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. 1988 Dec;56(12):3132–3138. doi: 10.1128/iai.56.12.3132-3138.1988

Loss of transferrin receptor activity in Neisseria meningitidis correlates with inability to use transferrin as an iron source.

J Tsai 1, D W Dyer 1, P F Sparling 1
PMCID: PMC259713  PMID: 3141281

Abstract

Although Neisseria meningitidis does not produce siderophores, it is able to obtain iron from human transferrin. We observed saturable specific binding of 125I-labeled human transferrin to meningococci. Human lactoferrin and mouse transferrin did not compete with human transferrin for binding, whereas human apotransferrin and 100% iron-saturated transferrin competed equally well. Meningococci thus have a specific receptor for human transferrin. Scatchard analysis yielded a relatively low Kd of 0.7 microM and an apparent copy number of 2,900 receptors per CFU. Receptor activity was iron-regulated. A meningococcal transformant specifically unable to utilize transferrin as an iron source had decreased transferrin receptor activity. These data are consistent with the hypothesis that receptor-mediated binding of transferrin is a rate-limiting step in meningococcal iron uptake from transferrin.

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Selected References

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