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Vol. 11, Issue 11, 3897-3909, November 2000
and
*INSERM U452, Faculté de Médecine, 28 Avenue de
Valombrose, 06107 Nice Cedex 2, France; Helicobacter pylori vacuolating toxin (VacA) causes
vacuolation in a variety of cultured cell lines, sensitivity to VacA
differing greatly, however, among the different cell types. We found
that the high sensitivity of HEp-2 cells to VacA was impaired by
treating the cells with phosphatidylinositol-specific
phospholipase C (PI-PLC) which removes
glycosylphosphatidylinositol (GPI)-anchored proteins from the
cell surface. Incubation of cells with a cholesterol-sequestering agent, that impairs both structure and function of
sphingolipid-cholesterol-rich membrane microdomains ("lipid
rafts"), also impaired VacA-induced cell vacuolation. Overexpression
into HEp-2 cells of proteins inhibiting clathrin-dependent endocytosis
(i.e., a dominant-negative mutant of Eps15, the five tandem
Src-homology-3 domains of intersectin, and the K44A dominant-negative
mutant of dynamin II) did not affect vacuolation induced by VacA.
Nevertheless, F-actin depolymerization, known to block the different
types of endocytic mechanisms, strongly impaired VacA vacuolating
activity. Taken together, our data suggest that the high cell
sensitivity to VacA depends on the presence of one or several
GPI-anchored protein(s), intact membrane lipid rafts, and an uptake
mechanism via a clathrin-independent endocytic pathway.
Department of Human
Pathology, University of Pavia and IRCCS Policlinico San Matteo, 27100 Pavia, Italy
Corresponding author. E-mail address:
boquet{at}unice.fr.
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