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Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin

Author

Listed:
  • Vishant Mahendra Boradia

    (National Institute of Pharmaceutical Education and Research (NIPER))

  • Himanshu Malhotra

    (Institute of Microbial Technology (IMTECH))

  • Janak Shrikant Thakkar

    (National Institute of Pharmaceutical Education and Research (NIPER))

  • Vikas Ajit Tillu

    (Institute of Microbial Technology (IMTECH)
    Present addresses: Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia)

  • Bhavana Vuppala

    (National Institute of Pharmaceutical Education and Research (NIPER))

  • Pravinkumar Patil

    (National Institute of Pharmaceutical Education and Research (NIPER))

  • Navdeep Sheokand

    (Institute of Microbial Technology (IMTECH))

  • Prerna Sharma

    (Institute of Microbial Technology (IMTECH)
    Present addresses: Indian Institute for Science Education and Research (IISER) Mohali, Knowledge city, Sector 81, SAS Nagar, Manauli, Punjab 140306, India)

  • Anoop Singh Chauhan

    (Institute of Microbial Technology (IMTECH))

  • Manoj Raje

    (Institute of Microbial Technology (IMTECH))

  • Chaaya Iyengar Raje

    (National Institute of Pharmaceutical Education and Research (NIPER))

Abstract

Mycobacterium tuberculosis (M.tb), which requires iron for survival, acquires this element by synthesizing iron-binding molecules known as siderophores and by recruiting a host iron-transport protein, transferrin, to the phagosome. The siderophores extract iron from transferrin and transport it into the bacterium. Here we describe an additional mechanism for iron acquisition, consisting of an M.tb protein that drives transport of human holo-transferrin into M.tb cells. The pathogenic strain M.tb H37Rv expresses several proteins that can bind human holo-transferrin. One of these proteins is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH, Rv1436), which is present on the surface of M.tb and its relative Mycobacterium smegmatis. Overexpression of GAPDH results in increased transferrin binding to M.tb cells and iron uptake. Human transferrin is internalized across the mycobacterial cell wall in a GAPDH-dependent manner within infected macrophages.

Suggested Citation

  • Vishant Mahendra Boradia & Himanshu Malhotra & Janak Shrikant Thakkar & Vikas Ajit Tillu & Bhavana Vuppala & Pravinkumar Patil & Navdeep Sheokand & Prerna Sharma & Anoop Singh Chauhan & Manoj Raje & C, 2014. "Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin," Nature Communications, Nature, vol. 5(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5730
    DOI: 10.1038/ncomms5730
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