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Unité de Pathogénie Microbienne Moléculaire et Unité Institut National de la Santé et de la Recherche Médicale 389, Institut Pasteur, 75724 Paris cédex 15, France
Interaction of Shigella flexneri with
epithelial cells includes contact of bacteria with the cell surface and
release of Ipa proteins through a specialized type III
secreton. A complex signaling process involving activation of
small GTPases of the Rho family and c-src causes major
rearrangements of the subcortical cytoskeleton, thereby allowing
bacterial entry by macropinocytosis. After entry, shigellae escape to
the cell cytoplasm and initiate intracytoplasmic movement through polar
nucleation and assembly of actin filaments caused by bacterial surface
protein IcsA, which binds and activates neuronal Wiskoff-Aldrich
syndrome protein (N-WASP), thus inducing actin nucleation in an
Arp 2/3-dependent mechanism. Actin-driven motility promotes efficient
colonization of the host cell cytoplasm and rapid cell-to-cell spread
via protrusions that are engulfed by adjacent cells in a
cadherin-dependent process. Bacterial invasion turns infected cells to
strongly proinflammatory cells through sustained activation of nuclear
factor-
B. A major consequence is interleukin (IL)-8 production,
which attracts polymorphonuclear leukocytes (PMNs). On transmigration,
PMNs disrupt the permeability of this epithelium and promote its
invasion by shigellae. At the early stage of infection, M cells of the
follicle-associated epithelium allow bacterial translocation.
Subsequent apoptotic killing of macrophages in a caspase
1-dependent process causes the release of IL-1
and IL-18, which
accounts for the initial steps of inflammation.
dysentery; epithelium; colon; inflammation
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