{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/FIKK10.2_TurboID_Data.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_full_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_full_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_pulse_heat_rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_pulse_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_pulse_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_pulse_heat_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_pulse_heat_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_pulse_rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/DZ2362_20211025_biotin_full_rep2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/TurboID_txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD073890/Sample_Information_and_QC_WesternBlot.pptx"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["moritz.treeck@gimm.pt"],"submitter":["David Jones"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Plasmodium Falciparum Malaria"],"software":[""],"submitter_keywords":["Plasmodium falciparum","Proximity labelling","Heat stress","Turboid"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD073890"],"tissue":["Blood Cell","Blood"],"sample_protocol":["Synchronous asexual blood stage Plasmodium falciparum parasites (0–2 hours post-invasion) were cultured in human red blood cells under standard conditions at 37 °C. TurboID-expressing parasite lines were labelled by supplementation of culture media with biotin during the trophozoite stage. Where applicable, parasites were exposed to heat stress at 39 °C, while control cultures were maintained at 37 °C. Following treatment, parasites were returned to 37 °C until sample collection.  Infected red blood cells were enriched at 40 hours post-invasion using a 60 percent Percoll density gradient and washed three times in phosphate-buffered saline. Parasite pellets were lysed in 8 M urea prepared in 50 mM HEPES (pH 8.5) supplemented with protease inhibitors. Lysates were sonicated on ice and clarified by centrifugation. Supernatants were snap-frozen in liquid nitrogen and stored at −80 °C until further processing.  Protein concentration was determined by BCA assay. Equal amounts of protein were reduced with dithiothreitol and alkylated with iodoacetamide, and excess alkylating agent was quenched prior to digestion. Samples were diluted to reduce urea concentration and digested sequentially with LysC followed by overnight digestion with trypsin at 37 °C.  Peptides were acidified with trifluoroacetic acid and insoluble material was removed by centrifugation. Dried peptides were reconstituted in BioSITe buffer. Biotinylated peptides were enriched by immunoprecipitation using anti-biotin antibodies. Dissolved peptides were incubated with anti-biotin antibody–conjugated protein G agarose beads, washed sequentially, and biotinylated peptides were eluted with 0.2% trifluoroacetic acid prior to LC–MS/MS analysis. Eluted peptides were desalted using C18 solid-phase extraction cartridges and dried by vacuum centrifugation. Dried peptides were resuspended in an acidic buffer prior to LC–MS/MS analysis. Peptides were loaded onto Evotips and separated using an Evosep One system fitted with a 15 cm PepSep column and a predefined 44-minute gradient, coupled to an Orbitrap Fusion Lumos mass spectrometer. The instrument was operated in data-dependent acquisition mode with Orbitrap MS1 survey scans acquired at 60,000 resolution, followed by HCD MS/MS scans in the ion trap using a 1-second cycle time, 15 s dynamic exclusion, and a normalised collision energy of 32."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Raw mass spectrometry files were processed using MaxQuant software (version 1.6.2.10). Peptide identification was performed using the Andromeda search engine integrated within MaxQuant. Spectra were searched against combined Plasmodium falciparum and Homo sapiens protein databases. Trypsin was specified as the digestion enzyme with up to three missed cleavages allowed. Carbamidomethylation of cysteine residues was set as a fixed modification. Oxidation of methionine and acetylation of protein N-termini were included as variable modifications. Biotinylation of lysine residues was included as a variable modification. The minimum peptide length was set to six amino acids. The precursor mass tolerance was set to 20 ppm for the initial search and 4.5 ppm for the main search. Fragment ion mass tolerance was set according to default MaxQuant parameters. False discovery rates were controlled at 1 percent at the peptide and protein levels using a target–decoy