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Infection with Campylobacter jejuni Induces Tyrosine‐Phosphorylated Proteins into INT‐407 Cells

The mechanisms used by Campylobacter jejuni to induce internalization into host intestinal epithelial cells have not been defined. In this study, we obtained evidence that exposure of INT‐407 cells to protein kinase inhibitors results in decreased invasion of these cells by C. jejuni in a dose dependent manner. Preincubation of INT‐407 cells in the presence of staurosporine, tyrphostin 46 and genistein decreased invasion of these cells by C. jejuni significantly. Moreover, C. jejuni infection of INT‐407 cells induced tyrosine phosphorylation of several Triton X‐100 soluble proteins with approximate molecular weights of 170, 145, 90, 60 and 55 kDa that were absent or reduced in the presence of genistein in cells after 1 hr of pretreatment. These data suggest that tyrosine protein kinase‐linked pathways strongly regulate the internalization of C. jejuni into intestinal epithelial cells.