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Infection and Immunity, February 2003, p. 739-746, Vol. 71, No. 2
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.2.739-746.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Sensitivity of Polarized Epithelial Cells to the Pore-Forming Toxin Aerolysin

Laurence Abrami,¹ Marc Fivaz,^1, Pierre-Etienne Glauser,¹ Nakaba Sugimoto,² Chiara Zurzolo,³ and F. Gisou van der Goot^1*

Department of Genetics and Microbiology, University of Geneva, 1211 Geneva 4, Switzerland,¹ Division of Advanced Medical Bacteriology, Department of Molecular and Applied Medicine, Medical School of Osaka University, Osaka, Japan,² Dipartimento di Biologia e Patologia Cellulare e Molecolare, Medical School, Naples University "Federico II," 80131 Naples, Italy³

Received 26 September 2002/ Returned for modification 1 November 2002/ Accepted 6 November 2002

Aerolysin is one of the major virulence factors produced by Aeromonas hydrophila, a human pathogen that produces deep wound infection and gastroenteritis. The toxin interacts with target mammalian cells by binding to the glycan core of glycosylphosphatidyl inositol (GPI)-anchored proteins and subsequently forms a pore in the plasma membrane. Since epithelial cells of the intestine are the primary targets of aerolysin, we investigated its effect on three types of polarized epithelial cells: Caco-2 cells, derived from human intestine; MDCK cells, a well-characterized cell line in terms of protein targeting; and FRT cells, an unusual cell line in that it targets its GPI-anchored proteins to the basolateral plasma membrane in contrast to other epithelial cells, which target them almost exclusively to the apical surface. Surprisingly, we found that all three cell types were sensitive to the toxin from both the apical and the basolateral sides. Apical sensitivity was always higher, even for FRT cells. In contrast, FRT cells were more sensitive from the basolateral than from the apical side to the related toxin Clostridium septicum alpha-toxin, which also binds to GPI-anchored proteins but lacks the lectin binding domain found in aerolysin. These observations are consistent with the notion that a shuttling mechanism involving low-affinity interactions with surface sugars allows aerolysin to gradually move toward the membrane surface, where it can finally encounter the glycan cores of GPI-anchored proteins.

Editor: J. T. Barbieri

Present address: Department of Molecular Pharmacology, Stanford University, Stanford, Calif.

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