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Related Experiment Videos

Energy-dependent changes in the gonococcal transferrin receptor

C N Cornelissen1, J E Anderson, P F Sparling

  • 1Department of Medicine, School of Medicine, University of North Carolina at Chapel Hill, USA. ccornelissen@gems.vcu.edu

Molecular Microbiology
|January 31, 1998
PubMed
Summary

Pathogenic Neisseria utilize host iron via transferrin-binding proteins (TbpA and TbpB). Energization of TbpA by the Ton system is crucial for iron uptake and TbpB function.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Pathogenic Neisseria species efficiently acquire iron from host proteins like transferrin.
  • Iron acquisition is essential for bacterial survival and virulence.
  • Transferrin iron uptake involves energy-dependent, receptor-mediated mechanisms.

Purpose of the Study:

  • To investigate the role of the TonB box in gonococcal transferrin-binding protein A (TbpA) function.
  • To elucidate the interaction between TbpA, TbpB, and the Ton system in iron utilization.
  • To understand the energy transduction mechanism for transferrin uptake.

Main Methods:

  • Construction and analysis of a TonB box mutant of gonococcal TbpA.
  • Assessment of protein binding and protease accessibility.

Related Experiment Videos

  • Evaluation of transferrin diffusion rates in de-energized mutants.

    • Main Results:

    • TonB box mutations in TbpA mimicked the effects of Ton system mutations.
    • TbpA energization influenced TbpB protease accessibility, suggesting protein-protein interaction.
    • De-energized mutants showed reduced transferrin diffusion, indicating impaired ligand release.

    Conclusions:

    • The TonB box of TbpA is essential for energy transduction in transferrin iron uptake.
    • TbpA and TbpB interact, and their function is regulated by the Ton system.
    • Receptor energization is critical for efficient transferrin binding and iron acquisition by Neisseria.