Antibiofilm Action of ZnO, SnO2 and CeO2 Nanoparticles Towards Grampositive Biofilm Forming Pathogenic Bacteria

Abstract

Background: The ability to form biofilm and produce several virulence factors has caused numerous human pathogens to become tremendously resistant towards traditional antibiotic treatments, thus, new alternative strategies are urgently in demand. One of the strategies that have recently been developed involves the application of metallic Nanoparticles (NPs). Up to the present, promising results in terms of antimicrobial and antibiofilm activities have been observed in a wide range of metal NPs. Methods: The present study has selected three metal oxides such as ZnO, SnO2 and CeO2 NPs to comparatively investigate their antibiofilm and antibacterial properties against two Gram-positive human pathogens, which are Listeria monocytogenes and Staphylococcus aureus. Result: The anti-biofilm activities of ZnO, SnO2 and CeO2 NPs against S. aureus and L. monocytogenes were assayed by crystal violet staining and confirmed by microscopic visualization using SEM. The synthesis of amyloid protein by S. aureus and exopolysaccharide by L. monocytogenes in the presence of ZnO, SnO2 and CeO2 NPs was evaluated by Congo red assay. Conclusion: Overall, these results indicated that ZnO, SnO2 and CeO2 NPs can be considered as potential agents for treating the infections caused by L. monocytogenes and S. aureus, especially those associated with biofilm formation. Based on the present study, further studies are required to understand their mechanisms at both phenotypic and molecular levels, as well as their in vivo cytotoxicity, thereby enabling the applications of these metal oxide NPs in biomedical fields and food industry. Discussion: Results have shown that ZnO, SnO2 and CeO2 NPs effectively inhibited biofilm formation of both L. monocytogenes and S. aureus. The microscopic analysis also confirmed the antibiofilm activity of these NPs. It was also found that only ZnO NPs inhibited cell growth as well as the production of amyloid protein in S. aureus.