Mycobacteria use type VII secretion (T7S) systems to secrete proteins across their complex cell envelope. Pathogenic mycobacteria, such as the notorious pathogen Mycobacterium tuberculosis, have up to five of these secretion systems, named ESX-1 to ESX-5. At least three of these secretion systems are essential for mycobacterial virulence and/or viability. Elucidating T7S is therefore essential to understand the success of M. tuberculosis and other pathogenic mycobacteria as pathogens, and could be instrumental to identify novel targets for drug- and vaccine-development. Recently, significant progress has been achieved in the identification of T7S substrates and a general secretion motif. In addition, a start has been made with unraveling the mechanism of secretion and the structural analysis of the different subunits. This review summarizes these recent findings, which are incorporated in a working model of this complex machinery. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.
|Number of pages||10|
|Journal||Biochimica et Biophysica Acta - Molecular Cell Research|
|State||Published - Aug 2014|
Bibliographical noteFunding Information:
Our work is supported by a grant ( P20GM103486 ) from the National Institute of General Medical Sciences (to KVK) and by a VIDI grant from the Netherlands Organization for Scientific Research (NWO) (to ENGH).
- Protein secretion
- Secretion signal
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology