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Staying alive overdosed: how does Helicobacter pylori control urease activity?
Kerstin Stingl1, Hilde De Reuse
1Institut Pasteur, Unité de Pathogénie Bactérienne des Muqueuses, 28, rue du Dr. Roux, F-75724 Paris, France. stingl@pasteur.fr
International Journal of Medical Microbiology : IJMM
|September 22, 2005
Summary
Helicobacter pylori produces excess urease to maintain an intracellular nickel pool. This ensures daughter cells have sufficient active urease, even during nickel deficiency, aiding pathogen survival.
Area of Science:
- Microbiology
- Biochemistry
Background:
- Urease is a nickel metalloenzyme crucial for Helicobacter pylori virulence.
- It enables acid resistance, facilitating colonization and persistence in the gastric environment.
Purpose of the Study:
- To investigate the regulatory mechanisms of urease activity in H. pylori.
- To understand the role of excess urease production in nickel homeostasis and virulence.
Main Methods:
- In vitro analysis of urease activity under varying nickel conditions.
- Modeling of nickel ion binding and intracellular pool maintenance.
Main Results:
- H. pylori urease activity is regulated at multiple levels, including nickel insertion and urea availability (via UreI).
- Even with limited nickel, a small proportion of activated urease confers acid resistance.
- Excess urease maintains an intracellular Ni2+ pool for daughter cells.
Conclusions:
- The overproduction of urease serves as a nickel storage mechanism.
- This strategy ensures sustained virulence and colonization potential in nickel-limited environments.