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GilData-dependent acquisitionMass SpectrometryMalariaGlucosephosphate Dehydrogenase DeficiencyCarbonylationG6pdPhosphorylationBlue nativePlasmodium falciparum exportomeTimstofhttps://www.ebi.ac.uk/pride/archive/projects/PXD061301ErythrocyteBloodExtraction of Membrane Complexes from Plasmodium falciparum-Infected Erythrocytes Samples were obtained from synchronous cultures of Plasmodium falciparum FCB-2 with parasitemia upper to 30% in erythrocytes from donors enzymatically healthy and G6PD-deficients. Infected red blood cells were collected at various developmental stages: rings (12-14 hours), trophozoites (24-28 hours) and schizonts (38-42 hours). Infected erythrocytes were treated with 5% sorbitol in 20 mM sodium HEPES buffer, pH 7.4, and vortexed to facilitate the lysis of red blood cells. The resulting samples were then centrifuged at 1700 rpm for 6 minutes at 4°C, allowing for the collection of the supernatant, which contains membrane proteins from infected erythrocytes, Plasmodium proteins, and soluble proteins. The sorbitol lysates were subsequently subjected to different centrifugation cycles in 5 mM phosphate buffer until obtaining the membrane protein fraction free of hemoglobin. These ghosts were preserved under native conditions to facilitate the isolation of protein complexes via Blue-native electrophoresis. Sample Preparation for Blue-Native Electrophoresis (BN-PAGE) For blue-native electrophoresis, the membrane ghosts were solubilized in 50 mM Bis-Tris (pH 7.0), 750 mM ε-aminocaproic acid, and 0.5 mM Na2EDTA, supplemented with 20% dodecyl-β-D-maltoside (DDM). Based on the extracted volume, one-fifth of 50% glycerol and one-twelfth of 5% Coomassie G250 were incorporated into the sample prior to loading onto the gel. The native blue gels were prepared with fixed percentages: a 3% stacking gel and an 8% resolving gel. Electrophoretic separation was performed at 250 V (constant) for approximately 10 hours at 4 °C, with temperature regulation facilitated by a thermostatic cooling bath system (LAUDA Alpha RA12). Mass Spectrometry Two gel bands conglomerates (1 and 2) at stacking and resolving border were excised from each lane of the one-dimensional native blue gels (1D BN) by each donor. Then, they were subjected to in-gel digestion utilizing the iST kit (PreOmics GmbH, Martinsried, Germany) with minor modifications. Initially, moisture was eliminated from the gel slices through washing with acetonitrile, followed by vacuum drying in a SpeedVac for 15 minutes. The gel slices were then incubated at 56 °C for 30 minutes in a 10 mM dithiothreitol (DTT) solution, serving as a reducing agent. After incubation, excess DTT was removed, and the slices were incubated with 55 mM iodoacetamide for 15 minutes in the dark. Any residual iodoacetamide was subsequently removed by incubation with acetonitrile, followed by a wash with 50 mM ammonium bicarbonate (AMBI). Acetonitrile was added to the AMBI solution without prior removal, and the mixture was further incubated for an additional 15 minutes. Following the removal of all liquids, the gel slices were dried in the SpeedVac for 45 minutes. Peptide digestion was conducted using trypsin at a ratio of 1 µg trypsin per 20 µg protein. The gel slices were incubated at 4 °C for 45 minutes. Subsequently, the trypsin solution was removed, and the gels