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Exported proteases of  Helicobacter pylori  ( H. pylori ) are potentially involved in pathogen-associated disorders leading to gastric inflammation and neoplasia. By comprehensive sequence screening of the  H. pylori  proteome for predicted secreted proteases, we retrieved several candidate genes. We detected caseinolytic activities of several such proteases, which are released independently from the  H. pylori  type IV secretion system encoded by the  cag  pathogenicity island ( cag PAI). Among these, we found the predicted serine protease HtrA (Hp1019), which was previously identified in the bacterial secretome of  H. pylori . Importantly, we further found that the  H. pylori  genes  hp1018  and  hp1019  represent a single gene likely coding for an exported protein. Here, we directly verified proteolytic activity of HtrA  in vitro  and identified the HtrA protease in zymograms by mass spectrometry. Overexpressed and purified HtrA exhibited pronounced proteolytic activity, which is inactivated after mutation of Ser205 to alanine in the predicted active center of HtrA. These data demonstrate that  H. pylori  secretes HtrA as an active protease, which might represent a novel candidate target for therapeutic intervention strategies.

Prediction of Extracellular Proteases of the Human Pathogen Helicobacter pylori Reveals Proteolytic Activity of the Hp1018/19 Protein HtrA