Teichoic acid poly(glycerol phosphate) polymerase (TagF) (TagF)

Teichoic acid poly(glycerol phosphate) polymerase, commonly known as TagF, is an essential bacterial enzyme responsible for the polymerization of the main chain of wall teichoic acids (WTAs) in many Gram-positive bacteria, including Staphylococcus aureus and Bacillus subtilis (UniProt P13485). It catalyzes the sequential transfer of glycerol phosphate units from CDP-glycerol to a membrane-anchored linkage unit, creating anionic polymers that are critical for cell division, morphology, and virulence (Fitzgerald & Foster, 2000, PubMed 10648531). Because WTAs are indispensable for the viability of many pathogenic species and the enzyme has no human homolog, TagF has emerged as a high-priority therapeutic target for developing novel antibacterial agents to combat drug-resistant infections (Sewell et al., 2009, PubMed 19411246). Structural studies have revealed that TagF is a monotopic membrane protein, allowing its active site to access lipid-bound substrates within the bacterial bilayer (Lovering et al., 2010, PubMed 20188669). While no clinical drugs targeting TagF are currently FDA-approved, experimental small molecule inhibitors and synthetic substrate analogs have demonstrated potent anti-infective potential in preclinical high-throughput screening efforts.

Other names

CDP-glycerol:poly(glycerophosphate) glycerophosphotransferaseCGPTaseMajor teichoic acid biosynthesis protein FPoly(glycerol phosphate) polymeraseTeichoic-acid synthase

Inhibition of teichoic acid polymerase activity to disrupt the assembly of wall teichoic acids and compromise bacterial cell wall integrity