Dataset Information

Proteomic analysis of exported chaperone/co－chaperone complexes of P. falciparum reveals an array of complex protein-protein interactions

ABSTRACT: Project describe: The P. falciparum export 300-400 proteins during infect human red blood cell, where they are involved in host cell modification including We recently identified a novel structure in P. falciparum-infected erythrocytes which we refer to as J-dots. These structures contain exported parasite-encoded Hsp40s and are implicated in protein transport through the erythrocyte. This project wants isolation and proteomic characterisation of parasite-induced intra-erythrocytic structure to understand their importance in parasite survival and virulence. A more thorough understanding of this novel process may eventually lead to new avenues for therapy.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Plasmodium Falciparum Homo Sapiens (human)

TISSUE(S): Blood Cell, Cell Culture, Blood

DISEASE(S): Plasmodium Falciparum Malaria

SUBMITTER: Qi Zhang

LAB HEAD: Jude M. Przyborski

PROVIDER: PXD003789 | Pride | 2018-10-18

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

Items per page:

1 - 5 of 27

Publications

Proteomic analysis of exported chaperone/co-chaperone complexes of P. falciparum reveals an array of complex protein-protein interactions.

Zhang Qi Q Ma Cheng C Oberli Alexander A Zinz Astrid A Engels Sonja S Przyborski Jude M JM

Scientific reports 20170220

Malaria parasites modify their human host cell, the mature erythrocyte. This modification is mediated by a large number of parasite proteins that are exported to the host cell, and is also the underlying cause for the pathology caused by malaria infection. Amongst these proteins are many Hsp40 co-chaperones, and a single Hsp70. These proteins have been implicated in several processes in the host cell, including a potential role in protein transport, however the further molecular players in this ...[more]

PMID: 28218284

Similar Datasets

Project description:The development of the human malaria parasite Plasmodium falciparum is controlled by coordinated changes in gene expression throughout its complex life cycle, but the corresponding regulatory mechanisms are incompletely understood. To study the relation between genome architecture and gene regulation in Plasmodium, we studied the genome structure of P. falciparum at three time points during its erythrocytic (asexual) cycle. Using chromosome conformation capture coupled with next-generation sequencing technology (Hi-C), we obtained high-resolution chromosomal contact maps, which we then used to construct a consensus three-dimensional genome structure for each time point. We observe strong clustering of centromeres, telomeres, ribosomal DNA and virulence genes, resulting in a complex architecture that cannot be explained by a simple volume exclusion model. Internal virulence gene clusters appear to be an important factor in shaping the genome architecture as they exhibit domain-like structures similar to topological domains in mammalian genomes. Midway during the cell cycle, at the highly transcriptionally active trophozoite stage, the genome adopts a more open chromatin structure with increased chromosomal intermingling. In addition, we observed reduced expression of genes located in spatial proximity to the repressive subtelomeric center, and colocalization of distinct groups of parasite-specific genes with coordinated expression profiles. Overall, our results are indicative of a strong association between the P. falciparum spatial genome organization and gene expression. Understanding the molecular processes involved in genome conformation dynamics could contribute to the discovery of novel antimalarial strategies. Analysis of the spatial organization of the P. falciparum genome at three stages of the erythrocytic cycle using chromosome conformation capture coupled with next generation sequencing (Hi-C). As a control, we included one sample for which chromatin contacts were not preserved by crosslinking of DNA and proteins.

			Action	DRS
	3D7-GFP_1.raw	Raw
	3D7-GFP_2.raw	Raw
	3D7-GFP_3.raw	Raw
	3D7-GFP_4.raw	Raw
	3D7-GFP_5.raw	Raw