approach. Peptide intensities were extracted from MaxQuant output files and used for downstream analysis. Only peptides passing quality filtering were retained. MaxQuant output tables were further processed using Perseus software. Common contaminants and reverse sequence hits were removed prior to analysis. Peptide intensity values were log2 transformed prior to downstream analysis."],"omics_type":["Proteomics"],"labhead":["Moritz Treeck"],"instrument_platform":[""],"labhead_affiliation":["Gulbenkian Institute for Molecular Medicine (GIMM), Lisbon, Portugal"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Plasmodium Falciparum (isolate 3d7)"],"submitter_mail":["david.a.e.jones@gmail.com"],"publication":["42126964 Jones D,Belda H,Broncel M,Fuchs G,Anaguano D,Nofal SD,Treeck M Physiological febrile heat stress increases cytoadhesion through increased protein trafficking of Plasmodium falciparum surface proteins into the red blood cell. Elife. 2026 May 13 14 10.7554/eLife.107860"],"submitter_affiliation":["The Francis Crick Institute"],"submitter_country":["United Kingdom"],"pubmed_abstract":["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 through increased trafficking of the major virulence factor PfEMP1 to the iRBC surface. This phenomenon is not limited to PfEMP1 and common laboratory strains, as it extends to the surface nutrient channel PSAC in four clinical isolates of diverse geographic origin. The increased surface protein display occurs without changes in overall protein expression or parasite developmental progression. Using phosphoproteomics and proximity labelling, we find that elevated temperature also increases trafficking and phosphorylation of exported proteins into the RBC. Enhanced export is likely reliant on the presence of a transmembrane domain as shown by NanoLuc reporter assays. Collectively, our results indicate that febrile temperatures commonly experienced during infection can accelerate protein export, likely at the parasitophorous vacuole. This enhanced export following heat stress is relevant because increased cytoadhesion could influence disease severity through earlier iRBC sequestration and elevated bound parasite mass."],"pubmed_title":["Physiological febrile heat stress increases cytoadhesion through increased protein trafficking of &lt;i&gt;Plasmodium falciparum&lt;/i&gt; surface proteins into the red blood cell."],"pubmed_authors":["Jones David D, Belda Hugo H, Broncel Malgorzata M, Fuchs Gwendolin G, Anaguano David D, Nofal Stephanie D SD, Treeck Moritz M"],"additional_accession":[]},"is_claimable":false,"name":"TurboID Proximity Profiling of FIKK10.2 (PF3D7_1039000) in Plasmodium falciparum–Infected Red Blood Cells During Febrile Heat Stress","description":"This project investigates how febrile heat stress alters the local protein environment of the Maurer’s cleft resident kinase FIKK10.2 in the malaria parasite Plasmodium falciparum. During human infection, parasites are routinely exposed to elevated temperatures associated with fever, yet how this physiological stress affects the organisation and trafficking of exported proteins within infected red blood cells remains poorly understood. To address this, we used proximity-dependent biotinylation (TurboID) to map changes in the protein neighbourhood of FIKK10.2 under normal and heat stress conditions. Transgenic parasites were generated expressing TurboID fused to the C-terminus of endogenous FIKK10.2. Highly synchronous (two hours window) asexual blood-stage parasites were exposed to febrile heat stress (39 °C) and compared with parasites maintained at standard culture temperature (37 °C). Biotin labelling was applied either continuously throughout the asexual life cycle or as a defined pulse between 16–24 hours post-invasion, with or without heat stress, resulting in three experimental conditions. Infected red blood cells were harvested at 40 hours post-invasion following Percoll density enrichment and lysed in 8 M urea. Proteins were digested to peptides, and biotinylated peptides were selectively enriched using anti-biotin antibodies. Enriched peptides were eluted under acidic conditions and analysed by liquid chromatography–tandem mass spectrometry. The resulting dataset provides a high-resolution view of the FIKK10.2 proximal proteome and, by extension, the Maurer’s cleft protein environment. These data reveal how febrile heat stress influences protein trafficking and local protein composition in P. falciparum, offering insights into temperature-dependent regulation of host cell remodelling during malaria 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