A strain of human influenza A virus binds to extended but not short gangliosides as assayed by thin-layer chromatography overlay

A human strain of influenza virus (A, H1N1) was shown to bind in an unexpec ted way to leukocyte and other gangliosides when compared with avian virus (A, H4N6) as assayed on TLC plates. The human strain bound only to species with about 10 or more sugars, white the avian strain bound to a wide range of gangliosides including the 5-sugar gangliosides, By use of specific tect ins, antibodies, and FAB and MALDI-TOF mass spectrometry an attempt was don e to preliminary identify the sequences of leukocyte gangliosides recognize d by the human strain. The virus binding pattern did not follow binding by VIM-2 monoclonal antibody and was not identical with binding by anti-siaiyl Lewis x antibody, There was no binding by the virus of linear NeuAc alpha3 - or NeuAc alpha6-containing gangliosides with up to seven monosaccharides per mol of ceramide, Active species were minor NeuAc alpha6-containing mole cules with probably repeated HexHexNAc units and fucose branches. This inve stigation demonstrates marked distinctions in the recognition of gangliosid es between avian and human influenza viruses. Our data emphasize the import ance of structural factors associated with more distant parts of the bindin g epitope and the complexity of carbohydrate recognition by human influenza viruses.