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J. Biochem, 1994, Vol. 115, No. 2 202-207
© 1994 Japanese Biochemical Society

research-article

Specificity of Sialyl-Sugar Chain Mediated Recognition by the Hemagglutinin of Human Influenza B Virus Isolates1

Guiyun Xu*, Takashi Suzuki*, Harunobu Tahara*, Makoto Kiso**, Akira Hasegawa** and Yasuo Suzuki*,2

*Department of Biochemistry, University of Shizuoka School of Pharmaceutical Science Shizuoka, Shizuoka 422
**Department of Applied Bio-organic Chemistry, Gifu University Gifu, Gifu 501-11

2To whom correspondence should be addressed.

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(a2–3), GM3({alpha}2–6), GM2, GM1a, GD3, GD1a, GD1b, and GT1b, were poor receptors.

1This work was supported in part by Grants-in-Aid for Scientific Research in Priority Areas (01308028, 05274101) (to Y S. and A H) from the Ministry of Education, Science and Culture of Japan and a Monbusho International Scientific Research Program Joint Research grant (03044121) (to Y.S.).


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