Ontology highlight
ABSTRACT:
PROVIDER: PRJNA176381 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| AFZI01.dat.gz | Other | |||
| AFZI01.fasta.gz | Fasta.gz | |||
| AFZI01.master.dat | Other | |||
| ANOX01.dat.gz | Other |
Items per page: 5 1 - 5 of 351 |
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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
Project description:Abstract: The Kinetoplastida (Euglenozoa) are unicellular flagellates that include the trypanosomatid parasites, most notably Trypanosoma brucei, T.cruzi and Leishmania spp. These organisms cause substantial mortality and morbidity in humans and their livestock worldwide as the causative agents of African sleeping sickness, Chagas disease and leishmaniasis respectively. Draft genome sequences are available for several species of both Trypanosoma and Leishmania. Bodo saltans is a free-living heterotroph found worldwide in freshwater and marine habitats, and it is among the closest bodonid relatives of the trypanosomatids. The purpose of a B. saltans genome sequence is to provide an 'out-group' for comparative genomic analysis of the trypanosomatid parasites. It will provide a model of the ancestral trypanosomatid to distinguish those derived parts of the parasite genomes (i.e., unique trypanosomatid adaptations) from those which are a legacy of the free-living ancestor. To aid annotation of the B.saltans genome sequence, total genomic RNA was extracted on four occasions from the total cellular mass of 160ml of B.saltans cell culture, for the purposes of transcription profiling by high throughput sequencing. Cells were unmodified. B.saltans cells were grown in water at 4oC. Total genomic RNA was extracted from a cell pellet using TRIZOL reagent and ethanol precipitated. Poly A+ mRNA was purified from total RNA using oligo dT dyna bead selection and libraries were created using the Illumina RNA-seq protocol. The samples were sequenced on an Illumina HiSeq 2000. This data is part of a pre-publication release. For information on the proper use of pre-publication data shared by the Wellcome Trust Sanger Institute (including details of any publication moratoria), please see http://www.sanger.ac.uk/datasharing/
2012-07-13 | E-ERAD-88 | biostudies-arrayexpress
Project description:RNA polymerase III (RNAP III) synthetizes small essential non-coding RNA molecules such as tRNAs and 5S rRNA. In yeast and vertebrates, RNAP III needs general transcription factors TFIIIA, TFIIIB and TFIIIC to initiate transcription. TFIIIC, composed of six subunits, binds to internal promoter elements in RNAP III-dependent genes. Limited information is available about RNAP III transcription in the trypanosomatid protozoa Trypanosoma brucei and Leishmania major, which diverged early from the eukaryotic lineage. Analyses of the first draft of the trypanosomatid genome sequences failed to recognize orthologs of any of the TFIIIC subunits, suggesting that this transcription factor is absent in these parasites. However, a single putative TFIIIC subunit was recently annotated in the databases. Here we characterize this subunit in T. brucei and L. major and demonstrate that it corresponds to Tau95. In silico analyses showed that both proteins possess the typical Tau95 sequences: the DNA binding region and the dimerization domain. As anticipated for a transcription factor, Tau95 localized to the nucleus in insect forms of both parasites. Chromatin immunoprecipitation (ChIP) assays demonstrated that Tau95 binds to tRNA and U2 snRNA genes in T. brucei. Remarkably, by performing tandem affinity purifications we identified orthologs of TFIIIC subunits Tau55, Tau131 and Tau138 in T. brucei and L. major. Thus, contrary to what was assumed, trypanosomatid parasites do possess a TFIIIC complex. Other putative interacting partners of Tau95 were identified in T. brucei and L. major.
2024-01-16 | PXD045036 | Pride
Project description:Exoproteome represents the proteome consisting of all secreted proteins and proteins derived from the cell surface and lysed cell. The exoproteome of the trypanosomatid parasite should interact with the host cells and the associated microbiota; however, the roles of infecting insect hosts are not yet understood. To uncover the functions of exoproteome, we identified the exoproteome of honey bee trypanosomatid parasite, Lotmaria passim, and found that approximately 28 % are shared with that common between Leishmania spp. It demonstrates a core exoproteome with conserved functions exists in the Leishmaniinae lineage. The bioinformatic characterization suggests that L.passim exoproteome may interact with the host and its microbiota as well as their metabolites. Deletion of genes encoding two secretome proteins revealed that an aspartyl protease but not chitinase affects the development of L. passim under the culture condition and is necessary for the efficient infection in the honey bee gut. Our results demonstrate that the exoproteome represents a resource to uncover the mechanisms of trypanosomatid parasites to infect the insect host by interacting with the gut environment.
