Lipoprotein signal peptidase II (LspA) (LspA)

Lipoprotein signal peptidase II (LspA) is an essential bacterial enzyme and a member of the aspartyl protease family [3, 5]. It plays a critical role in the post-translational modification of lipoproteins by cleaving the signal peptide from prolipoproteins after they have been lipidated by diacylglyceryl transferase (Lgt) [7, 8]. This process is vital for the maturation and localization of lipoproteins to the bacterial cell envelope, where they perform essential functions in nutrient acquisition, cell wall synthesis, and virulence [4, 10]. Because LspA is essential for the viability of many Gram-negative pathogens and has no known human homologs, it is considered a highly attractive target for the development of novel antibiotics [1, 2, 5]. Natural inhibitors like globomycin and myxovirescin have demonstrated potent antibacterial activity by binding to the LspA active site, though their clinical utility has been limited by poor pharmacokinetic properties [1, 7]. Recent research focuses on developing stable synthetic analogues to combat multi-drug resistant infections [2, 3].

Other names

Signal peptidase IISPase IIProlipoprotein signal peptidaseLsp

Inhibition of lipoprotein signal peptidase II activity, preventing the cleavage of signal peptides from prolipoproteins and leading to bacterial cell death [1, 2, 7].