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RIT-seq analysis of the anti-leishmanial drugs

ABSTRACT: Chemogenomic profiling of anti-leishmanial efficacy and resistance in the related kinetoplastid parasite Trypanosoma brucei

PROVIDER: PRJEB31973 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR3261666_1.fastq.gz	Fastqsanger.gz
	ERR3261666_2.fastq.gz	Fastqsanger.gz
	ERR3261667_1.fastq.gz	Fastqsanger.gz
	ERR3261667_2.fastq.gz	Fastqsanger.gz
	ERR3261668_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

RIT-seq analysis of the anti-leishmanial drugs

Project description:Chemogenomic profiling of anti-leishmanial efficacy and resistance in the related kinetoplastid parasite Trypanosoma brucei

| PRJEB31973 | ENA

Histone divergence in Trypanosoma brucei results in unique alterations in nucleosome structure

Project description:Eukaryotes have an array of diverse mechanisms for organising and using their genomes, but the histones that make up chromatin are highly conserved. Unusually, histones from Kinetoplastids are highly divergent. The structural and functional consequences of this variation are unknown. Here, we have biochemically characterised nucleosome core particles (NCPs) from the Kinetoplastid parasite Trypanosoma brucei. A structure of the T. brucei NCP reveals that global histone architecture is conserved, but specific sequence alterations lead to distinct DNA and protein interaction interfaces. The T. brucei NCP is unstable and has weakened DNA binding overall. However, dramatic changes at the H2A-H2B interface introduce local reinforcement of DNA contacts. The T. brucei acidic patch has altered topology and is refractory to known binders, indicating that the nature of chromatin interactions in T. brucei may be unique. Overall, our results provide a detailed molecular basis for understanding evolutionary divergence in chromatin structure.

2023-08-30 | GSE226029 | GEO

Mass spectrometry analysis of kinetoplastid kinetochore proteins (KKT23 acetyltransferase and its interactor KKT22) and histone acetylation levels in Trypanosoma brucei

Project description:KKT23 is a kinetoplastid kinetochore protein that has structural similarity to the GCN5 acetyltransferase domain. Using a kinetoplastid parasite Trypanosoma brucei, here we performed immunoprecipitation and mass spectrometry of GFP-tagged KKT23 N-terminal fragment (2–150) to identify co-purifying proteins, and immunoprecipitation and mass spectrometry of H2B-GFP after KKT23 depletion to examine acetylation states of histones. We also performed in vitro acetylation assays on recombinant trypanosome nucleosomes using recombinant KKT23 protein, followed by mass spectrometry.

2024-08-19 | PXD052922 | Pride

Trypanosome flagellar proteome

Project description:This study investigates the proteome of the flagellum of the parasite Trypanosoma brucei. This parasite is the causative agent in African trypanosomiasis. This structure contains a 9 + 2 axoneme structure, highly conserved throughout eukaryotic evolution. The kinetoplastid flagellum additionally has a trypanasome-specific structure, the paraflagellar rod. Here, we have performed analyses based upon 1D- and 2D-gel separation followed by LC-MS/MS identification of peptides associated with flagellar proteins.

2006-07-04 | PRD000017 | Pride

A domino effect in drug action: From metabolic assault towards parasite differentiation

Project description:Glycolysis is the sole free-energy source for the deadly parasite Trypanosoma brucei and is therefore a possible target pathway for anti-trypanosomal drugs. Plasma-membrane glucose transport exerts high control over trypanosome glycolysis and hence the transporter is a promising drug target. Here we show that at high inhibitor concentrations, inhibition of trypanosome glucose transport causes cell death. Most interestingly, sublethal concentrations initiate a domino effect in which network adaptations enhance inhibition.

2010-10-18 | GSE24275 | GEO

A domino effect in drug action: From metabolic assault towards parasite differentiation

2010-10-18 | E-GEOD-24275 | biostudies-arrayexpress

A conserved trypanosomatid differentiation regulator controls substrate attachment and morphological development in Trypanosoma congolense

Project description:Trypanosomatid parasites undergo developmental regulation to adapt to the different environments encountered during their life cycle. In Trypanosoma brucei, a genome wide selectional screen previously identified a regulator of the protein family ESAG9, which is highly expressed in stumpy forms, a morphologically distinct bloodstream stage adapted for tsetse transmission. This regulator, TbREG9.1, has an orthologue in Trypanosoma congolense, despite the absence of a stumpy morphotype in that parasite species, which is an important cause of livestock trypanosomosis. RNAi mediated gene silencing of TcREG9.1 in Trypanosoma congolense caused a loss of attachment of the parasites to a surface substrate in vitro, a key feature of the biology of these parasites that is distinct from T. brucei. This detachment was phenocopied by treatment of the parasites with a phosphodiesterase inhibitor, which also promotes detachment in the insect trypanosomatid Crithidia fasciculata. RNAseq analysis revealed that TcREG9.1 silencing caused the upregulation of mRNAs for several classes of surface molecules, including transferrin receptor-like molecules, immunodominant proteins, and molecules related to those associated with stumpy development in T. brucei. Depletion of TcREG9.1 in vivo also generated an enhanced level of parasites in the blood circulation consistent with reduced parasite attachment to the microvasculature. The morphological progression to insect forms of the parasite was also perturbed. We propose a model whereby TcREG9.1 acts as a regulator of attachment and development, with detached parasites being adapted for transmission.

2024-02-19 | GSE249623 | GEO

In vitro generation of human high-density-lipoprotein-resistant Trypanosoma brucei brucei

Project description:The host range of African trypanosomes is influenced by innate protective molecules in the blood of primates. A subfraction of human high-density lipoprotein (HDL) containing apolipoprotein A-I, apolipoprotein L-I, and haptoglobin-related protein is toxic to Trypanosoma brucei brucei but not the human sleeping sickness parasite Trypanosoma brucei rhodesiense. It is thought that T. b. rhodesiense evolved from a T. b. brucei-like ancestor and expresses a defense protein that ablates the antitrypanosomal activity of human HDL. To directly investigate this possibility, we developed an in vitro selection to generate human HDL-resistant T. b. brucei. Here we show that conversion of T. b. brucei from human HDL sensitive to resistant correlates with changes in the expression of the variant surface glycoprotein (VSG) and abolished uptake of the cytotoxic human HDLs. Complete transcriptome analysis of the HDL-susceptible and -resistant trypanosomes confirmed that VSG switching had occurred but failed to reveal the expression of other genes specifically associated with human HDL resistance, including the serum resistance-associated gene (SRA) of T. b. rhodesiense. In addition, we found that while the original active expression site was still utilized, expression of three expression site-associated genes (ESAG) was altered in the HDL-resistant trypanosomes. These findings demonstrate that resistance to human HDLs can be acquired by T. b. brucei. Keywords: Trypanosoma, VSG, antigenic switching, HDL-resistance

2007-07-04 | GSE8369 | GEO

Differentially expressed genes upon TbSAC3 depletion

Project description:This study examines differential expression upon TbSAC3 depletion in Trypanosoma brucei brucei strain 29.13

2023-02-22 | GSE79773 | GEO

Development and Characterisation of a Novel Class of Aroyl Guanidine Containing Anti-Trypanosomal Compounds

Project description:The mode of action of a novel class of aroyl guanidine containing anti-Trypanosomal compounds was investigated using an unbiased metabolomics approach. Trypanosoma brucei parasites were incubated for five hours with the test compounds at 1 µM concentration. Analysis of cell pellets allowed reproducible detection of diverse metabolites from a range of metabolic pathways.

2019-11-16 | ST001276 | MetabolomicsWorkbench

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