InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase.
The Listeria monocytogenes surface protein InlB promotes bacterial entry into mammalian cells. Here, we identify a cellular surface receptor required for InlB-mediated entry. Treatment of mammalian cells with InlB protein or infection with L. monocytogenes induces rapid tyrosine phosphorylation of Met, a receptor tyrosine kinase (RTK) for which the only known ligand is Hepatocyte Growth Factor ( HGF). Like HGF, InlB binds to the extracellular domain of Met and induces "scattering" of epithelial cells. Experiments with Met-positive and Met-deficient cell lines demonstrate that Met is required for InlB-dependent entry of L. monocytogenes. InlB is a novel Met agonist that induces bacterial entry through exploitation of a host RTK pathway.[1]References
- InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Shen, Y., Naujokas, M., Park, M., Ireton, K. Cell (2000) [Pubmed]
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