InlB-Dependent Internalization of Listeria Is Mediated by the Met Receptor Tyrosine Kinase

By Yang Shen, M. Naujokas, Morag Park, K. Ireton. 2000

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Listeria monocytogenes: a multifaceted model (2006, background): “Met is a protein tyrosine kinase, and the endogenous ligand of this receptor is hepatocyte growth factor (HGF”
Immune responses to Listeria monocytogenes (2004, background): “fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=986892">internalin B , which binds the hepatocyte growth factor receptor present at the cell surface of hepatocyte”
Invasive and Adherent Bacterial Pathogens Co-Opt Host Clathrin for Infection (2007, unknown): “Listeria invasion proteins InlA and InlB interact with cellular E-cadherin and Met, respectively (Gaillard et al., 1991; Lecuit et al., 1999; Shen et al., 2000 );Yersinia invasin (inv) directly binds to b1- integrin (Isberg and Leong, 1990), while Staphyloccocus express fibronectin-binding proteins”
Bacterial adhesion and entry into host cells. (2006, unknown): “The main cellular receptor for InlB is the hepatocyte growth factor receptor Met, a receptor tyrosine kinase (Shen et al., 2000), which binds to the leucine rich repeats of InlB.”
How bacterial pathogens colonize their hosts and invade deeper tissues. (2015, background): “Internalization of Listeria is mediated by two surface proteins, InlA and InlB, which respectively target E-cadherin and the hepatocyte growth factor receptor Met, which are both host plasma membrane proteins [52,53].”