title: Interaction of Sendai virions with resealed human erythrocyte ghosts. Lateral mobility of the viral glycoproteins in the cell membrane following fusion.
abstract: Two independent methods demonstrated that resealed human erythrocyte ghosts undergo Sendai virus-mediated cell-cell fusion to a much lower degree (about 4%) than intact erythrocytes, in spite of similar levels of viral envelope-cell fusion in the two preparations. Fluorescence photobleaching recovery (FPR) showed similar lateral mobilities of the viral glycoproteins following fusion with either ghosts or whole erythrocytes. It is suggested that although viral glycoprotein mobilization in the cell membrane is essential for cell-cell fusion, the target cell properties are also important; in the absence of the required cellular parameters, the mobilization may not be a sufficient condition.
authors.affiliation: Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
authors.forename: Y I
authors.initials: YI
authors.lastname: Henis
authors.forename: O
authors.initials: O
authors.lastname: Gutman
mesh_terms: D002459:Cell Fusion; D004910:Erythrocyte Membrane / Q000382:microbiology / Q000502:physiology*; D004912:Erythrocytes / Q000382:microbiology; D005456:Fluorescent Dyes; D006801:Humans; D008856:Microscopy, Fluorescence; D010222:Parainfluenza Virus 1, Human / Q000502:physiology*; D010714:Phosphatidylethanolamines; D014760:Viral Fusion Proteins / Q000502:physiology*; D014771:Virion / Q000502:physiology*
chemical_list: D005456:Fluorescent Dyes; D010714:Phosphatidylethanolamines; D014760:Viral Fusion Proteins; C042077:N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)phosphatidylethanolamine