Ferrichrome receptor (FhuA) (FhuA)

The Ferrichrome receptor, primarily exemplified by the bacterial protein FhuA, is a high-affinity outer membrane transporter essential for the acquisition of iron via the fungal-type siderophore ferrichrome [4, 18]. Functioning as a TonB-dependent transporter, it facilitates the active translocation of iron-ferrichrome complexes into the periplasm, a process crucial for bacterial survival in iron-limited environments [4, 8]. In pharmaceutical research, this receptor is a primary target for 'Trojan Horse' antibiotics, where drug molecules are conjugated to siderophores to bypass the outer membrane barrier through the receptor's transport channel [2, 14]. Beyond its role in microbiology, recent studies indicate that ferrichrome molecules themselves act as tumor suppressors in colorectal and pancreatic cancers by inducing apoptosis through the activation of the p53 and DDIT3 pathways [1, 5]. Consequently, the ferrichrome transport and signaling axis represents a versatile target for both novel antimicrobial strategies and oncology therapeutics [3, 8].

Other names

Ferrichrome-iron receptorIron(III) hydroxamate receptorTonAFhuA proteinArn1pStr1Siderophore-iron receptor

Siderophore-mediated drug delivery (Trojan Horse strategy) utilizing the receptor for active transport of antibiotics across the outer membrane; Induction of apoptosis in tumor cells via p53 and DDIT3 pathway activation