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Briefly, 4% SDS were added to the sample together with 1 µg Benzonase and incubated for 30 min at room temperature before homogenizing the sample for 10 min in a Bioruptor (30 s, 30 s off). Proteins were reduced with 5 mM TCEP and alkylated with 40 mM CAA for 1 h at room temperature. Sera-Mag beads were added to the sample followed by 50% ACN. The supernatant was removed after a brief incubation. The beads were washed twice with EtOH and once with ACN before the addition of digestion buffer, which contained 50 mM TEAB pH 8.5, LysC and Trypsin (both in enzyme:protein ratio 1:50 w:w). After incubation for 16 h at 37 °C, beads were washed twice by adding an excess of ACN. Peptides were eluted with 5% DMSO and dried until further use. Cross-linked peptides were enriched by offline fractionation using either SEC or SCX. For SEC, peptides were loaded on a SuperdexTM 30 Increase 3.2/300 (GE Healthcare) and separated over a 60 min gradient. Early eluting fractions were combined into eight samples and dried before MS acquisition. For SCX, peptides were loaded on a PolySULFOETHYL A column 100 x 2.1-mm; 3 µm; 300 Å (PolyLC INC.) and separated over a 95 min gradient. Selected fractions were combined into 8 samples, dried, acidified and desalted using C8 StageTips. Peptides were resuspended in 1% ACN, 0.05% TFA and injected into a Thermo Scientific™ Vanquish Neo system. Separation was performed using a PepMap C-18 trap column (0.075 mm x 50 mm, 3 µm particle size, 100 Å pore size, Thermo Fisher Scientific), followed by an in-house packed C18 analytical column (Poroshell 120 EC-C18, 2.7 µm, Agilent Technologies). Peptides were separated at a flow rate of 250 nL/min using a 177-minute gradient of increasing ACN concentration, and analyzed on an Orbitrap Exploris 480 mass spectrometer equipped with a FAIMS Pro™ device (Thermo Fisher Scientific), operated with Instrument Control Software version 4.2. For MS1 scans, data were acquired in the Orbitrap at a resolution of 120,000, with advanced peak determination enabled. The MS1 acquisition settings were as follows: data type profile; m/z range of 375 – 1,400; standard AGC target; maximum injection time 50 ms. Precursors with charges of +4 to +8 were isolated within a 1.6 m/z window and dynamically excluded for 60 s. MS2 scans were performed in the Orbitrap at a resolution of 45,000 with the following parameters: data type centroid; automatic scan range; 200% AGC target; 100 ms maximum injection time; stepped collision energies 27 ± 6%. Data acquisition cycled between FAIMS CVs -50, -60, and -75 with a cycle time of 2 seconds per CV."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["RAW data were analyzed using Scout version 1.5.1 with the following parameters: DSSO as the cross-linker reacting with lysine, serine, threonine and tyrosine side chains; trypsin digestion allowing up to 4 missed cleavages; peptide mass range 500 – 6,000 Da; peptide length 6 – 60 residues. Precursor mass tolerance was set to 10 ppm and fragment mass tolerance to 20 ppm. Oxidation of methionine and protein N-terminus acetylation were included as variable, carbamidomethylation as a fixed modification. The interactome data were searched against a joined database containing 1028 plasmodium falciparum and 270 human proteins identified in a standard single-shot proteomics run against the human and the plasmodium falciparum isolate 3D7 proteome (both retrieved from UniProt as one protein per gene) using MSFragger in Fragpipe version 22.0 with default settings. Inter- and intra-links were filtered separately to 2% false discovery rate on both, spectrum and peptide pair level. Peptide pairs have been exported from Scout and converted to a xiNET compatible format for visualization. Two residue pair files of independent experiments exported from Scout were concatenated to produce a combined dataset. This set was used for all modeling and statistical analyses."],"omics_type":["Proteomics"],"labhead":["Jan Kosinski"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["EMBL Hamburg Germany"],"species":["Homo Sapiens (human)","Plasmodium Falciparum 58.1"],"submitter_mail":["ruwolt@fmp-berlin.de"],"publication":["Not available"],"submitter_affiliation":["Leibniz-Forschungsinstitut for Molecular Pharmacology"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Deciphering Membrane Protein Complexes in Plasmodium falciparum Gametocytes via Cross-Linking Mass Spectrometry and Structural Modeling","description":"Malaria is a disease targeting the most vulnerable people. It is caused by the parasite Plasmodium falciparum, and is transmitted to humans by Anopheles mosquitos during a blood meal, who are in turn infected by the parasite if they feed on an infected human. While current eradication efforts focus on mosquito control, transmission blocking therapeutics will be critical for successful eradication. The parasite goes through several life stages and reproduces sexually. This reproduction is mediated by gametocytes, which are responsible for transmission from humans to mosquitos, and thus represent an excellent target for transmission blocking therapeutics. However, there is very little information on the composition and interactions of gametocyte-specific proteins, in particular membrane proteins. In order to fill this knowledge gap, we cultured the gametocytes and isolated their membrane fraction. We then used cross-linking mass-spectrometry as well as size-exclusion and strong-cation exchange fractionation to  identify protein-protein interaction networks. The interactions identified encompass host-pathogen and pathogen-pathogen complexes, and are distributed among many cellular compartments. The results of this study extend the understanding of malaria gametocyte biology, and serve as a springboard to accelerate research into potentially transmission-blocking Malaria therapeutics.","dates":{"publication":"2026-04-09","submission":"2025-08-25"},"accession":"PXD067699","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:625351","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1045775","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:1028307","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:928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