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, 77 (4), 1947-50

Sendai Virus Receptor: Proposed Recognition Structure Based on Binding to Plastic-Adsorbed Gangliosides

Sendai Virus Receptor: Proposed Recognition Structure Based on Binding to Plastic-Adsorbed Gangliosides

J Holmgren et al. Proc Natl Acad Sci U S A.

Abstract

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.

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References

    1. Adv Virus Res. 1972;17:1-50 - PubMed
    1. J Infect Dis. 1973 Jun;127(6):639-47 - PubMed
    1. Infect Immun. 1973 Aug;8(2):208-14 - PubMed
    1. J Mol Biol. 1974 Mar 15;83(4):427-36 - PubMed
    1. Proc Natl Acad Sci U S A. 1976 Mar;73(3):842-6 - PubMed

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