were incubated with AMBI at 37 °C overnight. Next, the tubes were equilibrated at room temperature for 15 minutes and then centrifuged at 13,000 rpm. The supernatant was transferred to new centrifuge tubes. To enhance peptide extraction, the gel slices underwent additional washes with acetonitrile, AMBI, and acetonitrile for 5 minutes each. The resulting supernatants were combined with the previously collected supernatant. Finally, the samples were dried for 2 hours using a SpeedVac and subsequently reconstituted in 100 µL of buffer (Acetonitrile 2% / formic acid 0.1%) for further analysis.PrideNot availableRaw files obtained from mass spectrometry, specifically through Data-Dependent Acquisition-Parallel Accumulation-Serial Fragmentation (DDA-PASEF), were processed using FragPipe (release 20.0), which is integrated with MSFragger for peptide spectrum matching. The proteomes of Homo sapiens and Plasmodium falciparum 3D7 were downloaded from the UniProt database (downloaded September 2023) to serve as a reference for peptide and protein identification. Trypsin was designated as the digestion enzyme, allowing for a maximum of two missed cleavages. Philosopher was utilized to generate a decoy database and to implement false discovery rate (FDR) filtering at a threshold of 1% for both peptide and protein levels. Label-free quantification (LFQ) was performed using IonQuant. Subsequent reports of protein identification were generated for further downstream analysis.ProteomicsDarío Méndez CuadroPARTIALUniversity of Cartagena, Faculty of Exact and Natural Sciences, Campus of San Pablo. Analytical Chemistry and Biomedicine Group.Plasmodium FalciparumHomo Sapiens (human)42390622 De la Rosa Cogollo I, Hernáez ML, Clemente LF, Marrugo-Padilla A, Rodríguez-Cavallo E, Méndez-Cuadro D. G6PD deficiency and the exportome of plasmodium falciparum FCB-2: A comparative analysis utilizing one-dimensional blue-native electrophoresis and timstof mass spectrometry. Parasitol Res. 2026 125(1):113 10.1007/s00436-026-08717-ycai.proteomica@pas.ucm.esUCMSpainPlasmodium falciparum, the etiological agent of severe malaria in humans, remodels the surface of infected erythrocytes to evade host immune defenses and ensure its survival. During its intraerythrocytic development, P. falciparum modifies the composition of protein complexes within the host cell membrane and cytoskeleton by exporting parasitic proteins to the surface of the infected erythrocyte. However, there is limited understanding of its behavior in cells harboring protective polymorphisms against severe malaria, such as those associated with glucose-6-phosphate dehydrogenase (G6PD) deficiency, where reduced adhesion and early phagocytosis have been observed due to oxidative damage to the surface proteins of parasitized erythrocytes. Nonetheless, the impact of G6PD deficiency on the exportome proteins of P. falciparum in infected erythrocytes remains to be elucidated. In this in vitro study, we conducted a comparative analysis of the P. falciparum FCB-2 exportome in G6PD-deficient versus normal human red blood cells. Two membrane protein conglomerates were isolated at the ring, trophozoite, and schizont stages using Blue-Native electrophoresis, followed by in-gel digestion and LC-MS-tims-TOF analysis. The analysis revealed a significant decrease in the number of P. falciparum proteins identified in all asexual stages for both protein conglomerates on the surface of infected G6PD-deficient erythrocytes. A decrease in the number of effector, adhesion, trafficking, and signaling proteins that reinforce the protective mechanisms previously described was observed. These findings provide new insights into the pathways for understanding the molecular events that support G6PD's protective mechanisms against malaria.G6PD deficiency and the exportome of plasmodium falciparum FCB-2: A comparative analysis utilizing one-dimensional blue-native electrophoresis and timstof mass spectrometry.De la Rosa Cogollo Isaac I, Hernáez María Luisa ML, Clemente Luis Felipe LF, Marrugo-Padilla Albeiro A, Rodríguez-Cavallo Erika E, Méndez-Cuadro Darío DfalseEffects of G6PD deficiency on the phosphorylation and carbonylation of membrane protein complexes of human erythrocytes infected with Plasmodium falciparumThe ancestral parasite-host relationship associated with human malaria has driven the emergence of mutations in genes, such as erythrocyte glucose-6-phosphate dehydrogenase (G6PD), that confer resistance to lethal malaria and enhance human survival. Protein complexes in the erythrocyte membrane play a crucial role in maintaining red blood cell integrity and elasticity, both of which are essential for the parasite’s asexual life cycle. To facilitate this, the Plasmodium falciparum parasite exports proteins that interact with erythrocyte membrane proteins on the cell surface. However, how G6PD deficiency affects the Plasmodium exportome, and the potential role of post-translational modifications (PTMs), such as phosphorylation, direct carbonylation, and 4-hydroxynonenal (4-HNE) carbonylation, on host cell membrane proteins in this interaction remain largely unexplored2026-09-282025-02-28PXD061301NEWT:6945NEWT:184922NEWT:6703NEWT:3555NEWT:2NEWT:157546NEWT:35554NEWT:38942NEWT:307972NEWT:32046NEWT:544496NEWT:2102NEWT:2042546NEWT:45351NEWT:43179NEWT:4513NEWT:5722NEWT:1247NEWT:376741NEWT:55153NCBITaxon:10407NEWT:1736309NEWT:309800NEWT:281395NEWT:10360NEWT:1211601NEWT:876138NEWT:47664NEWT:557436NEWT:3654NEWT:237561NEWT:5833NEWT:6928NEWT:10036NEWT:36745NEWT:1351NEWT:1438992NEWT:2649997NEWT:272563NEWT:79220NEWT:224326NCBITaxon:79857NEWT:1096976NEWT:82688NEWT:95648NEWT:3885NEWT:3888NEWT:1589NEWT:135622NCBITaxon:4896NEWT:6915NEWT:3649NEWT:101510NEWT:28903NEWT:3880NEWT:272559NEWT:3641NEWT:383379NEWT:466585NEWT:10029NEWT:913645NEWT:1000589NEWT:85963NEWT:85962NEWT:317447NEWT:7955NEWT:7959NEWT:2261NEWT:31156NEWT:398580NEWT:4565NEWT:1264690NEWT:515619NEWT:31155NEWT:192875NEWT:34305NEWT:59729NCBITaxon:183674NEWT:224308NEWT:84645NEWT:626528NEWT:3347NEWT:139927NEWT:4558NEWT:209285NEWT:5888NEWT:211586NEWT:1283NEWT:931281NEWT:4550NEWT:1000561NEWT:197NEWT:1390363NEWT:288705NCBITaxon:79824NEWT:4787NCBITaxon:4563NEWT:5755NEWT:44689NEWT:3218NEWT:5759NEWT:1736231NEWT:1270NEWT:374990NEWT:2242NEWT:4784NEWT:11320NEWT:360106NEWT:286NEWT:391619NEWT:360104NEWT:287NEWT:246197NEWT:10117NEWT:10239NEWT:10116NEWT:1280NEWT:1735272NEWT:83334NEWT:83332NEWT:44685NEWT:317513NEWT:1148NEWT:580240NEWT:5508NEWT:294128NEWT:11676NEWT:55571NEWT:35500NEWT:1140NEWT:100226NEWT:4530NEWT:4896NEWT:75058NEWT:13616NEWT:1390NEWT:1094343NEWT:1336795NEWT:172NEWT:296543NEWT:1773NEWT:1895NEWT:1182590NEWT:3712NEWT:105023NEWT:935293NEWT:64152NEWT:4924NEWT:749200NEWT:375146NEWT:990346NEWT:145953NEWT:257309NEWT:100816NEWT:263NEWT:230741NEWT:52283NEWT:284812NCBITaxon:1313NEWT:43330NEWT:980415NEWT:1603293NEWT:408169NEWT:44544NEWT:47946NEWT:4911NEWT:645463NEWT:3702NEWT:129249NEWT:243277NEWT:990119NEWT:408172NEWT:408170NEWT:493760NEWT:260710NEWT:257313NEWT:400772NEWT:3708NEWT:128161NEWT:332648NEWT:106592NEWT:536231NEWT:1436733NEWT:460519NEWT:1187947NEWT:1432138NEWT:10312NEWT:1424507NCBITaxon:1773NEWT:9598NEWT:8030NEWT:9483NEWT:1639NEWT:188229NEWT:3818NEWT:480NEWT:4909NEWT:67767NEWT:432359NEWT:46835NEWT:1182263NEWT:2711NEWT:300852NEWT:1502NEWT:376686NEWT:95486NEWT:9103NEWT:29159NEWT:253NEWT:10306NCBITaxon:2759NEWT:1233435NEWT:93061NEWT:8022NEWT:145943NCBITaxon:4932NEWT:595536NEWT:240906NEWT:593117NEWT:89920NEWT:3635NEWT:5811NEWT:235443NEWT:108458NEWT:272623NEWT:272624NEWT:2719099NEWT:411483NEWT:884019NEWT:198215NEWT:411490NEWT:983964NEWT:169963NEWT:32644NEWT:225117NEWT:499175NEWT:109779NEWT:476272NEWT:3747NEWT:195051NEWT:367830NEWT:1255228NEWT:178616NEWT:410289NEWT:373153NEWT:352472NEWT:357NEWT:360094NEWT:470NEWT:1313NEWT:411469NEWT:84023NEWT:559292NEWT:39491NCBITaxon:5811NEWT:411464NEWT:411460NEWT:2014887NEWT:2762NEWT:1174673NEWT:562NEWT:411470NEWT:33952NEWT:2094720NCBITaxon:2697049NEWT:571256NEWT:28038NEWT:1663NEWT:1423NEWT:4932NEWT:3603NEWT:2759NEWT:3847NEWT:38293NEWT:327159NEWT:178876NEWT:327160NEWT:573NEWT:9031NEWT:7091NEWT:108931NEWT:241368NEWT:42528NEWT:190802NEWT:9778NEWT:150475NEWT:303NEWT:9417NEWT:7111NEWT:347515NEWT:1216979NEWT:7237NEWT:5180NEWT:256737NEWT:9541NEWT:115104NEWT:1121114NEWT:663NEWT:1081927NEWT:1238993NEWT:67825NEWT:185579NEWT:941442NEWT:220668NEWT:13076NEWT:1249668NEWT:7108NEWT:317NEWT:1808362NEWT:7227NEWT:7469NEWT:885318NEWT:9402NEWT:9644NEWT:415540NEWT:550NEWT:675060NEWT:4081NEWT:334542NEWT:554NEWT:27592NEWT:98334NEWT:426428NEWT:1276815NEWT:588858NEWT:9639NEWT:242231NEWT:7574NEWT:1715256NEWT:7215NEWT:575412NEWT:929793NEWT:29204NEWT:2172103NEWT:7460NEWT:6491NEWT:507601NEWT:643680NCBITaxon:6157NEWT:746360NEWT:6239NEWT:470150NEWT:162425NEWT:216257NEWT:102169NEWT:9986NEWT:4054NEWT:73239NEWT:226186NEWT:1268063NEWT:8782NEWT:1263854NEWT:435590NEWT:1902NEWT:160488NEWT:28104NEWT:1908NEWT:13164NEWT:216129NCBITaxon:2NEWT:985076NEWT:1215323NEWT:623NEWT:52641NEWT:7038NEWT:6192NEWT:28532NCBITaxon:38727NEWT:198618NEWT:353152NEWT:2829NEWT:366581NEWT:216599NEWT:216595NEWT:1194669NEWT:51329NEWT:243230NEWT:8355NEWT:633NEWT:9685NEWT:7029NEWT:1080772NEWT:8479NEWT:1283300NEWT:632NEWT:6183NEWT:6063NEWT:630NEWT:334747NEWT:61235NEWT:15368NEWT:6289NEWT:436486NEWT:6287NEWT:300641NEWT:727NEWT:9796NEWT:725NEWT:170187NEWT:469008NEWT:260707NEWT:256318NCBITaxon:6191NEWT:1836NEWT:185431NEWT:2925NEWT:29760NEWT:260704NEWT:703612NEWT:260705NEWT:80863NEWT:2697049NEWT:105231NEWT:1216981NEWT:52638NEWT:4097NCBITaxon:6073NEWT:884204NEWT:6279NEWT:1123869NEWT:9544NEWT:7370NEWT:83906NEWT:607699NCBITaxon:1502NEWT:6282NEWT:426688NEWT:208964NEWT:1134506NEWT:575584NEWT:38783NEWT:8727NEWT:4006NEWT:8726NEWT:6426NEWT:6669NEWT:10090NEWT:4120NEWT:51515NEWT:5693NEWT:8724NEWT:51511NEWT:92867NEWT:8723NEWT:5334NEWT:37334NEWT:382352NCBITaxon:10359NEWT:242619NEWT:632957NEWT:34073NEWT:373995NEWT:5689NEWT:544404NEWT:9925NEWT:8839NEWT:4232NEWT:2758385NEWT:37349NEWT:4113NEWT:837NEWT:11298NEWT:171101NEWT:714NEWT:36015NEWT:421932NEWT:196627NEWT:5691NEWT:48479NEWT:627025NEWT:1097677NEWT:242507NEWT:61674NEWT:1117957NEWT:9913NEWT:8709NEWT:4100NEWT:2666255NEWT:1159556NE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