TY - JOUR
T1 - Take five - Type VII secretion systems of Mycobacteria
AU - Houben, E.N.G.
AU - Korotkov, K.V.
AU - Bitter, W.
N1 - Houben, Edith N G Korotkov, Konstantin V Bitter, Wilbert Journal article Biochim Biophys Acta. 2013 Nov 18. pii: S0167-4889(13)00382-0. doi: 10.1016/j.bbamcr.2013.11.003.
PY - 2014
Y1 - 2014
N2 - 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. © 2013 Elsevier B.V.
AB - 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. © 2013 Elsevier B.V.
U2 - 10.1016/j.bbamcr.2013.11.003
DO - 10.1016/j.bbamcr.2013.11.003
M3 - Article
SN - 0167-4889
VL - 1843
SP - 1707
EP - 1716
JO - Biochimica et Biophysica Acta. Molecular Cell Research
JF - Biochimica et Biophysica Acta. Molecular Cell Research
IS - 8
ER -
