Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum (HyPR_Api dataset)

ABSTRACT: Mass spectrometry analysis of HyPR_Api samples used for identifying apicoplast rRNA-associated proteins.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Plasmodium Falciparum (ncbitaxon:5833)

SUBMITTER: Laurence Florens

PROVIDER: MSV000095300 | MassIVE | Thu Jul 11 07:19:00 BST 2024

SECONDARY ACCESSION(S): PXD053884

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum (HyPR_Mito dataset)

Project description:Mass spectrometry analysis of HyPR_Mito samples used for identifying mitochondrial rRNA-associated proteins.

2024-07-11 | MSV000095305 | MassIVE

RAP proteins regulate apicoplast noncoding RNA processing in Plasmodium falciparum (IP-MS_RAP03_RAP08 dataset)

Project description:Mass spectrometry analysis of IP-MS samples used for identifying RAP03 and RAP08 associated proteins.

2024-07-11 | MSV000095304 | MassIVE

Plasmodium falciparum

Project description:5CAPture-seq: a method for enriching full-length cDNA and identifying 5′ capped nucleotides

| PRJNA399851 | ENA

Sequential processing of merozoite surface proteins during and after erythrocyte invasion by Plasmodium falciparum.

Project description:Plasmodium falciparum causes malaria disease during the asexual blood stages of infection when merozoites invade erythrocytes and replicate. Merozoite surface proteins (MSPs) are proposed to play a role in the initial binding of merozoites to erythrocytes, but precise roles remain undefined. Based on electron microscopy studies of invading Plasmodium merozoites, it is proposed that the majority of MSPs are cleaved and shed from the surface during invasion, perhaps to release receptor-ligand interactions. In this study, we demonstrate that there is not universal cleavage of MSPs during invasion. Instead, there is sequential and coordinated cleavage and shedding of proteins, indicating a diversity of roles for surface proteins during and after invasion. While MSP1 and peripheral surface proteins such as MSP3, MSP7, serine repeat antigen 4 (SERA4), and SERA5 are cleaved and shed at the tight junction between the invading merozoite and erythrocyte, the glycosylphosphatidylinositol (GPI)-anchored proteins MSP2 and MSP4 are carried into the erythrocyte without detectable processing. Following invasion, MSP2 rapidly degrades within 10 min, whereas MSP4 is maintained for hours. This suggests that while some proteins that are shed upon invasion may have roles in initial contact steps, others function during invasion and are then rapidly degraded, whereas others are internalized for roles during intraerythrocytic development. Interestingly, anti-MSP2 antibodies did not inhibit invasion and instead were carried into erythrocytes and maintained for approximately 20 h without inhibiting parasite development. These findings provide new insights into the mechanisms of invasion and knowledge to advance the development of new drugs and vaccines against malaria.

| S-EPMC3958018 | biostudies-literature

Plasmodium falciparum sexual parasites regulate infected erythrocyte permeability.

Project description:To ensure the transport of nutrients necessary for their survival, Plasmodium falciparum parasites increase erythrocyte permeability to diverse solutes. These new permeation pathways (NPPs) have been extensively characterized in the pathogenic asexual parasite stages, however the existence of NPPs has never been investigated in gametocytes, the sexual stages responsible for transmission to mosquitoes. Here, we show that NPPs are still active in erythrocytes infected with immature gametocytes and that this activity declines along gametocyte maturation. Our results indicate that NPPs are regulated by cyclic AMP (cAMP) signaling cascade, and that the decrease in cAMP levels in mature stages results in a slowdown of NPP activity. We also show that NPPs facilitate the uptake of artemisinin derivatives and that phosphodiesterase (PDE) inhibitors can reactivate NPPs and increase drug uptake in mature gametocytes. These processes are predicted to play a key role in P. falciparum gametocyte biology and susceptibility to antimalarials.

| S-EPMC7708629 | biostudies-literature

Molecular characterization of Plasmodium falciparum Bruno/CELF RNA binding proteins

Project description:The human malaria parasite Plasmodium falciparum employs intricate post-transcriptional regulatory mechanisms in different stages of its life cycle. Despite the importance of post-transcriptional regulation, key elements of these processes, namely RNA binding proteins (RBPs), are poorly characterized. In this study, the RNA binding properties of P. falciparum proteins were characterized including two putative members of the Bruno/CELF family of RBPs (PfCELF1 and PfCELF2), dihydrofolate reductase-thymidylate synthase (PfDHFR-TS), and adenosine deaminase (PfAda).The mRNA targets of these P. falciparum proteins were investigated by ribonomics using DNA microarrays. Two-condition ribonomic experiment, RBP vs. Mock enrichment of mRNAs. Ribonomic experimental replicates: 4-7 for each RBP, 5 for Mock. One replicate per array.

2014-10-23 | E-GEOD-56329 | biostudies-arrayexpress

Molecular characterization of Plasmodium falciparum Bruno/CELF RNA binding proteins

2014-10-23 | GSE56329 | GEO

Low-complexity regions in Plasmodium falciparum proteins.

Project description:Full-sequence data available for Plasmodium falciparum chromosomes 2 and 3 are exploited to perform a statistical analysis of the long tracts of biased amino acid composition that characterize the vast majority of P. falciparum proteins and to make a comparison with similarly defined tracts from other simple eukaryotes. When the relatively minor subset of prevalently hydrophobic segments is discarded from the set of low-complexity segments identified by current segmentation methods in P. falciparum proteins, a good correspondence is found between prevalently hydrophilic low-complexity segments and the species-specific, rapidly diverging insertions detected by multiple-alignment procedures when sequences of bona fide homologs are available. Amino acid preferences are fairly uniform in the set of hydrophilic low-complexity segments identified in the two P. falciparum chromosomes sequenced, as well as in sequenced genes from Plasmodium berghei, but differ from those observed in Saccharomyces cerevisiae and Dictyostelium discoideum. In the two plasmodial species, amino acid frequencies do not correlate with properties such as hydrophilicity, small volume, or flexibility, which might be expected to characterize residues involved in nonglobular domains but do correlate with A-richness in codons. An effect of phenotypic selection versus neutral drift, however, is suggested by the predominance of asparagine over lysine.

| S-EPMC311019 | biostudies-literature

Plasmodium falciparum

Project description:Nanopore sequencing of drug-resistance-associated genes in malaria parasites, Plasmodium falciparum

| PRJDB5281 | ENA

Plasmodium falciparum

Project description:Artemisinin resistance in Plasmodium falciparum is associated with an altered temporal pattern of transcription (expression)

| PRJNA142477 | ENA