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Mol Microbiol. 1993 Oct;10(2):311-8.

The ferric iron-binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin.

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1
Division of Sexually Transmitted Diseases Laboratory Research, Centers for Disease Control and Prevention, Atlanta, Georgia 30333.

Abstract

The ferric iron-binding protein (Fbp) expressed by pathogenic Neisseria spp. has been proposed to play a central role in the high-affinity acquisition of iron from human transferrin. The results of this investigation provide evidence that Fbp participates in this process as a functional analogue of a Gram-negative periplasmic-binding protein component, which operates as a part of a general active transport process for the receptor-mediated, high-affinity transport of iron from human transferrin. Known properties of Fbp are correlated with those of other well-characterized periplasmic-binding proteins, including structural features and the reversible binding of ligand. Predictive of a periplasmic-binding protein, which functions in the high-affinity acquisition of iron, is that Fbp is a transient participant in the process of iron acquisition from human transferrin. Evidence for this is demonstrated by results of pulse-chase experiments. Taken together, the data described here and elsewhere suggest that pathogenic Neisseria spp. use a periplasmic-binding protein-mediated active transport mechanism for the acquisition of iron from human transferrin.

[Indexed for MEDLINE]

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