In vitro and in silico approaches of antibiofilm activity of 1-hydroxy-1-norresistomycin against human clinical pathogens

Microb Pathog. 2019 Jul:132:343-354. doi: 10.1016/j.micpath.2019.05.021. Epub 2019 May 15.

Abstract

In the present study, an attempt has been made to explore the antibiofilm activity of bioactive compound 1-hydroxy-1-norresistomycin (HNM) derived from coral mucus associated actinomycete Streptomyces variabilis. Initially, different concentration of HNM inhibited the biofilm formation of human clinical pathogens Escherichia coli, Vibrio cholerae and Staphylococcus aureus was determined using crystal-violet staining assay. The light microscopic analysis showed that HNM reduced the biofilm formation and adherence of bacterial cells on the surface of coverslip. HNM also damages the 3D architecture with reduced thickness as well as cell aggregation of biofilm forming bacteria analysed by confocal laser scanning microscopy (CLSM). In addition, HNM also demonstrated the efficiency in inhibiting theoretical adhesion by altering the surface hydrophobicity that can potentially hamper cellular adhesion and prevent biofilm formation. Furthermore, the molecular docking showed the significant interaction between HNM and key biofilm forming proteins proved an excellent antibiofilm activity of HNM. Together, these results suggest that the HNM can serve as potential antibiofilm agent in controlling the infections of E. coli, V. cholerae and S. aureus.

Keywords: 1-Hydroxy-1-norresistomycin; Biofilm architecture; Clinical pathogens; Molecular docking.

MeSH terms

  • Actinobacteria / metabolism
  • Animals
  • Anthozoa / microbiology
  • AraC Transcription Factor / drug effects
  • Bacterial Adhesion / drug effects
  • Bacterial Proteins / drug effects
  • Biofilms / drug effects*
  • Computer Simulation
  • Cysteine Endopeptidases / drug effects
  • Escherichia coli / drug effects*
  • Escherichia coli Proteins / drug effects
  • Humans
  • Hydrogen Bonding
  • Molecular Docking Simulation
  • Pyrenes / chemistry
  • Pyrenes / pharmacology*
  • Staphylococcus aureus / drug effects*
  • Streptomyces / metabolism
  • Trans-Activators / drug effects
  • Vibrio cholerae / drug effects*
  • Zebrafish

Substances

  • 1-hydroxy-1-norresistomycin
  • AphA protein, Vibrio cholerae
  • AraC Transcription Factor
  • AraC protein, E coli
  • Bacterial Proteins
  • Escherichia coli Proteins
  • Pyrenes
  • SarA protein, Staphylococcus aureus
  • Trans-Activators
  • Cysteine Endopeptidases
  • staphopain A protein, Staphylococcus aureus