Helicobacter pylori biofilm interference by N-acyl homoserine lactonases: in vitro and in silico approaches.

Background: Qurom quenching enzyme have an impact on treatment efficacy and prevent the recurrence of Helicobacter pylori biofilm-related infections, although it has not been thoroughly investigated in vitro and in silico. The current study aims to characterize the N-acyl homoserine lactonase, the quorum quenching AiiA protein of Bacillus licheniformis against H. pylori biofilm.

Methods and results: In this study, AiiA protein were screened for their anti-biofilm activity, was found to effectively control biofilm formation of H. pylori with concentrations ranging from 2 to 10 µg/mL. According to CLSM and COMSTAT analysis, the untreated substratum had the robust biofilm biomass of 25-18 µM and biovolume of 3-4 mm³ /mm². The total biofilm biovolume and average biofilm thickness were considerably reduced by 40% with a single application of 10 µg/mL of AiiA protein. The biofilm treated with AiiA exhibited a lower urease and polysaccharides than to the untreated biofilm. Further, in silico analysis, exhibited a greater interaction of AiiA against the outer membrane proteins of H. pylori compared to virulence factors. The conserved domains in the binding pockets of AiiA proteins showed a highest binding affinity proving the catalytic activity of the protein.

Conclusion: In this study, the H. pylori biofilm architecture, exopolysaccharide and urease were significantly controlled by our purified N-acyl homoserine lactonase from B. licheniformis. Furthermore, the molecular docking showed the significant interaction between AiiA and key biofilm forming and virulence proteins proved an excellent antibiofilm activity controlling the infections of H. pylori human pathogen.