Different binding capacities of influenza A and Sendai viruses to gangliosides from human granulocytes

Glycoconj J. 1993 Feb;10(1):120-6. doi: 10.1007/BF00731196.


The structures of gangliosides from human granulocytes were elucidated by fast atom bombardment mass spectrometry and by gas chromatography/mass spectrometry as their partially methylated alditol acetates. In human granulocytes besides GM3 (II3Neu5Ac-LacCer), neolacto-series gangliosides (IV3Neu5Ac-nLcOse4Cer, IV6Neu5Ac-nLcOse4Cer and VI3Neu5Ac-nLcOse6Cer) containing C24:1, and to some extent C22:0; and C16:0 fatty acid in their respective ceramide portions, were identified as major components. In this study we demonstrate that gangliosides from human granulocytes, the second most abundant cells in peripheral blood, can serve as receptors for influenza viruses A/PR/8/34 (H1N1), A/X-31 (H3N2), and a parainfluenza virus Sendai virus (HNF1, Z-strain). Viruses were found to exhibit specific adhesion to terminal Neu5Ac alpha 2-3Gal and/or Neu5Ac alpha 2-6Gal sequences as well as depending on the chain length of ganglioside carbohydrate backbones from human granulocytes, these important effector cells which represent the first line of defence in immunologically mediated reactions.

Publication types

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

MeSH terms

  • Carbohydrate Sequence
  • Chromatography, Gas / methods
  • Chromatography, Thin Layer
  • Gangliosides / blood*
  • Granulocytes / metabolism*
  • Humans
  • Influenza A virus / metabolism*
  • Molecular Sequence Data
  • Parainfluenza Virus 1, Human / metabolism*
  • Receptors, Virus / metabolism*
  • Spectrometry, Mass, Fast Atom Bombardment
  • Sulfur Radioisotopes


  • Gangliosides
  • Receptors, Virus
  • Sulfur Radioisotopes