title: Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.
abstract: 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.
authors.affiliation: Aichi Prefectural Institute of Public Health, Nagoya 462, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Sato
authors.forename: G
authors.initials: G
authors.lastname: Hanagata
authors.forename: M
authors.initials: M
authors.lastname: Kiso
authors.forename: A
authors.initials: A
authors.lastname: Hasegawa
authors.forename: Y
authors.initials: Y
authors.lastname: Suzuki
mesh_terms: D002240:Carbohydrate Sequence; D005732:Gangliosides / Q000138:chemical synthesis / Q000378:metabolism*; D006801:Humans; D009980:Influenza A virus / Q000737:chemistry / Q000201:enzymology*; D007527:Isoenzymes / Q000378:metabolism*; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D005732:Gangliosides; D007527:Isoenzymes; D009439:Neuraminidase