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The number of GP2-expressing cells was significantly increased after infection with the WT, but not after infection with the ��sopB S. Typhimurium AZD8055 purchase strain ( Figure?6G). Furthermore, the immunohistological staining for Slug revealed a statistically significant increase in Slug expression in tissue sections of PPs from mice infected with WT, but not in those infected with the ��sopB S. Typhimurium strain ( Figure?6H), confirming that SopB is critical to S. Typhimurium-mediated induction of the EMT regulator Slug and M cells in?vivo. Here we show that S. Typhimurium is able to transform follicle-associated intestinal epithelial cells into M cells in order to enhance bacterial translocation across the intestinal mucosa. Specifically, the TTSS effector protein SopB plays a central role in inducing RANKL- and Wnt/��-catenin-regulated signaling that converges to trigger differentiation of a topographically restricted subset of enterocytes into M cells. This study provides explanation to a long-standing question in the field and reveals a host-pathogen interaction involving Ceramidase pathogen-driven transformation of host cells to promote invasion. Previous work has reported an increase in M cell number and/or enhanced transcytosis activity within the FAE following microbial challenge. Specifically, S. Typhimurium was shown to cause an increase in the number of M cells in mouse FAE at 12?hr of infection ( Savidge, 1996). Similarly, other pathogens have been reported to induce rapid (Anti-cancer Compound Library purchase a panel of S. Typhimurium mutant strains, we demonstrated that SopB is an essential effector protein that mediates the RANKL-dependent differentiation of M cells in culture. Of the range of different effector proteins that S. Typhimurium injects into host cells, the phosphoinositide phosphatase SopB is one of the most versatile proteins and controls a number of cellular pathways during different stages of infection ( Hernandez et?al., 2004; Knodler et?al., 2005; Patel et?al., 2009). Remarkably, all of these activities are strictly dependent on the phosphatase activity of SopB.