Results: 5

1.
FIG. 5.

FIG. 5. From: FbpA-Dependent Biosynthesis of Trehalose Dimycolate Is Required for the Intrinsic Multidrug Resistance, Cell Wall Structure, and Colonial Morphology of Mycobacterium smegmatis.

MAMEs of Mycobacterium smegmatis. The mycolates covalently linked to arabinogalactans of M. smegmatis MC2155, MAR1, and the fbpAMS-complemented strain were extracted and revealed by thin-layer chromatography, including α-MAME, α′-MAME, and epoxy-MAME. Radioisotope labeling experiments (as described for Fig. 4) indicated that the three strains incorporated equal levels of [14C]acetate into each of the three MAMEs.

Liem Nguyen, et al. J Bacteriol. 2005 October;187(19):6603-6611.
2.
FIG. 3.

FIG. 3. From: FbpA-Dependent Biosynthesis of Trehalose Dimycolate Is Required for the Intrinsic Multidrug Resistance, Cell Wall Structure, and Colonial Morphology of Mycobacterium smegmatis.

Altered morphologies and hydrophobicities of MAR1 colonies. A. The MAR1 colonial morphology was smooth and shiny compared to the rough and irregular surface and edge of wild-type M. smegmatis MC2155. B. The MAR1 surface was more hydrophilic compared to wild-type M. smegmatis MC2155. Droplets of oil or water containing trypan blue were applied to the surface of mutant and wild-type colonies. In the upper and lower panels, the oil spread into a thin film over the surface.

Liem Nguyen, et al. J Bacteriol. 2005 October;187(19):6603-6611.
3.
FIG.4.

FIG.4. From: FbpA-Dependent Biosynthesis of Trehalose Dimycolate Is Required for the Intrinsic Multidrug Resistance, Cell Wall Structure, and Colonial Morphology of Mycobacterium smegmatis.

α,α′-trehalose dimycolate from Mycobacterium smegmatis MC2155, MAR1, and the fbpAMS-complemented strain. A. Thin-layer chromatography of TDM extracts from equal amount of cells of mycobacterial strains. B. Quantitative analysis of TDM extracts from [14C]acetate-labeled mycobacterial cultures of wild-type M. smegmatis MC2155 (dark bars), MAR1 (shaded bars), and the fbpAMS complemented strain (empty bars) during growth, by scintillation counting of TLC-purified TDM. C. Identities of TDM extracts from mycobacterial cultures were compared to purified Mycobacterium tuberculosis TDM by IR spectroscopy.

Liem Nguyen, et al. J Bacteriol. 2005 October;187(19):6603-6611.
4.
FIG. 1.

FIG. 1. From: FbpA-Dependent Biosynthesis of Trehalose Dimycolate Is Required for the Intrinsic Multidrug Resistance, Cell Wall Structure, and Colonial Morphology of Mycobacterium smegmatis.

Effect of fbpA allele expression on antibiotic susceptibility of Mycobacterium smegmatis. Antibiotic sensitivities of the wild-type MC2155, the MAR1 mutant, and the MAR1 mutants expressing fbpAMS, fbpAMS(S171A), fbpAMTB, fbpDMS, or both fbpAMS and fbpDMS were assayed using E-test strips containing antibiotic gradients. A. Representative E-test assay with rifampin (left) and erythromycin (right) strips. B. MICs (in μg ml−1) of M. smegmatis strains to vancomycin (VA), rifampin (RI), erythromycin (EM), and imipenem (IP) as determined using this assay.

Liem Nguyen, et al. J Bacteriol. 2005 October;187(19):6603-6611.
5.
FIG. 2.

FIG. 2. From: FbpA-Dependent Biosynthesis of Trehalose Dimycolate Is Required for the Intrinsic Multidrug Resistance, Cell Wall Structure, and Colonial Morphology of Mycobacterium smegmatis.

Identification of transposon mutation of MAR1 and the orthologous loci in Mycobacterium smegmatis, Mycobacterium tuberculosis, and Mycobacterium leprae genomes. A. Synteny of the orthologous loci in three mycobacterial genomes. MAR1 had a transposon mutation in a gene homologous to fbpAMTB. Sequencing mapped the insertion to a TA dinucleotide that introduced a stop codon after the Leu79 residue. B. PCR amplification using primers flanking the fbpAMS open reading frame of wild-type M. smegmatis MC2155. The transposon insertion in MAR1 resulted in a corresponding increase in the size of the PCR product. C. Western blot assay results using monoclonal antibody against the M. tuberculosis antigen 85 complex. The higher-molecular-weight signal (arrow) was missing in the MAR1 protein filtrate sample, and it reappeared when MAR1 was complemented with fbpAMS. D. Alignment of the carboxyesterase domain of Fbp proteins from M. smegmatis (MS), M. tuberculosis (MTB), and the human carboxyesterase D (CarbestD). The carboxylesterase consensus sequence is underlined. and the conserved serine 171 is marked in bold. Amino acid shading indicates the degree of conservation.

Liem Nguyen, et al. J Bacteriol. 2005 October;187(19):6603-6611.

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk