{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_01.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_02.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_03.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/SN.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_06.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_07.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_08.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_05.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065129/P5005_04.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["matthew.dixon@unimelb.edu.au"],"submitter":["Laura Dagley"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"disease":["Plasmodium Falciparum Malaria"],"software":[""],"submitter_keywords":["Maurer’s clefts","Exported proteins","Mahrp2","Tether","Pfemp1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065129"],"tissue":["Blood Cell","Blood"],"sample_protocol":["Four biological replicates of control and MAHRP2 cKO iRBCs were analysed. 30-60 mL of iRBCs (20-32 hpi, ~5% parasitemia) were harvested by magnet purification and lysed using 10x pellet volumes of 0.03% saponin/PBS for 10mins in ice. The solution was centrifuged at 16, 000 x g, the supernatant discarded, and the pellet washed at least three times in 1x PBS. The pellets were lysed in 100 µL of preheated (95°C) buffer (2.5% SDS in 100 mM Tris-HCl, pH 8.5). Next DNA was hydrolysed with the addition of 2 µL neat TFA (Sigma) and lysates were neutralised to pH 8.5 by the addition of 40 µL 1M Tris-HCl as previously described (45). Protein concentrations were determined using Pierce™ BCA Protein Assay Kit following manufacturers’ instructions. Cell lysates (20 µg protein per replicate) were transferred to 0.5 mL LoBind Deep Well plate (Eppendorf) prepared for mass spectrometry analysis using the modified SP3 protocol, with some modifications. Briefly, samples were subjected to simultaneous reduction and alkylation with a final concentration of 10 mM Tris (2-carboxyethyl) phosphine (TCEP) and 40 mM 2-chloracetamide followed by heating at 95 °C for 10 minutes. Prewashed magnetic PureCube Carboxy agarose beads (20 µL, Cube Biotech) were added to all the samples along with acetonitrile (ACN,70% v/v final concentration) and incubated at room temperature for 20 min. Samples were placed on a magnetic rack and supernatants were discarded, and beads were washed twice with 70% ethanol and once with neat ACN. ACN was completely evaporated from the tubes using a CentriVap (Labconco) before the addition of digestion buffer (50 mM Tris-HCl, pH 8) containing 1 µg each of enzymes Lys-C (Wako, 129–02541) and SOLu-Trypsin (Sigma-Aldrich, EMS0004). Trypsin-LysC on-bead digestion was performed with agitation (400 rpm) for 1 h at 37 °C on a ThermoMixer C (Eppendorf). Following digestion, the samples were transferred to pre-equilibrated C18 StageTips (2× plugs of 3M Empore resin, no. 2215) for sample clean-up. The eluates were lyophilized to dryness before being reconstituted in 0.1% FA/2% ACN ready for mass spectrometry analysis.   Reconstituted peptides were separated using reverse-phase liquid chromatography on a 15 cm C18 fused silica column with an integrated emitter tip (IonOpticks, ID 75 µm, OD 360 µm, 1.6 µm C18 beads) on a NeoVanquish LC coupled to Thermo Orbitrap Astral. Peptides were analysed on a 25 min linear analytical gradient of increasing buffer B (80% ACN, 0.1% FA) from 2 to 34%. Data was acquired in a data independent (DIA) mode. The MS1 settings were as follows: Orbitrap resolution 240,000; scan range m/z 380-980; AGC target 500%. The DIA parameters were as follows: isolation window: custom; HCD collision energy: 25%; scan range: m/z 145-1450; maximum injection time: 3 ms; AGC target: 800%."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw DIA data were analysed on Spectronaut version 19.2 using BGS factory settings of directDIA analysis. Plasmodium falciparum Uniprot Reference Proteome (2021) was used for database searching. Data processing and analysis were performed using R (version 4.4.1). Proteins without any proteotypic precursors, with q-value greater than 0.01 and/or were identified by one peptide were removed. In addition, only proteins that were quantified in at least 50% of replicates in at least one condition were kept. Total of 4,219 proteins were included in the analysis. Protein intensities were log2-transformed.  