Specificity of sialyl-sugar chain mediated recognition by the hemagglutinin of human influenza B virus isolates.

Recognition specificity for sialylsugar chains by the hemagglutinin of influenza B viruses isolated in different years from 1940 through 1990 (B/Lee/40, B/Setagaya/3/56, B/Tokyo/7/66, B/Kagoshima/1/68, B/Gifu/2/73, B/Kanagawa/3/76, B/Ibaraki/2/85, B/Yamagata/16/88, and B/Bangkok/163/90) was studied using 13 gangliosides. Reactivity of the viruses' hemagglutinin binding to gangliosides was determined by using thin-layer chromatography/virus-binding assay, and also by measuring virus binding to erythrocytes modified by incubation with gangliosides in terms of the absorbance of hemoglobin released from the infected cells. Eight strains preferentially recognized a novel ganglioside, carrying lacto-series type I and II sugar chains with the Neu5Ac alpha 2-6Gal linkage. It was found that B/Gifu/2/73 strain binds to lacto-series gangliosides containing Neu5Ac alpha 2-6Gal and Neu5Ac alpha 2-3Gal linkages. Other gangliosides studied, including GM4, GM3(alpha 2-3), GM3(alpha 2-6), GM2, GM1a, GD3, GD1a, GD1b, and GT1b, were poor receptors.