Pseudolysin (LasB) (LasB)

Pseudolysin, commonly known as Pseudomonas aeruginosa elastase or LasB, is a major extracellular zinc metalloprotease secreted by the opportunistic pathogen Pseudomonas aeruginosa (UniProt Consortium, 2023, P06022). It functions as a critical virulence factor by degrading a wide array of host proteins, including elastin, collagen, and various components of the innate and adaptive immune systems (Cathcart et al., 2011, Journal of Biological Chemistry). By cleaving cytokines, immunoglobulins, and complement proteins, LasB facilitates immune evasion and promotes tissue invasion and nutrient acquisition. The enzyme also plays a significant role in the maturation and structural integrity of biofilms, which are central to the persistence of chronic infections. In clinical settings, LasB activity is associated with the pathogenesis of cystic fibrosis, ventilator-associated pneumonia, and severe burn wound infections (Everett and Davies, 2021, Drug Discovery Today). Because LasB is essential for virulence but not for bacterial survival, it is a prime candidate for anti-virulence therapy. Such therapies aim to attenuate the pathogen's destructive potential without exerting the selective pressure that typically drives antibiotic resistance. Current drug discovery efforts focus on developing potent and selective inhibitors that target the catalytic zinc ion within the enzyme's active site (Karkare et al., 2017, Journal of Medicinal Chemistry).

Other names

Pseudomonas aeruginosa elastaseElastase BZinc metalloproteinase LasBP. aeruginosa elastaseLasB protease

Inhibition of the catalytic zinc-dependent proteolytic activity by binding to the active site zinc ion.