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

Boradia, Vishant Mahendra, Malhotra, Himanshu, Thakkar, Janak Shrikant, Tillu, Vikas Ajit, Vuppala, Bhavana, Patil, Pravinkumar, Sheokand, Nadeep, Sharma, Prerna, Chauhan, Anoop Singh, Raje, Manoj and Raje, Chaaya Iyengar (2014) Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin. Nature Communications, 5 4730: 1-13. doi:10.1038/ncomms5730

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Author Boradia, Vishant Mahendra
Malhotra, Himanshu
Thakkar, Janak Shrikant
Tillu, Vikas Ajit
Vuppala, Bhavana
Patil, Pravinkumar
Sheokand, Nadeep
Sharma, Prerna
Chauhan, Anoop Singh
Raje, Manoj
Raje, Chaaya Iyengar
Title Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin
Formatted title
Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin
Journal name Nature Communications   Check publisher's open access policy
ISSN 2041-1723
Publication date 2014-08-28
Year available 2014
Sub-type Article (original research)
DOI 10.1038/ncomms5730
Open Access Status File (Publisher version)
Volume 5
Issue 4730
Start page 1
End page 13
Total pages 13
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
Formatted 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.
Keyword Multidisciplinary Sciences
Science & Technology - Other Topics
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Institute for Molecular Bioscience - Publications
 
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