Lactoferrin receptors and bacterial surface proteins

Lactoferrin receptors and bacterial surface proteins encompass a group of distinct molecules that interact with lactoferrin, a multifunctional iron-binding glycoprotein [1]. In humans, the primary receptors include Intelectin-1 (ITLN1), which mediates intestinal iron absorption and immune signaling, and the Low-density lipoprotein receptor-related protein 1 (LRP1/CD91), which facilitates endocytosis and signaling in various tissues [2, 3]. These human receptors play crucial roles in iron homeostasis, immune system modulation, and anti-inflammatory responses [1]. Conversely, many pathogenic bacteria, particularly those in the Neisseriaceae family, express specialized surface proteins such as Lactoferrin-binding protein A (LbpA) and B (LbpB) to hijack host lactoferrin for iron acquisition, which is essential for their survival and pathogenesis [4, 5]. Therapeutically, lactoferrin itself is used as a drug (e.g., Talactoferrin alfa) to target these pathways for treating infections, neonatal sepsis, and certain cancers [6]. Bacterial Lbps are also significant targets for vaccine development, aiming to block iron uptake and neutralize bacterial virulence [5].

Other names

Intelectin-1ITLN1Low-density lipoprotein receptor-related protein 1LRP1CD91Lactoferrin-binding protein A (LbpA)Lactoferrin-binding protein B (LbpB)HLFRLactoferrin receptor

Ligand binding to human receptors (ITLN1, LRP1) triggers iron uptake and immunomodulatory signaling; binding to bacterial surface proteins (LbpA/B) facilitates iron extraction and transport into the bacterial cell.