SummaryShigella is a genus of highly adapted bacterial pathogens that cause bacillary dysentery in humans.Bacteria reaching the colon invade intestinal epithehal cells by a process of bacterial-directed endocytosis mediated by the Ipa proteins: IpaB, IpaC, and IpaD of Shigella. The invasion of epithelial cells is thought to be a receptor-mediated phenomenon, although the cellular components of the host that interact with the Ipa proteins have not yet been identified. We report here that in a Shigellaflexneri invasive system and Chinese hamster ovary (CHO) cell monolayers, the Ipa proteins were capable of interacting directly with oL5131 integrin. The invasive capacity of S. flexneri for CHO cells increased as levels of cx5131 integrin were elevated. When CHO cells were infected with S. flexneri, the tyrosine phosphorylation both ofpp 125 F~, an integrin-regulated 125 K focal adhesion kinase, and of paxillin was stimulated. In contrast, an isogenic strain of S. flexneri that was defective in invasion owing to a mutation in its spa32 gene failed to induce such phosphorylation. Under in vitro and in vivo conditions, the released IpaB, IpaC, and IpaD proteins bound to ot5[~ 1 integrin in a manner different from that of soluble fibronectin but similar to that of the tissue form of fibronectin. At the site of attachment of S. flexneri to CHO cells, ot5131 integrin converged with polymerization of actin. These data thus suggest that the capacity oflpa proteins to interact with o~5151 integrin may be an important Shigella factor in triggering the reorganization of actin cytoskeletons.
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