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The ferric iron‐binding protein of pathogenic

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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.
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Document Type: Research Article

Affiliations: 1: Division of Sexually Transmitted Diseases Laboratory Research, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333, USA. 2: Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pennsylvania 15261, USA.

Publication date: October 1, 1993

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