MET-activating Residues in the B-repeat of the Listeria monocytogenes Invasion Protein InlB.

ABSTRACT: The facultative intracellular pathogen Listeria monocytogenes causes listeriosis, a rare but life-threatening disease. Host cell entry begins with activation of the human receptor tyrosine kinase MET through the bacterial invasion protein InlB, which contains an internalin domain, a B-repeat, and three GW domains. The internalin domain is known to bind MET, but no interaction partner is known for the B-repeat. Adding the B-repeat to the internalin domain potentiates MET activation and is required to stimulate Madin-Darby canine kidney (MDCK) cell scatter. Therefore, it has been hypothesized that the B-repeat may bind a co-receptor on host cells. To test this hypothesis, we mutated residues that might be important for binding an interaction partner. We identified two adjacent residues in st

SUBMITTER: Bleymuller WM 

PROVIDER: S-EPMC5207255 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature