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C478 functional and structural studies were performed, focusing on SmeDEF, the most relevant antibioticand triclosan-removing multidrug efflux pump of S. maltophilia. Expression of smeDEF is regulated by the repressor SmeT. Triclosan released SmeT from its operator and induces the expression of smeDEF, thus reducing the susceptibility of S. maltophilia to antibiotics in the presence of the biocide. The structure of SmeT bound to triclosan is described. Two molecules of triclosan were found to bind to one subunit of the SmeT homodimer. The binding of the biocide stabilizes the N terminal domain of both subunits in a conformation unable to bind DNA. This complex structure is the first structural evidence of the ability of triclosan to act as an effector via its binding to a transcriptional regulator (SmeT). Given that SmeT mediate the susceptibility of Stenotrophomonas maltophilia to antibiotics by repressing SmeDEF expression, the present results provide information that aids our understanding of the molecular basis of biocide-induced antibiotic resistance.

Muropeptide-driven revival from dormancy in bacterial pathogens: a structural perspective