TY - JOUR
T1 - PPE and PE-PGRS proteins of Mycobacterium marinum are transported via the type VII secretion system ESX-5
AU - Abdallah, Abdallah M.
AU - Verboom, Theo
AU - Weerdenburg, Eveline M.
AU - Gey Van Pittius, Nicolaas C.
AU - Mahasha, Phetole W.
AU - Jiménez, Connie
AU - Parra, Marcela
AU - Cadieux, Nathalie
AU - Brennan, Michael J.
AU - Appelmelk, Ben J.
AU - Bitter, Wilbert
PY - 2009/8
Y1 - 2009/8
N2 - ESX-5 is one of the five type VII secretion systems found in mycobacteria. These secretion systems are also known as ESAT-6-like secretion systems. Here, we have determined the secretome of ESX-5 by a proteomic approach in two different strains of Mycobacterium marinum. Comparison of the secretion profile of wild-type strains and their ESX-5 mutants showed that a number of PE-PGRS and PPE-MPTR proteins are dependent on ESX-5 for transport. The PE and PPE protein families are unique to mycobacteria, are highly expanded in several pathogenic species, such as Mycobacterium tuberculosis and M. marinum, and certain family members are cell surface antigens associated with virulence. Using a monoclonal antibody directed against the PGRS domain we showed that nearly all PE-PGRS proteins that are recognized by this antibody are missing in the supernatant of ESX-5 mutants. In addition to PE-PGRS and PPE proteins, the ESX-5 secretion system is responsible for the secretion of a ESAT-6-like proteins. Together, these data show that ESX-5 is probably a major secretion pathway for mycobacteria and that this system is responsible for the secretion of recently evolved PE-PGRS and PPE proteins.
AB - ESX-5 is one of the five type VII secretion systems found in mycobacteria. These secretion systems are also known as ESAT-6-like secretion systems. Here, we have determined the secretome of ESX-5 by a proteomic approach in two different strains of Mycobacterium marinum. Comparison of the secretion profile of wild-type strains and their ESX-5 mutants showed that a number of PE-PGRS and PPE-MPTR proteins are dependent on ESX-5 for transport. The PE and PPE protein families are unique to mycobacteria, are highly expanded in several pathogenic species, such as Mycobacterium tuberculosis and M. marinum, and certain family members are cell surface antigens associated with virulence. Using a monoclonal antibody directed against the PGRS domain we showed that nearly all PE-PGRS proteins that are recognized by this antibody are missing in the supernatant of ESX-5 mutants. In addition to PE-PGRS and PPE proteins, the ESX-5 secretion system is responsible for the secretion of a ESAT-6-like proteins. Together, these data show that ESX-5 is probably a major secretion pathway for mycobacteria and that this system is responsible for the secretion of recently evolved PE-PGRS and PPE proteins.
UR - http://www.scopus.com/inward/record.url?scp=67651233950&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2958.2009.06783.x
DO - 10.1111/j.1365-2958.2009.06783.x
M3 - Article
C2 - 19602152
AN - SCOPUS:67651233950
SN - 0950-382X
VL - 73
SP - 329
EP - 340
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 3
ER -
