FbpA — A bacterial transferrin with more to offer

• Published in: Biochimica et biophysica acta Vol. 1820; no. 3; pp. 379 - 392
• Main Authors: Parker Siburt, Claire J., Mietzner, Timothy A., Crumbliss, Alvin L.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2012
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Bacterial transferrin; Bacterial Transferrin Receptor Complex - chemistry; Bacterial Transferrin Receptor Complex - metabolism; binding proteins; cytosol; Ferric binding protein; Gram-negative bacteria; Haemophilus influenzae - metabolism; humans; Ion Transport; iron; Iron - metabolism; Iron transport; mechanism of action; Models, Molecular; Neisseria gonorrhoeae; Neisseria gonorrhoeae - metabolism; Neisseria meningitidis - metabolism; Periplasmic binding protein; Periplasmic Binding Proteins - chemistry; Periplasmic Binding Proteins - metabolism; Protein Structure, Tertiary; Siderophores - metabolism; transferrin; Transferrins - chemistry; Transferrins - metabolism; virulence; TfR; ABC; hLf; LFER; Periplasmic binding protein; TbpB; TonB; FbpA; FeL; Tf; Fbp; Lf; PBP; SBP; SUPREX; Bacterial transferrin; Ferric binding protein; Iron transport; NTBI; FbpB/C; FhuD; Neisseria gonorrhoeae; OMR; TbpA; hTf
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2011.09.001

Gram negative bacteria require iron for growth and virulence. It has been shown that certain pathogenic bacteria such as Neisseria gonorrhoeae possess a periplasmic protein called ferric binding protein (FbpA), which is a node in the transport of iron from the cell exterior to the cytosol. The relevant literature is reviewed which establishes the molecular mechanism of FbpA mediated iron transport across the periplasm to the inner membrane. Here we establish that FbpA may be considered a bacterial transferrin on structural and functional grounds. Data are presented which suggest a continuum whereby FbpA may be considered as a naked iron carrier, as well as a Fe–chelate carrier, and finally a member of the larger family of periplasmic binding proteins. An investigation of the molecular mechanisms of action of FbpA as a member of the transferrin super family enhances our understanding of bacterial mechanisms for acquisition of the essential nutrient iron, as well as the modes of action of human transferrin, and may provide approaches to the control of pathogenic diseases. This article is part of a Special Issue entitled Transferrins: Molecular mechanisms of iron transport and disorders. ► FbpA may be considered a structural and functional bacterial transferrin. ► The mechanism of FbpA mediated iron transport across the periplasm is described. ► FbpA is a naked iron carrier, a Fe-chel carrier, and a periplasmic binding protein. ► Studies reviewed here enhance understanding of human transferrin mechanisms. ► Studies reviewed here may provide approaches to the control of pathogenic diseases.