LAUSR

AIMS Staphylococcus aureus has emerged as a serious threat to food safety owing to biofilm formation. The study aimed to examine antibiofilm mechanism of a novel milk-derived antimicrobial peptide BCp12 against it. METHODS AND RESULTS Anti-biofilm activity of BCp12 was studied by crystal violet staining, MTT assay, motility, SEM and CLSM. TMT proteome, real-time PCR, and molecular docking in silico were conducted to evaluate the mechanism of BCp12 against S. aureus biofilm. The results showed that BCp12 had significant anti-biofilm activity at 1×MIC and sub-MIC. BCp12 induced the dispersion of structure of S. aureus biofilm BCp12 inhibited the movement of S. aureus. A total of 703 proteins were down-regulated and 334 proteins were up-regulated after BCp12 treatment. The proteins (agrA, agrB, agrC, and psmβ) of the QS systems were down-regulated. Additionally, the expression of the agr-related genes, agrA, agrB, agrC, and psmβ were down-regulated. BCp12 was bound to the receptor proteins agrA and agrC through hydrogen bonds and π-π bonds. CONCLUSIONS The results indicated the antibiofilm activity of BCp12 and it inhibiting biofilm formation by interfering agr QS system. SIGNIFICANCE AND IMPACT OF STUDY BCp12 has the potential to be a novel anti-biofilm agent against S. aureus biofilm and used in the food industry.