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Bromamphenicol (BRM) is a derivative of the antibiotic chloramphenicol. It functions as an inhibitor of Dr haemagglutinin, a bacterial adhesin expressed on the surface of uropathogenic and diffusely adherent strains of Escherichia coli. The major adhesin subunit (DraE/AfaE) of Dr haemagglutinin mediates bacterial attachment to host cells by recognizing the complement regulator decay-accelerating factor (DAF), members of the carcinoembryonic antigen (CEA) family, and type IV collagen. Bromamphenicol binds to the adhesin subunit, thereby inhibiting these receptor interactions. Structural studies indicate that the binding pocket of DraE can accommodate bulkier substituents on the N-acyl group of chloramphenicol derivatives, suggesting that modifications to the 3-hydroxyl group could lead to potent Dr haemagglutinin inhibitors with reduced toxic side effects compared to the bacteriostatic activity of chloramphenicol.
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