By I. A. Cardos, Galal Yahya,…..and Simona Cavalu
Viscum album L. (mistletoe) is a hemiparasitic plant known for its wide range of bioactive compounds, including phenolics, flavonoids, and lectins, which contribute to its diverse pharmacological properties. In the present study, we focused on identifying and quantifying the phenolic compounds present in V. album L. leaf extracts and evaluating their potential as inhibitors of key Helicobacter pylori enzymes through both in silico and in vitro approaches. Using molecular docking, we assessed the binding affinity and stability of selected mistletoe’s phytochemicals with specific H. pylori targets, including peptide deformylase, shikimate pathway enzymes, and urease. Additionally, to complement the computational findings, we conducted an in vitro assay to evaluate the anti-urease activity of the crude V. album L. extract against the urease activity of Proteus mirabilis. The extract demonstrated significant inhibitory activity, indicating its potential as a natural urease inhibitor at a concentration of 0.0125 mg/mL, leading to a marked reduction in urease-mediated crystal formation in artificial urine. Furthermore, the extract exhibited broad-spectrum anti virulence effects by suppressing biofilm formation in Staphylococcus aureus and Escherichia coli, and inhibiting protease activity in S. aureus and Pseudomonas aeruginosa. Together, these findings highlight V. album phenolics as promising dual-action natural inhibitors that not only target essential metabolic enzymes but also attenuate virulence factors critical for pathogenesis. This integrated strategy positions V. album as a strong candidate for the development of plant-based therapeutics against multidrug-resistant pathogens with possible applications in the treatment of H. pylori-related gastrointestinal disorders. Copyright Simona Cavalu et al.
Molecular docking revealed strong binding affinities of caffeic acid and quercetin—major phenolic and flavonoid components of the extract—against essential H. pylori enzymes, including peptide deformylase and key enzymes of the shikimate pathway (shikimate kinase and chorismate synthase). These targets are critical for bacterial survival and are absent in humans, enhancing the therapeutic selectivity of the proposed inhibitors. Copyright Simona Cavalu et al.
Moreover, V. album exhibited extended anti virulence activity across pathogens, disrupting biofilm formation in S. aureus and E. coli, and suppressing protease activity in S. aureus and P. aeruginosa. These combined results establish V. album phenolics as dual-action inhibitors that both target essential bacterial enzymes and attenuate key virulence traits, offering a promising natural therapeutic approach against multidrug-resistant bacteria. Copyright Simona Cavalu et al.
Full text at | https://doi.org/10.3389/fcimb.2025.1690969