2024-02-18 | PXD040336 | Pride
Project description:In humans and other eukaryotes, histone post-translational modifications (hPTMs) play an essential role in the epigenetic control of gene expression. In trypanosomatid parasites, conversely, gene regulation occurs mainly at the post-transcriptional level. However, our group has recently shown that hPTMs are abundant and varied in Trypanosoma cruzi, the etiological agent of Chagas Disease, signaling for possible conserved epigenetic functions. Here, we provide a high-confidence comprehensive map of hPTMs, distributed in all canonical, variant and linker histones of T. cruzi. Our updated landscape expands the number of known T. cruzi hPTMs by almost 2-fold, representing the largest dataset of hPTMs available to any trypanosomatid to date, and can be used as a basis for functional studies on the dynamic regulation of chromatin by epigenetic mechanisms and the selection of candidates for the development of epigenetic drugs in trypanosomatids.
2021-01-04 | PXD019104 | Pride
Project description:Trypanosoma brucei is the causative agent of human African trypanosomiasis, which is responsible for thousands of deaths every year. Current therapies are limited and there is an urgent need to develop new drugs. The anti-trypanosomal compound, 3-(oxazolo[4,5-b]pyridine-2-yl)anilide (OXPA), was initially identified in a phenotypic screen and subsequently optimized by structure–activity directed medicinal chemistry. It has been shown to be non-toxic and to be active against a number of trypanosomatid parasites. However, nothing is known about its mechanism of action.
2017-10-09 | MTBLS360 | MetaboLights
Project description:The evolution of parasitism is a recurring event in the history of life and a core question in evolutionary biology. Trypanosomatids are important parasites including the human pathogens Trypanosoma brucei, T. cruzi and Leishmania spp., which have evolved complex life cycles to exploit a series of defined host environments after diverging from free-living, phagotrophic bodonids. However, the origins of genomic adaptations for transmission, disease and pathogenesis remain obscure because there has been no genomic comparison of parasitic and free-living species. Addressing this absence, we have produced a genome sequence for Bodo saltans, the closest known non-parasitic relative of trypanosomatids. Here we show how genomic reduction and innovation contributed to the character of trypanosomatid genomes. We find that despite a genetic ‘streamlining’ of diverse physiological functions, including macromolecular degradation and cellular homeostasis, the origin of trypanosomatid parasitism did not lead to a substantial reduction in genome function. Instead, we observe dramatic elaboration of gene families that facilitate host-parasite interactions and pathogenesis. We also show how parasite-specific proteins that characterize the enigmatic cell surfaces of Trypanosoma and Leishmania were derived from the same ancestral proteins, still represented in B. saltans. Our new evidence distinguishes adaptive innovations of trypanosomatids that post-date their parasitic origin from essentially kinetoplastid legacies of a free-living past. It shows that when the labile environment of a phagotrophic ancestor was replaced by the defined conditions of their various hosts, trypanosomatid physiology was reoriented towards host interaction, and ancestral structures were radically transformed to provide adaptations for obligate parasitism.
2018-10-24 | PXD002628 | Pride
Project description:The functions of the majority of trypanosomatid-specific proteins are unknown, hindering our understanding of the biology and pathogenesis of Trypanosomatida. While protein-protein interactions are highly informative about protein function, a global map of protein interactions and complexes is still lacking for these important human parasites. Here, benefiting from in-depth biochemical fractionation, we systematically examined the protein complexes of more than 3354 protein groups in procyclic life stage of Trypanosoma brucei, the protozoan parasite responsible for human African trypanosomiasis. Using a rigorous methodology, our analysis led to identification of 128 high-confidence complexes encompassing 716 protein groups, including 635 protein groups that had no available experimental annotation. These complexes correlate well with known pathways as well as for proteins co-expressed across the T. brucei life cycle, and provide potential functions for a large number of previously uncharacterized proteins. We validated the functions of several novel proteins associated with the RNA-editing machinery, identifying candidates potentially involved in the life stage specific post-transcriptional regulation in T. brucei. Our data provide an unprecedented view of the protein complex map of T. brucei, and serve as a reliable resource for further characterization of trypanosomatid proteins.
2016-02-29 | PXD002640 | Pride