Chirality of tyrosine controls biofilm formation via the regulation of bacterial adhesion

Biofilm is the main cause of membrane biofouling and microbial corrosion. One of the most efficient strategies for biofilm reduction is inhibiting bacteria adhesion. In this study, we selected D-tyrosine to inhibit the adhesion of Escherichia coli, and the molecular response and metabolic pathways of E. coli were explored with tran-scriptome analysis. D-tyrosine could obviously inhibit the bacterial adhesion via lowering the adhesion force. The number of extracellular proteins decreased by 45% in the presence of D-tyrosine, leading to less hydro-phobicity and autonomous aggregation of cells. Furthermore, transcriptome analysis showed that the inhibitory ability of D-tyrosine to the adhesion of E. coli decreased with time. At the initial stage, D-tyrosine could regulate tryptophan, curli, peptidoglycan, and adhesion-like protein synthesis, leading to less extracellular protein and lower cell hydrophobicity, and thus reduce cell aggregation and surface adhesion. This study provides a better understanding for the roles of D-amino acids in bacterial adhesion and develops a new strategy for biofilm reduction to mitigate membrane biofouling and microbial corrosion.

Automated summary

Biofilm is the main cause of membrane biofouling and microbial corrosion. Inhibiting bacteria adhesion is an efficient strategy for biofilm reduction. This study explores the molecular response and metabolic pathways of Escherichia coli when D-tyrosine is used to inhibit bacterial adhesion. D-tyrosine can significantly inhibit bacterial adhesion by reducing the adhesion force and extracellular protein production, leading to decreased cell hydrophobicity and autonomous cell aggregation.