Purification and characterization of Mycobacterium tuberculosis KatG, KatG(S315T), and Mycobacterium bovis KatG(R463L)

2004 ◽  
Vol 36 (2) ◽  
pp. 232-243 ◽  
Author(s):  
Nancy L Wengenack ◽  
Brian D Lane ◽  
Preston J Hill ◽  
James R Uhl ◽  
Gudrun S Lukat-Rodgers ◽  
...  
1970 ◽  
Vol 1 (2) ◽  
pp. 164-168
Author(s):  
Thomas M. Daniel ◽  
Lavenia E. Ferguson

Two proteins have been purified from culture filtrates of Mycobacterium tuberculosis , H 37 Ra strain by a procedure combining gel filtration, diethylaminoethyl (DEAE)-cellulose chromatography, and zone electrophoresis. The two proteins are similar in molecular weight but differ slightly in charge. The faster migrating protein, designated a 1 , is not antigenic. The slower migrating protein, designated a 2 , is antigenic both with respect to antisera and as a skin-testing antigen.


2008 ◽  
Vol 14 (S3) ◽  
pp. 124-125
Author(s):  
L. Jordao ◽  
M. Simoes ◽  
C. Bleck ◽  
G. Griffiths ◽  
E. Anes

Mycobacterium tuberculosis complex are among the most successful pathogens. Their success resides in the ability to interfere with intracellular traffic avoiding natural pathways of the phagosome maturation. Recently, mycobacteria escape from the phagosome to the cytosol was investigated as an alternative survival strategy. In this context we decided to determine the exact intracellular location of Mycobacterium bovis in different host macrophages and characterize the pathogen intracellular niche for survival. The main goal here was to characterize live vs dead M. bovis spp phagosome in different host macrophages. Macrophages infection, fluorescence and EM procedures were carried out as described previously.


1999 ◽  
Vol 67 (4) ◽  
pp. 2035-2039 ◽  
Author(s):  
Jovana Gobin ◽  
Diane K. Wong ◽  
Bradford W. Gibson ◽  
Marcus A. Horwitz

ABSTRACT Pathogenic mycobacteria must acquire iron in the host in order to multiply and cause disease. To do so, they release abundant quantities of siderophores called exochelins, which have the capacity to scavenge iron from host iron-binding proteins and deliver it to the mycobacteria. In this study, we have characterized the exochelins of Mycobacterium bovis, the causative agent of bovine and occasionally of human tuberculosis, and the highly attenuated descendant of M. bovis, bacillus Calmette-Guérin (BCG), widely used as a vaccine against human tuberculosis. The M. bovis type strain, five substrains ofM. bovis BCG (Copenhagen, Glaxo, Japanese, Pasteur, and Tice), and two strains of virulent Mycobacterium tuberculosis all produce the same set of exochelins, although the relative amounts of individual exochelins may differ. Among these mycobacteria, the total amount of exochelins produced is greatest in M. tuberculosis, intermediate in M. bovis, and smallest in M. bovis BCG.


2006 ◽  
Vol 45 (1) ◽  
pp. 241-248 ◽  
Author(s):  
Yanping Yang ◽  
Shengfeng Xu ◽  
Min Zhang ◽  
Ruiliang Jin ◽  
Lu Zhang ◽  
...  

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