Fucose-binding lectin LecB (LecB)

LecB (also known as PA-IIL) is a tetrameric, calcium-dependent fucose-binding lectin produced by the opportunistic pathogen Pseudomonas aeruginosa [1, 10]. It serves as a critical virulence factor by mediating bacterial adhesion to host tissues and stabilizing the biofilm matrix through its interaction with the exopolysaccharide Psl [2, 6]. Beyond its structural role, LecB modulates host cell signaling, triggering the internalization of integrins, the degradation of growth factor receptors like IGF-1R, and the inhibition of epithelial wound healing and ciliary beating [4, 8, 15]. Because of its essential role in establishing and maintaining chronic infections, such as those in cystic fibrosis and ventilator-associated pneumonia, LecB is a primary target for anti-virulence drug development [7, 9]. Therapeutic approaches involve the use of small-molecule glycomimetics, C-glycosidic inhibitors, and antibiotic-carbohydrate conjugates designed to competitively block its binding sites, thereby disrupting biofilm integrity and enhancing the efficacy of co-administered antibiotics [5, 11, 12]. Research also explores the use of LecB-targeted prodrugs to deliver antibiotics specifically to the site of infection, thereby reducing systemic toxicity [11]. Overall, LecB represents a promising target for overcoming antimicrobial resistance in P. aeruginosa by neutralizing its ability to form protective biofilms and evade host defenses [1, 7].

Other names

PA-IILPA-IILecB lectinPseudomonas aeruginosa lectin BFucose-binding lectin PA-IIL

Competitive inhibition of carbohydrate binding sites to prevent bacterial adhesion and biofilm stabilization [7, 13]