Proteomics

Dataset Information

0

Phosphoproteomics of Plasmodium falciparum infected red blood cells under Heat Stress

ABSTRACT: This project investigates changes in protein phosphorylation in the malaria parasite Plasmodium falciparum in response to heat stress. During infection parasites are exposed to febrile temperatures in the human host. Heat stress is known to trigger adaptive responses but the role of protein phosphorylation in this process is not fully understood. The aim of this study is to identify phosphorylation events that change following exposure to elevated temperature. Synchronous asexual blood stage parasites were exposed to heat stress and compared with parasites maintained at normal culture temperature. Parasites were harvested after heat stress and proteins were extracted and digested into peptides. Phosphopeptides were enriched prior to analysis by liquid chromatography coupled to tandem mass spectrometry. The resulting data provide a global view of phosphorylation changes associated with heat stress in P. falciparum. This dataset enables the identification of heat responsive phosphosites and supports analysis of signalling pathways and regulatory processes that may contribute to parasite adaptation to febrile conditions.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human) Plasmodium Falciparum (isolate 3d7)

TISSUE(S): Blood Cell, Blood

SUBMITTER: David Jones  

LAB HEAD: Moritz Treeck

PROVIDER: PXD073843 | Pride | 2026-05-14

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
DZ2172_126.raw Raw
DZ2172_127C.raw Raw
DZ2172_127N.raw Raw
DZ2172_128C.raw Raw
DZ2172_128N.raw Raw
Items per page:
1 - 5 of 38
altmetric image

Publications

Physiological febrile heat stress increases cytoadhesion through increased protein trafficking of <i>Plasmodium falciparum</i> surface proteins into the red blood cell.

Jones David D   Belda Hugo H   Broncel Malgorzata M   Fuchs Gwendolin G   Anaguano David D   Nofal Stephanie D SD   Treeck Moritz M  

eLife 20260513

Fever is a hallmark of malaria. Several studies have linked febrile temperatures to reduced parasite viability, but also to increased cytoadhesion, a key driver of pathology. However, different mechanisms have been proposed to cause changes in cytoadhesion and parasite sensitivity to heat. Here, we demonstrate that exposure of <i>Plasmodium falciparum</i>-infected red blood cells (iRBCs) to physiologically relevant febrile heat stress (39 °C), derived from patient data, enhances cytoadhesion thr  ...[more]

Similar Datasets

Proteomics TurboID Proximity Profiling of FIKK10.2 (PF3D7_1039000) in Plasmodium falciparum–Infected Red Blood Cells During Febrile Heat Stress
2026-05-14 | PXD073890 | Pride
Transcriptomics P. falciparum heat shock response in a PfAP2-HS-defective population compared to its wild type control.
2021-05-17 | GSE149392 | GEO
Proteomics Activity-Based Protein Profiling of Human and Plasmodium Serine Hydrolases and Interrogation of Potential Antimalarial Targets
2022-10-14 | PXD035891 | Pride
Transcriptomics RNA-seq of blood and adipose tissue from mice infected with Trypanosoma brucei
2016-05-26 | E-MTAB-4061 | biostudies-arrayexpress
Transcriptomics RNA-seq of Plasmodium berghei PbWT and PbHMGB1KO parasite strains
2024-09-17 | E-MTAB-14378 | biostudies-arrayexpress
Transcriptomics Transcript level responses of Plasmodium falciparum to antimycin A
2012-04-19 | E-GEOD-28625 | biostudies-arrayexpress
Transcriptomics Transcription profiling of P. falciparum parasites from human placenta or culture
2007-10-01 | E-MEXP-1087 | biostudies-arrayexpress
Transcriptomics Chromatin immunoprecipitation to determine localization of H3K9me3 in Plasmodium falciparum
2009-02-24 | E-MEXP-1805 | biostudies-arrayexpress
Proteomics Protein interactions and phosphorylation status of Maf1 during optimal growth and stress conditions in the human parasite Leishmania major
2025-11-24 | PXD067545 | Pride
Proteomics PKA C3 depletion phosphoproteomics
2024-07-12 | PXD042989 | Pride