Abstract
THE cytotoxicity of the plant lectin ricin, of Ricinus communis seeds, towards mammalian cells is mediated in three steps1. Binding of the toxin to cell surface galactose or N-acetylgalactosamine receptors is followed by entry of the bound lectin into the cells, perhaps by endocytosis2,3 and inhibition of protein synthesis4–6. Several variant lines of cells selected for resistance to ricin have been shown7–10 to bind ricin poorly and to carry much smaller amounts of receptors at the cell surface. We report here that when such a resistant cell line of baby hamster kidney (BHK) fibroblasts8,9 is incubated with a ricin-binding glycolipid fraction prepared from human erythrocytes, glycolipid is taken up and the cells exhibit increased binding of ricin and greater sensitivity to lectin-mediated inhibition of cell protein synthesis. These studies suggest that glycolipids can function in certain circumstances as membrane receptors in the binding of ricin and mediation of ricin cytotoxicity.
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HUGHES, R., GARDAS, A. Phenotypic reversion of ricin-resistant hamster fibroblasts to a sensitive state after coating with glycolipid receptors. Nature 264, 63–66 (1976). https://doi.org/10.1038/264063a0
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DOI: https://doi.org/10.1038/264063a0
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