Specificity of the N1 and N2 sialidase subtypes of human influenza A virus for natural and synthetic gangliosides.
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.
Sato
K
K
Aichi Prefectural Institute of Public Health, Nagoya 462, Japan.
Hanagata
G
G
Kiso
M
M
Hasegawa
A
A
Suzuki
Y
Y
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
D005732:Gangliosides; D007527:Isoenzymes; D009439:Neuraminidase