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Bacterial rhamnosyltransferase is an enzyme (glycosyltransferase) responsible for transferring L-rhamnose from nucleotide sugar donors (primarily dTDP-L-rhamnose) to acceptor molecules, thereby incorporating rhamnose into bacterial glycans, such as O-antigen polysaccharides and key cell wall linkers.[2][3][4][6] This function is critical for the structural integrity of the bacterial envelope, virulence, and in some species (e.g., Mycobacterium tuberculosis), essential for viability. There are several rhamnosyltransferases in bacteria, with the best characterized including WbbL (involved in O-antigen and mycobacterial cell wall synthesis) and EarP (responsible for post-translational rhamnosylation of elongation factor P, regulating translation and pathogenicity in Pseudomonas aeruginosa).[1][2][4] These enzymes are absent in mammalian cells and represent promising antibiotic or antivirulence targets, as their inhibition can disrupt key bacterial survival structures without directly affecting mammalian pathways.[2][3][6]
Inhibition of rhamnose transfer to glycoconjugates blocks biosynthesis or modification of bacterial cell envelope components, impairing cell wall integrity and virulence[2][3]
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