Sialidase of swine influenza A viruses: variation of the recognition specificities for sialyl linkages and for the molecular species of sialic acid with the year of isolation

Glycoconj J. 1995 Apr;12(2):156-61. doi: 10.1007/BF00731360.


The sialidase of swine influenza A viruses of N1 and N2 subtypes, isolated from 1930 to 1992, was studied for substrate specificity with ganglio-series, lacto-series type II and GM3 gangliosides containing Neu5Ac alpha 2-3Gal, Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. All viral sialidases tested showed that the activity for hydrolysing substrates with Neu5Ac alpha 2-3Gal was higher than the activities with Neu5Gc alpha 2-3Gal and Neu5Ac alpha 2-6Gal linkages. When GM1b, GM3 and sialylparagloboside were used as substrates, the earliest strain (A/Wisconsin/15/30 H1N1, isolated in 1930) showed the activity ratio of Neu5Ac alpha 2-6Gal to Neu5Ac alpha 2-3Gal to be 0.13:0.2, and the ratio Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal to be 0.19:0.37, while those strains isolated from 1978 to 1992 exhibited ratios of 0.29:0.58 for Neu5Ac alpha 2-6Gal/Neu5Ac alpha 2-3Gal and 0.51:0.76 for Neu5Gc alpha 2-3Gal/Neu5Ac alpha 2-3Gal. The above results indicate that the substrate specificities of sialidases from swine influenza A viruses towards sialyl linkages and the molecular species of sialic acid are related to the year of isolation, i.e. strains isolated after 1978 exhibited higher activity towards Neu5Ac alpha 2-6Gal and Neu5Gc alpha 2-3Gal linkages when compared with strains isolated in an earlier year, 1930.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Gangliosides / chemistry
  • Gangliosides / metabolism
  • Influenza A virus / enzymology*
  • Kinetics
  • Molecular Sequence Data
  • N-Acetylneuraminic Acid
  • Neuraminidase / metabolism*
  • Sialic Acids / chemistry
  • Sialic Acids / metabolism*
  • Substrate Specificity


  • Gangliosides
  • Sialic Acids
  • Neuraminidase
  • N-Acetylneuraminic Acid