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Vol. 11, Issue 5, 1775-1787, May 2000
and
*Institut National de la Santé et de la Recherche
Médicale, Unité 452, Faculté de Médecine, 06107 Nice Cedex 2, France; and Cytotoxic necrotizing factor 1 (CNF1), a protein produced by
pathogenic strains of Escherichia coli, activates the
p21 Rho-GTP-binding protein, inducing a profound reorganization of the
actin cytoskeleton. CNF1 binds to its cell surface receptor on HEp-2
cells with high affinity (Kd = 20 pM).
In HEp-2 cells the action of CNF1 is not blocked in the presence of
filipin, a drug described to reduce cholera toxin internalization by
the caveolae-like mechanism. Moreover, HEp-2 cells, which express a
dominant negative form of proteins that impair the formation of
clathrin coated-vesicles and internalization of transferrin (Eps15,
dynamin or intersectin-Src homology 3), are still sensitive to
CNF1. In this respect, the endocytosis of CNF1 is similar to the plant
toxin ricin. However, unlike ricin toxin, CNF1 does not cross the Golgi
apparatus and requires an acidic cell compartment to transfer its
enzymatic activity into the cytosol in a manner similar to that
required by diphtheria toxin. As shown for diphtheria toxin, the
pH-dependent membrane translocation step of CNF1 could be mimicked at
the level of the plasma membrane by a brief exposure to a pH of Institut National de la
Santé et de la Recherche Médicale, E9925, Faculté de
Médecine Necker-Enfants Malades, 75756 Paris Cedex 15, France
5.2.
CNF1 is the first bacterial toxin described that uses both a
clathrin-independent endocytic mechanism and an acidic-dependent
membrane translocation step in its delivery of the catalytic domain to
the cell cytosol.
Corresponding author. E-mail address:
boquet{at}unice.fr.
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