TY - JOUR
T1 - Composition of the type VII secretion system membrane complex.
AU - Houben, E.N.G.
AU - Bestebroer, J.
AU - Ummels, R.
AU - Wilson, L.
AU - Piersma, S.R.
AU - Jimenez, C.R.
AU - Ottenhoff, T.H.M.
AU - Luirink, S.
AU - Bitter, W.
PY - 2012
Y1 - 2012
N2 - Pathogenic mycobacteria require type VII secretion (T7S) systems to transport virulence factors across their complex cell envelope. These bacteria have up to five of these systems, termed ESX-1 to ESX-5. Here, we show that ESX-5 of Mycobacterium tuberculosis mediates the secretion of EsxN, PPE and PE_PGRS proteins, indicating that ESX-5 is a major secretion pathway in this important pathogen. Using the ESX-5 system of Mycobacterium marinum and Mycobacterium bovis BCG as a model, we have purified and analysed the T7S membrane complex under native conditions. blue native-PAGE and immunoprecipitation experiments showed that the ESX-5 membrane complex of both species has a size of ~1500kDa and is composed of four conserved membrane proteins, i.e. EccB
AB - Pathogenic mycobacteria require type VII secretion (T7S) systems to transport virulence factors across their complex cell envelope. These bacteria have up to five of these systems, termed ESX-1 to ESX-5. Here, we show that ESX-5 of Mycobacterium tuberculosis mediates the secretion of EsxN, PPE and PE_PGRS proteins, indicating that ESX-5 is a major secretion pathway in this important pathogen. Using the ESX-5 system of Mycobacterium marinum and Mycobacterium bovis BCG as a model, we have purified and analysed the T7S membrane complex under native conditions. blue native-PAGE and immunoprecipitation experiments showed that the ESX-5 membrane complex of both species has a size of ~1500kDa and is composed of four conserved membrane proteins, i.e. EccB
U2 - https://doi.org/10.1111/j.1365-2958.2012.08206.x
DO - https://doi.org/10.1111/j.1365-2958.2012.08206.x
M3 - Article
C2 - 22925462
SN - 0950-382X
VL - 86
SP - 472
EP - 484
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 2
ER -
