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Parasites were exposed to heat stress at 39 °C during the trophozoite stage. Control cultures were maintained at 37 °C. Following heat stress parasites were returned to 37 °C until sample collection. Infected red blood cells were enriched at 30 hours post invasion using a 60 percent Percoll density gradient. Enriched cells were washed three times in phosphate buffered saline. Parasite pellets were lysed in 8 M urea prepared in 50 mM HEPES pH 8.5. Protease inhibitors and phosphatase inhibitors were added to all samples. 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 using a BCA assay. Equal amounts of protein were reduced with dithiothreitol and alkylated with iodoacetamide. Excess alkylating agent was quenched prior to digestion. Samples were diluted to reduce urea concentration and digested first with LysC followed by overnight digestion with trypsin at 37 °C. Peptides were acidified with trifluoroacetic acid and insoluble material was removed by centrifugation. Peptides were desalted using C18 solid phase extraction cartridges and dried by vacuum centrifugation. Dried peptides were resuspended in HEPES buffer containing acetonitrile for tandem mass tag labelling. TMT 10 plex and TMTpro 16 plex reagents were used according to the manufacturer’s instructions. Labelling reactions were quenched and samples were acidified prior to pooling. Labelling efficiency was confirmed by mass spectrometry before combining samples in equal ratios. Phosphopeptides were enriched using a sequential metal oxide affinity chromatography approach. Titanium dioxide enrichment was performed first according to the manufacturer’s protocol. The supernatant from this step was retained and subjected to a second enrichment using iron nitrilotriacetic acid resin. Phosphopeptide eluates from both enrichment steps were combined. The flow through containing non phosphorylated peptides was retained as a total proteome reference. Enriched phosphopeptides were fractionated using high pH reversed phase chromatography. Fractions were dried by vacuum centrifugation and resuspended in acidic buffer prior to LC MS MS analysis."],"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 acetylation of protein N termini and phosphorylation of serine threonine and tyrosine residues were included as variable modifications. For datasets containing proximity labelling data 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 protein and site levels using a target decoy approach. Reporter ion quantification was performed within MaxQuant using the appropriate TMT or TMTpro settings. Only peptides passing quality filtering were used for quantification. Phosphosite localisation probabilities were calculated by MaxQuant and used to assign confident phosphorylation sites. MaxQuant output files were further processed using Perseus software. Common contaminants and reverse sequence hits were"],"omics_type":["Proteomics"],"labhead":["Moritz Treeck"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Group Leader, GIMM, Lisbon, Portugal"],"species":["Homo Sapiens (human)","Plasmodium Falciparum (isolate 3d7)"],"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_mail":["david.a.e.jones@gmail.com"],"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":"Phosphoproteomics of Plasmodium falciparum infected red blood cells under Heat Stress","description":"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 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