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Spectrin is sequestered to Enteropathogenic Escherichia coli pedestals
Author(s) -
Ruetz Tyson,
Guttman Julian
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.827.4
Subject(s) - intimin , spectrin , effector , enteropathogenic escherichia coli , biology , cytoskeleton , actin , microbiology and biotechnology , secretion , mutant , escherichia coli , enterobacteriaceae , genetics , cell , biochemistry , gene
Enteropathogenic Escherichia coli (EPEC) is a bacterial pathogen that colonizes the small intestine of humans, causing serious diarrhea that can result in death. Upon attachment to host cells, EPEC injects effector proteins that hijack numerous sub‐cellular components, which leads to the generation of actin‐rich pedestals located within the host cells beneath the bacteria. A key effector responsible for pedestal formation is the translocated intimin receptor (Tir). Because EPEC alters the functions of all major cytoskeletal components examined thus far (actin filaments, intermediate filaments and microtubules) we investigated another cytoskeletal protein, spectrin, to test the hypothesis that the spectrin cytoskeleton is also modified by these pathogens. Spectrin was immunolocalized during in vitro infections with wild‐type EPEC and compared to mutants defective in effector secretion as well as Tir‐specific bacterial mutants. Surprisingly, spectrin was sequestered to wild‐type EPEC pedestals, but not to sites of bacterial attachment using EPEC effector mutants. Western blots identified that spectrin levels were equivalent in both infected and control cells. Our findings provide the first evidence of spectrin involvement in pathogenic E. coli ‐mediated disease, whereby spectrin is re‐localized to the pedestals of EPEC. Grant Funding Source CIHR, NSERC