A novel role of catalase in cholesterol uptake of Helicobacter pylori

•H. pylori catalase (KatA) exhibits high binding affinity for cholesterol.•KatA with normal folding conformation plays an important role in cholesterol uptake.•Putative amino acid sequence of KatA includes a number of cholesterol-binding sites.•H. pylori KatA is suggested to act as a cholesterol-binding or -storage protein. Helicobacter pylori infection is known to be a significant risk factor for the development of gastric cancers in humans. This pathogen exhibits unique biological characteristics in membrane lipid composition. Specifically, H. pylori incorporates exogenous cholesterol into biomembranes and uses cholesterol as the membrane lipid constituents. A previous study by our group demonstrated that phosphatidylethanolamine of H. pylori functions as the cholesterol-binding lipid. It is, however, unclear whether H. pylori is equipped with protein molecules involved in the cholesterol uptake. We, therefore, examined H. pylori proteins that tightly bind to cholesterol. As a consequence, H. pylori catalase (KatA) turned out to be a candidate of the cholesterol uptake-associated protein. In addition, an H. pylori mutant strain that expresses KatA protein lacking catalase activity was significantly lower in total cholesterol contents than the wild-type H. pylori strain. The putative amino acid sequence of KatA found out to contain a number of the cholesterol recognition/interaction amino acid consensus sequence domains (CRAC and CARC domains). These results suggest that H. pylori KatA with normal folding conformation acts as the cholesterol-binding or -storage protein.