Inhibition ofHelicobacter pyloriurease activityin vivoby the synthetic nickel binding protein Hpn

• DOI: 10.1556/eujmi.3.2013.1.11
• Publication Date: 2013-03-14T02:11:59Z
• Authors: Kerstin A. Heyl; André Fischer; Ulf B. Göbel; Peter Henklein; Markus M. Heimesaat; Stefan Bereswill
• Keywords: Pepsin; Hydrogenase

Helicobacter pylori infection is the most common cause of gastroduodenal ulcerations worldwide.Adaptation H. to acidic environment mediated by urease splitting urea into carbon dioxide and ammonia.Whereas neutralization acid ammonia essential for gastric colonization, catalytic activity nickel ions.Therefore, uptake metabolism play key roles in considered first line target drug development vaccination.Since binding within cells Histidine-rich protein designated Hpn, we investigated whether a synthetic Hpn capable abrogating live liquid cultures.Supplementation growth media with completely inhibited acitivity cells, indicating that effectively blocked Hpn.Thus, chelation stronger than offering therapeutic use Hpn.Although was confirmed assays vitro, its anti-H.pylori directed strategy will further need be adapted given protons interfere degraded pepsin.