Biochemical evidence for a conserved interaction between bacterial transferrin binding protein A and transferrin binding protein B.

@article{Fuller1998BiochemicalEF,
  title={Biochemical evidence for a conserved interaction between bacterial transferrin binding protein A and transferrin binding protein B.},
  author={Cynthia A. Fuller and Rong-hua Yu and Stephen A Irwin and Anthony B Schryvers},
  journal={Microbial pathogenesis},
  year={1998},
  volume={24 2},
  pages={75-87}
}
As an adaptation to the iron-restricted environment of the host, some bacterial pathogens possess iron acquisition pathways mediated by surface receptors that specifically bind transferrin from the host. The receptor is composed of two receptor proteins, TbpA and TbpB, which are both capable of binding to transferrin. Previous studies have demonstrated that affinity isolation of TbpB from Neisseria meningitidis or Haemophilus influenzae with immobilized human transferrin required the homologous… CONTINUE READING

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