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Glycobiology, Vol 8, 527-532, Copyright © 1998 by Society for Glycobiology

ORIGINAL ARTICLES

Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides

K Sato, G Hanagata, M Kiso, A Hasegawa and Y Suzuki
Aichi Prefectural Institute of Public Health, Nagoya 462, Japan.

Sialyl-linkage specificity of sialidases of the human influenza A virus strains, A/Aichi/2/68 (H3N2) and A/PR/8/34 (H1N1) were studied using natural and synthetic gangliosides. The sialidase of the A/Aichi/2/68 strain hydrolyzed the terminal Neu5Acalpha2-3Gal sequence but not the Neu5Acalpha2-3 linkage on the inner Gal of GM1a, which is a ganglioside that has the gangliotetraose chain (Galbeta1-3GalNAcbeta1-4- (Neu5Acalpha2-3)Galbeta1++ +-4Glcbeta1-Cer). The sialidase hydrolyzed the Neu5Ac on the inner Gal of GM2, which had a shorter gangliotriose chain. GM4, which had the shortest chain (Neu5Acalpha2-3Galbeta1-Cer) of the gangliosides, had a lower substrate specificity. The N1 and N2 sialidase subtypes of the human influenza A virus had no significant variation in their substrate specificity for the gangliosides. Analysis of 11 synthetic gangliosides, which contained various ceramide or sialic acid moieties, demonstrated that A/Aichi/2/68 (H3N2) sialidase recognized the ceramide and sialic acid moiety and the length and structure of the sialyl sugar chain.
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C.-T. Guo, X.-L. Sun, O. Kanie, K. F. Shortridge, T. Suzuki, D. Miyamoto, K. I.-P. J. Hidari, C.-H. Wong, and Y. Suzuki
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