Lactoferrin-binding protein B (LbpB) (LbpB)

Lactoferrin-binding protein B (LbpB) is a surface-exposed lipoprotein found in several pathogenic Gram-negative bacteria, including Neisseria meningitidis and Neisseria gonorrhoeae (Morgenthau et al., 2013). It functions as part of a bipartite receptor system with LbpA to capture iron from human lactoferrin, a crucial nutrient for bacterial survival and pathogenesis within the host (Brooks et al., 2014). Beyond iron acquisition, LbpB has been shown to protect bacteria from host cationic antimicrobial peptides through its highly negatively charged C-terminal regions (Ostan et al., 2017). This dual functionality makes it a critical virulence factor for bacteria colonizing mucosal surfaces where lactoferrin and antimicrobial peptides are prevalent. Due to its essential role in nutrient acquisition and its accessibility on the bacterial surface, LbpB is a primary candidate for vaccine development and a potential target for novel antimicrobial therapies (Schryvers & St. Michael, 1999). Experimental studies have explored using LbpB as a component in multicomponent vaccines to provide broader protection against meningococcal and gonococcal infections. However, its high degree of sequence diversity among different bacterial strains presents a significant challenge for broad-spectrum targeting (Beddek & Schryvers, 2010). Therapeutic strategies targeting LbpB aim to either block iron uptake or sensitize the bacteria to the host's innate immune defenses.

Other names

Lactoferrin receptor protein BLactoferrin-binding protein 2Lbp2Iron-regulated protein

Inhibition of iron acquisition from host lactoferrin and neutralization of protection against host antimicrobial peptides to reduce bacterial fitness and survival.