Cell-mediated cytotoxicity against targets bearing Sendai virus glycoproteins in the absence of viral infection.
The glycoproteins HN and F and the lipids were solubilized from Sendai virus envelopes by using the nonionic detergent beta-D-octylglucoside. When beta-D-octylglucoside was removed by dialysis, the glycoproteins and lipids reassociated to form vesicles. These vesicles displayed hemagglutinating, neuraminidase, and hemolysin activities comparable to those expressed by the intact virus. The vesicles were used as carriers to transfer the glycoproteins to the surface of P815 cells. The recipient cells were tested for the acquisition of the glycoproteins by demonstration of surface neuraminidase, hemadsorption activity, and antigens. The modified cells were used as targets for natural cell-mediated lysis and were found to be sensitive.
D000818:Animals; D000956:Antigens, Viral / Q000276:immunology*; D002460:Cell Line; D002642:Chick Embryo; D004589:Electrophoresis, Disc; D005455:Fluorescent Antibody Technique; D006023:Glycoproteins / Q000276:immunology*; D006461:Hemolysis; D006801:Humans; D007111:Immunity, Cellular; D007694:Killer Cells, Natural / Q000276:immunology; D008055:Lipids / Q000276:immunology; D051379:Mice; D008819:Mice, Nude; D010222:Parainfluenza Virus 1, Human / Q000276:immunology*; D010954:Plasmacytoma / Q000276:immunology; D014759:Viral Envelope Proteins / Q000276:immunology*
D000956:Antigens, Viral; D006023:Glycoproteins; D008055:Lipids; D014759:Viral Envelope Proteins