Ferric ion binding protein A (FbpA)

Ferric ion binding protein is a component of bacterial iron acquisition pathways, notably in pathogens such as Pasteurella, Neisseria, and Haemophilus. It resides in the periplasm and captures iron from host sources, presenting it to an ATP-binding cassette transporter for internalization. Structurally, FbpA consists of two globular domains connected by β-strands that act as a hinge, forming a binding cleft that tightly coordinates a single Fe^3+^ ion with the help of specific amino acid ligands and an anion. Its role in microbial virulence, by facilitating efficient iron uptake, makes FbpA a potential antibacterial target, and experimental studies have explored inhibitors that block its function. No FbpA-targeting drugs are currently approved. FbpA homologs are regarded as functional equivalents of transferrin for bacteria[3][4][1].

Other names

Ferric binding proteinFbpABacterial transferrinPeriplasmic ferric ion-binding proteinIron-binding protein A

Competitive inhibition or blocking of iron binding to FbpA or disruption of associated transport systems limits iron uptake, inhibiting bacterial growth and virulence potential