In silico analyzes of porins involved in niche adaptation: Exploring the role of Helicobacter pylori outer membrane phospholipase A in acid tolerance.

Abstract

Helicobacter pylori is an ulcer-causing bacterium that evolutionary needs to adapt quickly to changing conditions. Hilde Synnøve Vollan’s bioinformatics studies revealed that H. pylori outer membrane phospholipase A (OMPLA) is multifunctional with both enzymatic and pore activity. OMPLA is a protein found in a variety of bacterial species, and usually functions as an enzyme that degrades the outer membrane. Previous studies indicate that OMPLA must be intact for H. pylori survival in an acidic environment, while its enzymatic activity is not required. The present study presents the hypothesis that OMPLA is involved in acid management. Analyzes of the modeled H. pylori OMPLA 3D structure indicate that the niche-adaption likely is urea-influx and ammonium-efflux. This model may be paradigmatic for all gastric Helicobacter species. This work will be used in future studies aimed at preventing ulcers and gastric cancers caused by H. pylori.