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The Dsb protein family is responsible for introducing disulfide bonds into nascent proteins in prokaryotes, stabilizing the structure of many proteins.  Helicobacter pylori  HP0231 is a Dsb-like protein, shown to catalyze disulfide bond formation and to participate in redox homeostasis. Notably, many  H .  pylori  virulence factors are stabilized by the formation of disulfide bonds. By employing  H .  pylori  HP0231 deficient strains we analyzed the effect of lack of this bacterial protein on the functionality of virulence factors containing putative disulfide bonds. The lack of  H .  pylori  HP0231 impaired CagA translocation into gastric epithelial cells and reduced VacA-induced cellular vacuolation. Moreover,  H .  pylori  HP0231 deficient bacteria were not able to colonize the gastric mucosa of mice, probably due to compromised motility. Together, our data demonstrate an essential function for  H .  pylori  HP0231 in gastric colonization and proper function of bacterial virulence factors related to gastric pathology.

Helicobacter pylori HP0231 Influences Bacterial Virulence and Is Essential for Gastric Colonization