Host-pathogen interactions during entry and actin-based movement of Listeria monocytogenes

Annual Review of Genetics
K Ireton, Pascale Cossart

Abstract

Listeria monocytogenes is a pathogenic bacterium that induces its own uptake into mammalian cells, and spreads from one cell to another by an actin-based motility process. Entry into host cells involves the bacterial surface proteins InlA (internalin) and InlB. The receptor for InlA is the cell adhesion molecule E-cadherin. InlB-mediated entry requires activation of the host protein phosphoinositide (PI) 3-kinase, probably in response to engagement of a receptor. Actin-based movement of L. monocytogenes is mediated by the bacterial surface protein ActA. The N-terminal region of this protein is necessary and sufficient for polymerization of host cell actin. Other host proteins involved in bacterial motility include profilin, Vasodilator-Stimulated Phosphoprotein (VASP), the Arp2/Arp3 complex, and cofilin. Studies of entry and intracellular movement of L. monocytogenes could lead to a better understanding of receptor-ligand signaling and dynamics of actin polymerization in mammalian cells.

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Nov 24, 1999·Archives of Biochemistry and Biophysics·M KuhnW Goebel
Aug 10, 2000·FEMS Microbiology Letters·I TsarfatyE Segal
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Methods Mentioned

BETA
GTPase
GTPases
two-hybrid
transfection
fluorescence microscopy

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