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- Title
Lymphostatin regulates epithelial barrier function.
- Authors
Klapproth, Jan-Michael Axel; Sasaki, Maiko; Nusrat, Asma; Babbin, Brian
- Abstract
Lymphocyte inhibitory factor A (lifA) encodes for lymphostatin from Citrobacter rodentium and is responsible for colonization of extraintestinal organs. We hypothesize that lymphostatin regulates epithelial barrier function by modifying Rho GTPases. lifA glycosyltransferase (CrG1M21) and the protease motif (CrPrM5) were mutated by homologous recombination and epithelial barrier function was analyzed by FITC-dextran flux. Rho GTPase activation status was determined by Rhotekin and Pak binding assays. All strains induced increased paracellular flux which was significantly less for CrG1M21. Interestingly, ZO-1 was redistributed from tight junctions (TJs) following infection with WT and CrPrM5 but not CrG1M21. While both WT and CrPrM5 inhibited activation of Cdc42, infection with CrG1M21 resulted in increased Cdc42 activity. In contrast to WT and CrG1M21, CrPrM5 failed to activate RhoA. In summary, lifA glycosyltransferase motif is critical for inhibition of Cdc42 and the protease motif is essential for activation of RhoA. We conclude that inhibition of Cdc42 by the glycosyltransferase plays a significant role in regulating epithelial barrier function.
- Subjects
PROTEINS; EPITHELIAL cells; GUANOSINE triphosphatase; TIGHT junctions; PROTEOLYTIC enzymes
- Publication
FASEB Journal, 2007, Vol 21, Issue 5, pA191
- ISSN
0892-6638
- Publication type
Article