Sendai virus receptor: proposed recognition structure based on binding to plastic-adsorbed gangliosides.
The binding of Sendai virus to polystyrene petri dishes to which various gangliosides of defined structures had been adsorbed was determined. The ganglioside-bound virus was visualized either by a water vapor condensation method or by a hemadsorption method. By either assay, specific virus binding of high affinity was demonstrated to the gangliosides GT1a, GQ1b, and GPlc which have a common end sequence in the oligosaccharide moiety: NeuAc alpha 2 leads to 8NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc leads to. Binding also occurred to the GD1a and GT1b gangliosides, which have the same end carbohydrate sequence except for the terminal N-acetylneuraminic acid, but the affinity was only 1-9% of that of the gangliosides with a terminal disialosyl linkage. It is proposed that the structure NeuAc alpha 2 leads to 8NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc is the recognition-specific structure of the receptor for Sendai virus that is present on cell membrane gangliosides and possibly also glycoproteins. Binding tests to plastic-adsorbed glycolipids are suggested to be a useful tool for identification of the receptor recognition structure.
D000327:Adsorption; D001665:Binding Sites; D005732:Gangliosides / Q000378:metabolism*; D008954:Models, Biological; D010222:Parainfluenza Virus 1, Human; D010969:Plastics; D011991:Receptors, Virus / Q000378:metabolism*; D013329:Structure-Activity Relationship
D005732:Gangliosides; D010969:Plastics; D011991:Receptors, Virus