Tuberculosis (TB) remains a major public health concern in most low-income countries. Hence, rapid and sensitive TB diagnostics play an important role in detecting and preventing …
A Mehra, A Zahra, V Thompson… - PLoS …, 2013 - journals.plos.org
Mycobacterium tuberculosis (Mtb) disrupts anti-microbial pathways of macrophages, cells that normally kill bacteria. Over 40 years ago, D'Arcy Hart showed that Mtb avoids delivery to …
J De Leon, G Jiang, Y Ma, E Rubin, S Fortune… - Journal of Biological …, 2012 - ASBMB
Mycobacterium tuberculosis ESAT-6 (MtbESAT-6) reportedly shows membrane/cell-lysis activity, and recently its biological roles in pathogenesis have been implicated in rupture of …
C Poulsen, S Panjikar, SJ Holton, M Wilmanns… - PLoS …, 2014 - journals.plos.org
Members of the WXG100 protein superfamily form homo-or heterodimeric complexes. The most studied proteins among them are the secreted T-cell antigens CFP-10 (10 kDa culture …
JH Chang, D Desveaux… - Annual review of …, 2014 - annualreviews.org
Bacteria have many export and secretion systems that translocate cargo into and across biological membranes. Seven secretion systems contribute to pathogenicity by translocating …
The 6-kDa early secreted antigenic target (ESAT-6; EsxA) of Mycobacterium tuberculosis was first identified as a potent T-cell antigen, and it is now recognized as a pore-forming …
D Ilghari, KL Lightbody, V Veverka, LC Waters… - Journal of Biological …, 2011 - ASBMB
Mycobacterium tuberculosis encodes five type VII secretion systems that are responsible for exporting a number of proteins, including members of the Esx family, which have been …
Mycobacteria, such as the major human pathogen Mycobacterium tuberculosis, have a highly unusual and characteristic diderm cell envelope that protects them against harmful …
Y Ma, V Keil, J Sun - Journal of Biological Chemistry, 2015 - ASBMB
EsxA (ESAT-6), an important virulence factor of Mycobacterium tuberculosis, plays an essential role in phagosome rupture and bacterial cytosolic translocation within host …