Open AccessThe A nnexin A 2/p11 complex is required for efficient invasion of S almonella T yphimurium in epithelial cells
Author(s) -
Jolly Carrie,
Winfree Seth,
Hansen Bryan,
SteeleMortimer Olivia
Publication year - 2014
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12180
Subject(s) - biology , annexin a2 , effector , salmonella enterica , microbiology and biotechnology , type three secretion system , membrane ruffling , secretion , actin , internalization , annexin , salmonella , cytoskeleton , cell , bacteria , biochemistry , virulence , genetics , gene
Summary The facultative intracellular pathogen, S almonella enterica , triggers its own uptake into non‐phagocytic epithelial cells. Invasion is dependent on a type 3 secretion system ( T 3 SS ), which delivers a cohort of effector proteins across the plasma membrane where they induce dynamic actin‐driven ruffling of the membrane and ultimately, internalization of the bacteria into a modified phagosome. In eukaryotic cells, the calcium‐ and phospholipid‐binding protein A nnexin A 2 ( AnxA 2) functions as a platform for actin remodelling in the vicinity of dynamic cellular membranes. AnxA 2 is mostly found in a stable heterotetramer, with p11, which can interact with other proteins such as the giant phosphoprotein AHNAK . We show here that AnxA 2, p11 and AHNAK are required for T 3 SS ‐mediated S almonella invasion of cultured epithelial cells and that the T 3 SS effector SopB is required for recruitment of AnxA 2 and AHNAK to S almonella invasion sites. Altogether this work shows that, in addition to targeting Rho ‐family GTPases , S almonella can intersect the host cell actin pathway via AnxA 2.