ArticleScientific reports2019
Overexpression of Trypanosoma cruzi High Mobility Group B protein (TcHMGB) alters the nuclear structure, impairs cytokinesis and reduces the parasite infectivity.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Next generation genetic screens in kinetoplastids.Nucleic acids research · 2025Review
- Metacyclogenesis as the Starting Point of Chagas Disease.International journal of molecular sciences · 2023Review
- Synthesis and biological evaluation in vitro and in silico of N-propionyl-N'-benzeneacylhydrazone derivatives as cruzain inhibitors of Trypanosoma cruzi.Molecular diversity · 2022Article
- Ablation of theFrontiers in cellular and infection microbiology · 2022Article
- Drug Target Validation of the Protein KinaseMicrobiology spectrum · 2021Article
- Three-dimensional chromatin in infectious disease-A role for gene regulation and pathogenicity?PLoS pathogens · 2021Review
- Alpha-Tubulin Acetylation inFrontiers in cellular and infection microbiology · 2021Article
- Comparative Analysis of the Minimum Number of Replication Origins in Trypanosomatids and Yeasts.Genes · 2020Article
- Role of Trypanosoma cruzi nucleoside diphosphate kinase 1 in DNA damage responses.Memorias do Instituto Oswaldo Cruz · 2020Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Kinetoplastid parasites, included Trypanosoma cruzi, the causal agent of Chagas disease, present a unique genome organization and gene expression. Although they control gene expression mainly post-transcriptionally, chromatin accessibility plays a fundamental role in transcription initiation control. We have previously shown that High Mobility Group B protein from Trypanosoma cruzi (TcHMGB) can bind DNA in vitro. Here, we show that TcHMGB also acts as an architectural protein in vivo, since the overexpression of this protein induces changes in the nuclear structure, mainly the reduction of the nucleolus and a decrease in the heterochromatin:euchromatin ratio. Epimastigote replication rate was markedly reduced presumably due to a delayed cell cycle progression with accumulation of parasites in G2/M phase and impaired cytokinesis. Some functions involved in pathogenesis were also altered in TcHMGB-overexpressing parasites, like the decreased efficiency of trypomastigotes to infect cells in vitro, the reduction of intracellular amastigotes replication and the number of released trypomastigotes. Taken together, our results suggest that the TcHMGB protein is a pleiotropic player that controls cell phenotype and it is involved in key cellular processes.
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