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Ultrastructural analysis of toxin binding and entry into mammalian cells

Nature volume 251, pages 628–630 (1974)Cite this article

Abstract

VERY low concentrations of phytotoxins can kill mammalian cells, and some of them, such as ricin and abrin, isolated from Ricinus communis and Abrus precatorius, have been reported to suppress protein synthesis in cells1–3 and cell-free systems4,5. Ricin inhibits peptide chain elongation by catalytically inactivating the 60S subunits of ribosomes5–7. It is a galactosebinding glycoprotein of molecular weight 60,000, containing two nonidentical subunits linked by disulphide bridges8–11 and seems to be identical to the lectin R. communis agglutinin II (RCAII) isolated by affinity chromatography8–12. Ricin, or RCAII, has been used to suppress the growth of ascites tumour cells in vivo13, and as a cell surface probe for oligosaccharide receptors14–17 containing terminal D-galactose or N-acetyl-D-galactosamine-like saccharides11,14,18,19. I have found that RCAII enters mammalian cells by endocytosis (similar to the findings of Oliver et al.20) and is then released into the cytoplasm, where it apparently acts directly on protein synthesis.

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  1. Cancer Council and Electron Microscopy Laboratories, The Salk Institute for Biological Studies, San Diego, California, 92112

    GARTH L. NICOLSON

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NICOLSON, G. Ultrastructural analysis of toxin binding and entry into mammalian cells. Nature 251, 628–630 (1974). https://doi.org/10.1038/251628a0

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