Lactoferrin-binding protein (Lbp) (Lbp)

The Helicobacter pylori lactoferrin receptor, primarily identified as a 70-kDa lactoferrin-binding protein (Lbp), is an outer membrane protein essential for the bacterium's survival in the iron-limited environment of the human stomach (Dhaenens et al., 1997; Husson et al., 1993). It specifically binds to human lactoferrin to extract iron, which is a critical nutrient for bacterial growth and the expression of virulence factors like the cag Type IV Secretion System (cag T4SS) (Lu et al., 2021). By facilitating iron acquisition, the receptor supports chronic colonization and contributes to the pathogenesis of gastritis, peptic ulcers, and gastric cancer (Imoto et al., 2023). Therapeutic strategies often involve supplementing standard antibiotic regimens with bovine or recombinant human lactoferrin, which can inhibit the bacteria by sequestering iron or exerting direct antimicrobial effects (Imoto et al., 2023; Di Mario et al., 2003). This receptor is considered a potential target for vaccines and novel antimicrobial agents aimed at disrupting H. pylori's iron metabolism (Dhaenens et al., 1997). Its expression is typically upregulated under iron-restricted conditions, making it a key player in the pathogen's adaptation to the host's nutritional immunity (Lu et al., 2021).

Other names

Lactoferrin receptor70-kDa lactoferrin-binding proteinHLf receptorHuman lactoferrin-binding protein

Lactoferrin and its derivatives act as antimicrobial agents by sequestering iron (apo-lactoferrin) or by direct bactericidal action, thereby interfering with the bacterial lactoferrin receptor's ability to acquire iron and enhancing the efficacy of standard eradication therapies.