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Trends Cell Biol. 2002 Jan;12(1):15-20.

Direct modulation of the host cell cytoskeleton by Salmonella actin-binding proteins.

Author information

1
University of Cambridge, Dept of Pathology, Tennis Court Road, CB2 1QP, Cambridge, UK. rdh24@mole.bio.cam.ac.uk

Abstract

Invasive Salmonella trigger their own uptake into non-phagocytic eukaryotic cells by delivering virulence proteins that stimulate signaling pathways and remodel the actin cytoskeleton. It has recently emerged that Salmonella encodes two actin-binding proteins, SipC and SipA, which together efficiently nucleate actin polymerization and stabilize the resulting supramolecular filament architecture. Therefore, Salmonella might directly initiate actin polymerization independently of the cellular Arp2/3 complex early in the cell entry process. This is an unprecedented example of a direct intervention strategy to facilitate entry of a pathogen into a target cell. Here, we discuss the Salmonella actin-binding proteins and how they might function in combination with entry effectors that stimulate Rho GTPases. We propose that membrane-targeted bacterial effector proteins might trigger actin polymerization through diverse mechanisms during cell entry by bacterial pathogens.

PMID:
11854005
[Indexed for MEDLINE]

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