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Site-directed mutagenesis of Mycobacterium tuberculosis and functional validation to investigate potential bedaquiline resistance causing mutations

ABSTRACT: Site-directed mutagenesis of Mycobacterium tuberculosis and functional validation to investigate potential bedaquiline resistance causing mutations

PROVIDER: PRJEB55096 | ENA |

REPOSITORIES: ENA

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Site-directed mutagenesis for bedaquiline resistance

Project description:SITE-DIRECTED MUTAGENESIS OF MYCOBACTERIUM TUBERCULOSIS AND FUNCTIONAL VALIDATION TO INVESTIGATE POTENTIAL BEDAQUILINE RESISTANCE CAUSING MUTATIONS

| PRJEB52049 | ENA

Global Gene expression data from Mycobacterium tuberculosis treated with new TB drug named Bedaquiline

Project description:Sirturo or Bedaquiline has been shown to inhibit the ATP synthase of Mycobacterium tuberculosis. We used microarrays to investigate compound-induced gene expression changes in general as well as effects on the transcription of the different ATP synthase genes and other metabolic pathways. Log phase Mycobacterium tuberculosis were cultivated in Middlebrook 7H9 broth and treated with 1 M-BM-5M Bedaquiline. We have extracted RNA from five different time-points after treatment: 0 min (T0), 30 min (T30), 60 min (T60), 180 min (T180) and 360 min (T360).

2014-03-03 | E-GEOD-43749 | biostudies-arrayexpress

Global Gene expression data from Mycobacterium tuberculosis treated with new TB drug named Bedaquiline

2014-03-03 | GSE43749 | GEO

Transcriptional Response of Mycobacterium tuberculosis H37Rv to Bedaquiline

Project description:Bacteria commonly adapt to stresses by altering gene expression. To understand the response of M. tuberculosis (MTB) to bedaquiline, we performed transcriptomics over a time-course on MTB bacilli exposed to the drug.

2016-05-05 | GSE72459 | GEO

Bedaquiline-induced transcriptional response of Mycobacterium smegmatis mc2 155

2015-04-06 | GSE59871 | GEO

Bedaquiline-induced transcriptional response of Mycobacterium smegmatis mc2 155

Project description:Transcriptional profiling of M. smegmatis mc2155 grown on Hartmans de Bont (HdB) supplemented with 0.2% glycerol and 0.05% Tween80 challenged with 2 μg/ml Bedaquiline and Dimethyl sulfoxide (DMSO) Two-condition experiment. Biological replicates: 5 independently grown and harvested. One replicate per array.

2015-04-06 | E-GEOD-59871 | biostudies-arrayexpress

Mycobacterium tuberculosis transcriptional response to Bedaquiline

Project description:The ability of Mycobacterium tuberculosis (Mtb) to adopt heterogeneous physiological states, underlies it’s success in evading the immune system and tolerating antibiotic killing. Drug tolerant phenotypes are a major reason why the tuberculosis (TB) mortality rate is so high, with over 1.8 million deaths annually. To develop new TB therapeutics that better treat the infection (faster and more completely), a systems-level approach is needed to reveal the complexity of network-based adaptations of Mtb. Here, we report the transcriptional response of Mtb to the drug Bedaquiline. We performed transcriptomic sequencing (RNA-seq) on Mtb bacilli at 4, 24, 72 h following exposure to the drug.

2021-12-15 | GSE166546 | GEO

Bedaquiline remodels the macrophage response

Project description:Bedaquiline remodels the macrophage response

| PRJNA550090 | ENA

Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis.

Project description:Fibronectin's RGD-mediated binding to the alpha5beta1 integrin is dramatically enhanced by a synergy site within fibronectin III domain 9 (FN9). Guided by the crystal structure of the cell-binding domain, we selected amino acids in FN9 that project in the same direction as the RGD, presumably toward the integrin, and mutated them to alanine. R1379 in the peptide PHSRN, and the nearby R1374 have been shown previously to be important for alpha5beta1-mediated adhesion (Aota, S., M. Nomizu, and K.M. Yamada. 1994. J. Biol. Chem. 269:24756-24761). Our more extensive set of mutants showed that R1379 is the key residue in the synergistic effect, but other residues contribute substantially. R1374A decreased adhesion slightly by itself, but the double mutant R1374A-R1379A was significantly less adhesive than R1379A alone. Single mutations of R1369A, R1371A, T1385A, and N1386A had negligible effects on cell adhesion, but combining these substitutions either with R1379A or each other gave a more dramatic reduction of cell adhesion. The triple mutant R1374A/P1376A/R1379A had no detectable adhesion activity. We conclude that, in addition to the R of the PHRSN peptide, other residues on the same face of FN9 are required for the full synergistic effect. The integrin-binding synergy site is a much more extensive surface than the small linear peptide sequence.

| S-EPMC2175162 | biostudies-literature

REPLACR-mutagenesis, a one-step method for site-directed mutagenesis by recombineering.

Project description:Mutagenesis is an important tool to study gene regulation, model disease-causing mutations and for functional characterisation of proteins. Most of the current methods for mutagenesis involve multiple step procedures. One of the most accurate methods for genetically altering DNA is recombineering, which uses bacteria expressing viral recombination proteins. Recently, the use of in vitro seamless assembly systems using purified enzymes for multiple-fragment cloning as well as mutagenesis is gaining ground. Although these in vitro isothermal reactions are useful when cloning multiple fragments, for site-directed mutagenesis it is unnecessary. Moreover, the use of purified enzymes in vitro is not only expensive but also more inaccurate than the high-fidelity recombination inside bacteria. Here we present a single-step method, named REPLACR-mutagenesis (Recombineering of Ends of linearised PLAsmids after PCR), for creating mutations (deletions, substitutions and additions) in plasmids by in vivo recombineering. REPLACR-mutagenesis only involves transformation of PCR products in bacteria expressing Red/ET recombineering proteins. Modifications in a variety of plasmids up to bacterial artificial chromosomes (BACs; 144 kb deletion) have been achieved by this method. The presented method is more robust, involves fewer steps and is cost-efficient.

| S-EPMC4707547 | biostudies-literature

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