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. 1990 Jan;58(1):43–47. doi: 10.1128/iai.58.1.43-47.1990

Specificity of glycosphingolipid recognition by Entamoeba histolytica trophozoites.

G B Bailey 1, E D Nudelman 1, D B Day 1, C F Harper 1, J R Gilmour 1
PMCID: PMC258406  PMID: 2294057

Abstract

The ability of purified glycosphingolipids to enhance liposome-stimulated Entamoeba histolytica actin polymerization was assessed as a means of defining the specificity of mammalian cell membrane lipid glycan recognition by this parasite. Synthetic liposomes containing a variety of individual glycosphingolipids bearing neutral, straight-chain oligomeric glycans with galactose or N-acetylgalactosamine termini stimulated rapid (90-s) polymerization of amoeba actin. Glycans with terminal N-acetylglucosamine residues were not stimulatory at all or were only weakly stimulatory. Glycans with glucose, N-acetylglucosamine, galactose, and N-acetylgalactosamine as the penultimate residue were recognized. Attachment of N-acetylneuraminate to the terminal residue of a stimulatory glycosphingolipid eliminated activity; attachment of fucose to the penultimate sugar reduced activity. Glycans with a terminal beta 1-4 or 1-3 glycosidic bond were most effective; glycans with terminal alpha 1-4 or 1-3 glycosides were less effective. The activity of glycans with both beta- and alpha-linked terminal glycosides was inhibited by lactose, suggesting recognition of both configurations by a single amoeba protein. The ability of liposomes to stimulate actin polymerization reflected the extent of liposome phagocytosis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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