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Journal of Cell Science 115, e1701-e1701 (2002)
© 2002 The Company of Biologists Limited

In this issue

InlB: a bacterial tyrosine kinase receptor agonist


Synthesis of proteins that mimic natural host cell ligands and induce uptake of bacteria expressing them is an effective invasion strategy used by several pathogenic bacteria. Listeria monocytogenes, which causes serious infections in immunocompromised individuals and pregnant women, produces two such proteins: InlA and InlB. In a Commentary on p. 3357, Hélène Bierne and Pascale Cossart discuss work that is shedding light on how InlB functions. The protein binds to hepatocyte growth factor receptors (HGF-Rs) on the surface of hepatocytes, epithelial cells and endothelial cells. This stimulates internalization of the bacterium by a mechanism similar to phagocytosis: the cell extends membrane around the particle and forms a continuous F-actin cup, which is disassembled following engulfment. Interestingly, in addition to stimulating pathways required for phagocytosis, InlB has other effects on target cells. It acts as a tyrosine kinase receptor agonist, regulating signalling cascades involving phospholipase C{gamma}1, Akt and NF-{kappa}B. This could be important after internalization and might promote cell survival once the bacterium is released into the cytosol.


Related articles in JCS:

InlB, a surface protein of Listeria monocytogenes that behaves as an invasin and a growth factor
Hélène Bierne and Pascale Cossart
JCS 2002 115: 3357-3367. [Abstract] [Full Text]  




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