No imputation was applied, except for proteins that were completely missing in one group but detected in the other group, to enable statistical comparison. For these proteins, missing values were imputed using random numbers drawn from a normal distribution shifted 1.8 standard deviations down and with a width (standard deviation) of 0.3. The data was normalised using RUVIIIC (v.1.0.19). Differential analysis was performed using limma (v.3.52.4). A protein was determined to be significantly differentially expressed if the absolute value of log fold change was greater than or equal to 1 and the false discovery rate (FDR) was ≤ 5% after correcting for multiple testing using Benjamini–Hochberg (H-B) approach."],"omics_type":["Proteomics"],"labhead":["Matthew W A Dixon"],"instrument_platform":[""],"labhead_affiliation":["Walter and Eliza Hall Institute of Medical Research and The University of Melbourne"],"submission_type":["PARTIAL"],"species":["Plasmodium Falciparum (isolate 3d7)"],"publication":["42291314 Shibu MA, Shami GJ, Hanssen E, Carmo OMS, Vaibhav V, Yousef J, Dagley LF, McCarthy J, Dixon MWA. MAHRP2 is required for tether formation and cytoadherence in &lt;i&gt;Plasmodium falciparum&lt;/i&gt; infected red blood cells. Front Cell Infect Microbiol. 2026 16:1675134 10.3389/fcimb.2026.1675134"],"submitter_mail":["dagley.l@wehi.edu.au"],"submitter_affiliation":["WEHI"],"submitter_country":["Australia"],"pubmed_abstract":["The ability of the human malaria parasite <i>Plasmodium falciparum</i> to remodel its host red blood cell (RBC) is central to the parasite's ability to survive within the circulation of its host and cause disease. Following invasion, the parasite exports proteins into the RBC cytoplasm where they remodel the membrane skeleton and alter the cell's biophysical properties. Many of the exported proteins are trafficked through parasite derived structures called Maurer's clefts in the cytoplasm of the RBC. These clefts act as an intermediate compartment for proteins <i>en route</i> to the RBC membrane such as the major virulence protein, <i>Plasmodium falciparum</i> Erythrocyte Membrane Protein 1 (<i>Pf</i>EMP1). From the Maurer's clefts, <i>Pf</i>EMP1 is delivered to the RBC membrane through a poorly understood process, which may involve trafficking via a physical connection and/or vesicle mediated trafficking. Electron-tomography of 3D7 infected RBCs reveals a tube-like structure, called the tether, that connects the Maurer's clefts to the RBC membrane. To date, the formation and function of these tether structures is unclear, with only one protein, the Membrane Associated Histidine Rich Protein 2 (MAHRP2) known to locate at these structures. In this study, we show that deletion of MAHRP2 leads to a loss of tethers, reduced Maurer's cleft immobilization at the RBC membrane and an increase in Maurer's cleft size. Lastly, we show that deletion of MAHRP2 impacts PTP2 related vesicle formation, and a reduced ability to cytoadhere to the endothelial ligands CD36."],"pubmed_title":["MAHRP2 is required for tether formation and cytoadherence in &lt;i&gt;Plasmodium falciparum&lt;/i&gt; infected red blood cells."],"pubmed_authors":["Shibu Mohini A MA, Shami Gerald J GJ, Hanssen Eric E, Carmo Olivia M S OMS, Vaibhav Vineet V, Yousef Jumana J, Dagley Laura F LF, McCarthy James J, Dixon Matthew W A MWA"],"additional_accession":[]},"is_claimable":false,"name":"MAHRP2 is required for tether formation and PfEMP1 trafficking in Plasmodium falciparum infected red blood cells.","description":"The ability of the human malaria parasite Plasmodium falciparum to remodel its host red blood cell (RBC) is central to the parasite’s ability to survive within the circulation of its host and cause disease. Following invasion, the parasite exports proteins into the RBC cytoplasm where they remodel the membrane skeleton and alter the cells biophysical properties. Many of the exported proteins are trafficked through parasite derived structures called Maurer’s clefts in the cytoplasm of the RBC. These clefts act as an intermediate compartment for proteins en route to the RBC membrane such as the major virulence protein, Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1). From the Maurer’s clefts, PfEMP1 is delivered to the RBC membrane through a poorly understood process, which is thought to combine physical tethering of the Maurer’s clefts to the membrane and vesicle mediated trafficking. A tube-like structure called the tether can be seen by electron-tomography connecting the Maurer’s clefts to the RBC membrane. To date, the function and formation of these tether structures are unknown, with only one protein, the Membrane Associated Histidine Rich Protein 2 (MAHRP2) known to locate at these structures. In this study, we show that deletion of MAHRP2 ablates tether formation, affects Maurer’s cleft immobilisation at the RBC membrane, resulting in a significant reduction in PfEMP1 trafficking to the membrane and the parasite’s ability to cytoadhere. Lastly, we show that deletion of MAHRP2 leads to global impacts in PTP2 related vesicle formation and a reduction in J-dot chaperone 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