Fucose-binding lectin (LecB) (LecB)

LecB, also known as PA-IIL, is a fucose-binding lectin produced by the opportunistic pathogen Pseudomonas aeruginosa [2, 7]. It is a tetrameric protein that serves as a critical virulence factor by mediating bacterial adhesion to host tissues and facilitating the formation of biofilms [3, 6]. LecB binds to fucose-containing glycoconjugates on host cell surfaces, leading to the internalization of receptors such as integrins, which can impair wound healing and host immune responses [4, 9]. Within the bacterium, LecB interacts with the outer membrane protein OprF to ensure its proper surface localization [3]. Due to its essential role in chronic infections, particularly in the respiratory tract of cystic fibrosis patients, LecB is a prominent target for anti-virulence therapies [2, 16]. Experimental treatments involve the use of glycomimetics and fucose derivatives that competitively inhibit LecB binding, thereby reducing bacterial colonization and increasing the susceptibility of biofilms to antibiotics [2, 3, 16].

Other names

PA-IILFucose-binding lectin PA-IILPA3361

Competitive inhibition of carbohydrate-binding sites to prevent bacterial adhesion and biofilm formation