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HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Plasmodium falciparum

PROVIDER: GSE141762 | GEO | 2021/04/14

REPOSITORIES: GEO

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HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [HiC]

Project description:The mutually exclusive expression of virulence genes is critical for the immune evasion and pathogenesis of malaria parasites, Plasmodium falciparum, in human host. The three-dimensional genome structure has emerged as a new factor involved in transcriptional regulation of virulence gene families in the parasites. However, the mechanism controlling this epigenetic regulation pathway remains elusive. Here, we have identified the highly conserved high mobility group protein HMGB1 as a critical architectural regulator in establishment of high-order genome structure via interaction with centromeres in P. falciparum. Genetic manipulation of Pfhmgb1 gene and Hi-C analysis showed that the boundary of telomere and centromere clusters in an opposite spatial relationship in the nucleus was disrupted upon hmgb1 knockout. The collapse of euchromatic centromere cluster from nuclear periphery towards the opposite heterochromatic telomere cluster triggered relocation of the original active var gene, which resulted in complete silence of the entire repertoire of var gene family. ChIP-seq and fluorescence assay analysis confirmed the specific interaction between PfHMGB1 and centromeres. Meanwhile, as in other eukaryotes, PfHMGB1 was also widely present on the promoter regions of a variety of genes and co-regulated transcription, including other non-var variant gene families, suggesting multiple dimensions of epigenetic gene regulation by PfHMGB1. Finally, the natural genome organization could be reconstructed by hmgb1 gene complementation, which rescued the mutually exclusive expression of virulence genes. Taken together, our work provides new insight into the evolution of biological functions of the HMG architectural superfamily in eukaryotes.

2021-04-14 | GSE141759 | GEO

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [HM-ChIP]

2021-04-14 | GSE141760 | GEO

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [TF ChIP]

2021-04-14 | GSE141761 | GEO

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [RNA-seq]

2021-04-14 | GSE141758 | GEO

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum

Project description:HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum

| PRJNA594633 | ENA

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [HiC]

Project description:HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [HiC]

| PRJNA594637 | ENA

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [HM-ChIP]

Project description:HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [HM-ChIP]

| PRJNA594636 | ENA

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [RNA-seq]

Project description:HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [RNA-seq]

| PRJNA594639 | ENA

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [TF ChIP]

Project description:HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [TF ChIP]

| PRJNA594640 | ENA

Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes.

Project description:A major part of virulence for Plasmodium falciparum malaria infection, the most lethal parasitic disease of humans, results from increased rigidity and adhesiveness of infected host red cells. These changes are caused by parasite proteins exported to the erythrocyte using novel trafficking machinery assembled in the host cell. To understand these unique modifications, we used a large-scale gene knockout strategy combined with functional screens to identify proteins exported into parasite-infected erythrocytes and involved in remodeling these cells. Eight genes were identified encoding proteins required for export of the parasite adhesin PfEMP1 and assembly of knobs that function as physical platforms to anchor the adhesin. Additionally, we show that multiple proteins play a role in generating increased rigidity of infected erythrocytes. Collectively these proteins function as a pathogen secretion system, similar to bacteria and may provide targets for antivirulence based therapies to a disease responsible for millions of deaths annually.

| S-EPMC2568870 | biostudies-literature

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