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We have previously shown that  Lactobacillus gasseri  Kx110A1, a human stomach isolate, can colonize mouse stomach and reduce the initial colonization of  Helicobacter pylori . Here, we investigated the role of sortase-dependent proteins (SDPs) involved in these functions by the construction of a mutant for  srtA , the gene encoding the housekeeping sortase that covalently anchors SDPs to the cell surface. The  srtA  mutant showed a decrease in hydrophobicity and autoaggregation under acidic conditions, indicating the effect of SDPs on cell surface properties. Correspondingly, the  srtA  mutant lost the capacity to adhere to gastric epithelial cells, thus resulting in an inability to provide a physical barrier to prevent  H. pylori  adherence. These results indicate that sortase A is a key determinant of the cell surface properties of  L. gasseri  Kx110A1 and contributes to  Lactobacillus -mediated exclusion of  H. pylori . Understanding the molecular mechanisms by which lactobacilli antagonize  H. pylori  might contribute to the development of novel therapeutic strategies that take advantage of health-promoting bacteria and reduce the burden of antibiotic resistance.

Role of Sortase A in Lactobacillus gasseri Kx110A1 Adhesion to Gastric Epithelial Cells and Competitive Exclusion of Helicobacter pylori