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© Research
Publication : EMBO reports

Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in EMBO reports - 07 Jul 2006

Hamiaux C, van Eerde A, Parsot C, Broos J, Dijkstra BW

Link to Pubmed [PMID] – 16826238

EMBO Rep. 2006 Aug;7(8):794-9

Invasion of epithelial cells by Shigella flexneri is characterized by cytoskeletal rearrangements of the host cell membrane, promoting internalization of the bacterium. The bacterial effector IpaA is injected into the epithelial cell by a type III secretion apparatus and recruits vinculin to regulate actin polymerization at the site of entry. We analysed the complex formed between a carboxy-terminal fragment of IpaA (IpaA(560-633)) and the vinculin D1 domain (VD1), both in crystals and in solution. We present evidence that IpaA(560-633) has two alpha-helical vinculin-binding sites that simultaneously bind two VD1 molecules. The interaction of IpaA(560-633) with VD1 is highly similar to the interaction of the endogenous, eukaryotic proteins talin and alpha-actinin with VD1, showing that Shigella uses a structural mimicry strategy to activate vinculin.

http://www.ncbi.nlm.nih.gov/pubmed/16826238