Lgt is indispensable in Gram-negative bacteria for lipoprotein biogenesis:
Mechanism: Transfers diacylglyceryl groups to prolipoproteins, forming thioether bonds critical for membrane anchoring .
Essentiality: Depletion of Lgt disrupts outer membrane integrity, increasing susceptibility to antibiotics and serum killing in pathogens like E. coli and Acinetobacter baumannii .
Pathogenicity Link: In Campylobacter species, lipoproteins contribute to virulence factors such as host-cell adhesion and immune evasion .
Inhibitors targeting Lgt (e.g., compounds G9066, G2823) show potent activity (IC<sub>50</sub> values ≤0.93 μM) in biochemical assays, disrupting lipoprotein maturation .
Unlike downstream lipoprotein pathway inhibitors, Lgt-targeted compounds remain effective even in lpp-deficient strains, reducing resistance risks .
Cusabio. (n.d.). Recombinant Campylobacter curvus Prolipoprotein diacylglyceryl transferase (lgt). Retrieved from Cusabio
PMC. (2020). Novel inhibitors of E. coli lipoprotein diacylglyceryl transferase. PMC Article
PMC. (2012). Comparative characterization of virulence gene clusters in Campylobacter. PMC Article
MyBioSource. (n.d.). Recombinant Prolipoprotein diacylglyceryl transferase. Retrieved from MyBioSource
PMC. (2022). A defect in lipoprotein modification by Lgt leads to abnormal morphology. PMC Article
KEGG: ccv:CCV52592_2203
STRING: 360105.CCV52592_2203