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Cytoskeleton‐modulating effectors of enteropathogenic and enterohemorrhagic Escherichia coli : role of EspL2 in adherence and an alternative pathway for modulating cytoskeleton through Annexin A2 function
Author(s) -
Tobe Toru
Publication year - 2010
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2010.07654.x
Subject(s) - annexin a2 , enteropathogenic escherichia coli , intimin , microbiology and biotechnology , cytoskeleton , effector , biology , actin cytoskeleton , actin , secretion , type three secretion system , annexin , escherichia coli , cell , biochemistry , enterobacteriaceae , virulence , gene
Enterohemorrhagic Escherichia coli (EHEC) and enteropathogenic Escherichia coli (EPEC) are attaching/effacing pathogens that possess a type III secretion system and deliver a variety of effectors into host cells for successful infection. EHEC produces at least 20 effector families with various functions. Reorganization of the cellular cytoskeleton at the adherent site is a hallmark of these pathogens. EspL2 of EHEC is a novel effector class that can modulate the cellular cytoskeleton. By interacting with and activating Annexin A2, EspL2 contributes to the formation of a condensed microcolony and may adhere to host cells in a translocated intimin receptor‐independent manner. The interaction of EspL2 with Annexin A2 increases F‐actin bundling activity and strengthens the membrane–cytoskeleton linkage, resulting in the condensation of actin fibers and the induction of a pseudopod‐like structure. Membrane microdomains, namely the lipid raft, which is rich in Annexin A2, may be a platform by which EHEC/EPEC infection modulates cellular signaling and the cytoskeleton.