Pseudomonas aeruginosa elastase (LasB) (LasB)

Pseudomonas aeruginosa elastase, commonly referred to as LasB or pseudolysin, is a potent extracellular zinc-metalloprotease and a primary virulence factor of the opportunistic pathogen Pseudomonas aeruginosa (UniProt P06132). It functions by degrading a broad spectrum of host proteins, including elastin, collagen, laminin, and various immune system components such as cytokines, complement factors, and immunoglobulins (PMID: 25151270). This enzymatic activity facilitates bacterial attachment, tissue penetration, and the neutralization of host immune responses, particularly in chronic infections like those found in cystic fibrosis and non-healing wounds (PMID: 21854357). LasB also contributes to the structural integrity of bacterial biofilms, making the pathogen more resistant to treatment. As an anti-virulence target, inhibiting LasB aims to disarm the bacteria rather than killing them directly, which may exert less selective pressure for the development of antibiotic resistance (PMID: 32692544). Current therapeutic strategies involve the design of small-molecule inhibitors that specifically bind the zinc-containing active site of the enzyme. These inhibitors are being explored to reduce tissue damage and enhance the efficacy of conventional antibiotics.

Other names

PseudolysinPseudomonas elastaseLasB proteaseZinc metalloendopeptidaseLasB metalloendopeptidase

Inhibition of the zinc-dependent catalytic activity of the enzyme to prevent degradation of host tissues and immune factors.