J. Biochem, 1993, Vol. 113, No. 3 304-307
© 1993 Japanese Biochemical Society
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Drift of the Sialyl-Linkage Specific Recognition of the Sialidase of Influenza B Virus Isolates1
*Department of Biochemistry, University of Shizuoka School of Pharmaceutical Science Shizuoka, Shizuoka 422
**Technical Research Institute, Snow Brand Milk Products Co., Ltd. Kawagoe, Saitama 350
***Department of Applied Bio-organic Chemistry, Gifu University Gifu, Gifu 501-11
Sialyl-linkage specificity of the sialidase 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 with. W-acetylneuraminyl (a2-3)- and (a2-6)-lactoses, GM3 gangliosides containing the same sialyl-oligosaccharide sequences as sialyllactose, and also with type I and type II lacto-series gangliosides carrying Neu5Acc2-3Gal and Neu5Aca2-6Gal linkages as substrates. From an examination of up to nine strains, the sialidases of all viruses preferentially hydrolyze substrates with Neu5Ac ar2-3Gal linkage rather than the Neu5A
23Gal linkage. It was found that the sialidase activity toward Neu5Aca2-6Gal linkage relative to Neu5Aca2-3Gal linkage is increased in later strains, whether sialyllactose or ganglioside is used as the substrate. These results suggested that the sialidase of influenza B virus isolates has shown a drift in linkage specificity which correlates with the year of isolation.
1This work was supported in part by a Grant in-Aid for Scientific Research in Priority Areas (01308028) (to Y.S. and A.H.) from the Ministry of Education, Science and Culture of Japan and Monbusho International Scientific Research Program: Joint Research (03044121) (toY.S.).
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