CDP-glycerol glycerophosphotransferase (TagF) (TagF)

CDP-glycerol glycerophosphotransferase, commonly known as TagF, is an essential membrane-associated enzyme involved in the biosynthesis of wall teichoic acids (WTAs) in Gram-positive bacteria such as Staphylococcus epidermidis and Bacillus subtilis [1, 4]. It catalyzes the polymerization of the teichoic acid main chain by sequentially transferring glycerol-phosphate units from CDP-glycerol to a membrane-bound linkage unit [2, 6]. WTAs are anionic polymers critical for maintaining bacterial cell wall integrity, regulating ion concentrations, and facilitating biofilm formation and host-pathogen interactions [7, 14]. Because WTAs are absent in human cells and essential for the viability and virulence of many pathogens, TagF is considered an attractive target for the development of novel antibacterial therapies [4, 10]. Inhibition of this enzyme disrupts cell wall assembly, significantly attenuating bacterial virulence and sensitizing pathogens to existing antibiotics like beta-lactams [9, 11]. While several natural and synthetic compounds have shown potential as TagF inhibitors in research settings, no drugs targeting this enzyme are currently approved for clinical use [3, 16].

Other names

Poly(glycerol-phosphate) polymeraseTeichoic-acid synthaseCDP-glycerol:poly(glycerophosphate) glycerophosphotransferaseCytidine diphosphoglycerol glycerophosphotransferaseGlycerophosphate synthetaseTeichoic acid glycerol transferaseCGPTase

Inhibition of teichoic acid chain elongation, leading to defective cell wall assembly, increased susceptibility to osmotic stress, and sensitization of the bacterium to host immune factors and beta-lactam antibiotics.