Evidence for different receptor sites in mouse spleen cells for the Sendai virus hemagglutinin-neuraminidase (HN) and fusion (F) glycoproteins.
Liposomes were reconstituted from phosphatidylcholine and Sendai virus glycoproteins HN or F and their interaction with mouse spleen cells was studied. Both the HN and F liposomes were able to stimulate chemiluminescence (CL), indicating that the glycoproteins were able to interact with the cell membrane independently of each other. The induction of CL in cells which had been pretreated with liposomes by monoclonal antibodies to either HN or F demonstrated that HN and F bind to the cells independently. The presence of F liposomes on the cell surface was also confirmed by immunoelectron microscopy. Cells pretreated with HN and F liposomes revealed a different pattern of CL when challenged with intact virus or the calcium ionophore A23187 indicating that HN and F bind to different receptor sites.
D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism*; D015707:HN Protein; D008081:Liposomes; D008163:Luminescent Measurements; D010222:Parainfluenza Virus 1, Human / Q000032:analysis*; D011991:Receptors, Virus / Q000378:metabolism; D013154:Spleen / Q000166:cytology* / Q000378:metabolism; D014760:Viral Fusion Proteins; D014764:Viral Proteins / Q000378:metabolism*
D015707:HN Protein; C039111:HN protein receptor; D008081:Liposomes; D011991:Receptors, Virus; D014760:Viral Fusion Proteins; D014764:Viral Proteins; C039110:virus fusion protein receptor, Sendai virus