InlB-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 M...

Full description

Saved in:
Bibliographic Details
Published inCell Vol. 103; no. 3; pp. 501 - 510
Main Authors Shen, Yang, Naujokas, Monica, Park, Morag, Ireton, Keith
Format Journal Article
LanguageEnglish
Published Elsevier Inc 01.10.2000
Online AccessGet full text

Cover

More Information
Summary: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.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)00141-0