyanates; D014357:Trypsin / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000378:metabolism*; D014760:Viral Fusion Proteins; D014764:Viral Proteins / Q000378:metabolism*; D014771:Virion / Q000378:metabolism
chemical_list: D005452:Fluoresceins; D015707:HN Protein; D013861:Thiocyanates; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; D014764:Viral Proteins; D010664:Phenylmethylsulfonyl Fluoride; D014357:Trypsin; D016650:Fluorescein-5-isothiocyanate; D004229:Dithiothreitol