pylori infection (Sayi et al., 2009). Conversely, IFN-γ can lower the colonization of H. pylori and is critical for H. pylori clearance (Yamamoto et al., 2004; Sayi et al., 2009). Most evidence indicates that IFN-γ plays a protective role in H. pylori infection (Sawai et al., 1999; Hasegawa et al., 2004; Yamamoto et al., 2004; Cinque et al., 2006; Sayi et al., 2009); furthermore, this occurs principally between IFN-γ and the bacteria. Our results provide further evidence that IFN-γ may help control H. pylori infection indirectly by controlling its virulence factor, CagA. Previous studies suggested that IFN-γ is a key

antimicrobial factor, against, in particular, intracellular pathogens such as viruses and Mycobacterium tuberculosis (Young et al., 2007). We too showed that Ceritinib in vivo IFN-γ can downregulate the expression of the major virulent factor CagA in the extracellular bacterium H. pylori for an indirect effect on such pathogens. IFN-γ

is a well-known immune active factor (Wu et al., 2005), and its production is accompanied by host immunity change in response to H. pylori (Shimizu et al., 2004; Pellicanòet al., 2007). In turn, IFN-γ can downregulate CagA expression. We found that H. pylori SS1 had the same effect as H. pylori 26695 (data not shown), but this needs to be confirmed by animal models. Hence, immune responses to H. pylori play an important role in the defense see more against bacterial infection. In conclusion, we found that INF-γ can bind to the surface of H. pylori, which results in the downregulated expression of CagA, the major virulent factor in H. pylori. These findings provide insights into understanding the effect of a high level of IFN-γ on gastric mucosa infected with H. pylori and how IFN-γ can CYTH4 contribute to control H. pylori infection. The mechanism by which IFN-γ causes downregulation of CagA needs further investigation. This work was supported by the National Natural Science

Foundation of China (Nos 30770118, 30972775, 30800406, 30800037, 30971151 and 30800614), the National Basic Research Program of China (973 Program 2007CB512001) and the Science Foundation of Shandong Province, China (Nos ZR2009CZ001 and ZR2009CM002). Yinghui Zhao and Yabin Zhou contributed equally to this work. Fig. S1. Effect of IFN-γ on the growth of Helicobacter pylori. Fig. S2. Binding of IFN-γ to Helicobacter pylori. Please note: Wiley-Blackwell is not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. “
“The adenosine monophosphate-activated protein kinase (AMPK) is activated by antigen receptor signals and energy stress in T cells. In many cell types, AMPK can maintain energy homeostasis and can enforce quiescence to limit energy demands.