title: Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin.
creator: Boradia, Vishant Mahendra
creator: Malhotra, Himanshu
creator: Thakkar, Janak Shrikant
creator: Tillu, Vikas Ajit
creator: Vuppala, Bhavana
creator: Patil, Pravinkumar
creator: Sheokand, Navdeep
creator: Sharma, Prerna
creator: Chauhan, Anoop Singh
creator: Raje, Manoj
creator: Raje, Chaaya Iyengar
subject: QR Microbiology
description: 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.
publisher: Nature Pub. Group
date: 2014
type: Article
type: PeerReviewed
relation: http://www.nature.com/ncomms/2014/140828/ncomms5730/full/ncomms5730.html
identifier:   Boradia, Vishant Mahendra and Malhotra, Himanshu and Thakkar, Janak Shrikant and Tillu, Vikas Ajit and Vuppala, Bhavana and Patil, Pravinkumar and Sheokand, Navdeep and Sharma, Prerna and Chauhan, Anoop Singh and Raje, Manoj and Raje, Chaaya Iyengar  (2014) Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin.  Nature communications, 5.  p. 4730.  ISSN 2041-1723     
relation: http://crdd.osdd.net/open/1530/