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Role of lipid rafts in Shiga toxin 1 interaction with the apical surface of Caco-2 cells

¹ Department of Medicine, Johns Hopkins University, Baltimore, MD, USA
² Department of Biology, Johns Hopkins University, Baltimore, MD, USA

*Author for correspondence (e-mail: olukrn{at}yahoo.com)

Accepted August 8, 2001

Enterohemorrhagic Escherichia coli producing Shiga toxins 1 and/or 2 have become major foodborne pathogens. The specific binding of Shiga toxin 1 B-subunit to its receptor, a neutral glycolipid globotriaosylceramide Gb₃, on the apical surface of colonic epithelium followed by toxin entry into cells are the initial steps of the process, which can result in toxin transcytosis and systemic effects of infection including hemolytic uremic syndrome. Understanding the complex mechanisms of Shiga toxin 1 binding and internalization may help to develop new strategies directed at preventing toxin internalization. Fluorescence resonance energy transfer microscopy revealed the clustering of Shiga toxin receptors Gb₃ in lipid rafts with another glycosphingolipid G_M1 on the apical surface of highly polarized intestinal epithelial Caco-2 cells. Lipid rafts disruption significantly decreased internalization of Shiga toxin 1 B-subunit. Although disruption of lipid rafts by cholesterol depletion did not affect the amount of bound Shiga toxin 1 B-subunit, lipid rafts are necessary for toxin uptake across the apical membrane of Caco-2 cells.

Key words: Shiga toxin, Globotriaosylceramide Gb₃, Lipid rafts, Cholesterol, Caco-2 cells

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