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Heller"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"disease":["Giardiasis"],"software":[""],"submitter_keywords":["Membrane-binding","Giardia lamblia","Unconventional secretion","Oligomerization","Pip","Endocytic compartments","Molecular dynamics","Annexin a5","Lipid","Alpha-giardin"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074377"],"sample_protocol":["G. lamblia trophozoites expressing a tagged reporter construct of interest or wt control WB were grown in two T25 culture flask per line over two days until confluency was reached on both sides of the flask (turned after the first 24 hours). For harvesting, the cultures were placed on ice for a minimum of one hour for the cells to detach before they were transferred to 50ml Falcon tubes. Cells were centrifuged and resuspended in 10ml PBS with addition of protease inhibitors (Sigma) and 1% Triton-X-100. Cells were burst using sonication and then incubated in the cold for two hours with gentle rotation. Samples were transferred to Eppendorf tubes and centrifuged at 16000g for 10 min at 4°. Supernatants were filtered through 0.2μm PVDF membrane syringe filters and incubated with anti-HA agarose beads (Thermo Fisher Scientifc) for protein pulldown according to manufacturer’s instructions (40µl slurry/extract from a T25 flask). Following the overnight incubation, the beads were washed 3x with PBS+ 0.1% Triton-X-100 and 3x with PBS. For simple co-IP, beads were stored frozen before analysis. For DSSO crosslinking, beads corresponding to one flask per line were resuspended in 500ul PBS and 10ul DSSO in DMSO (50mM) was added to reach approximately a 100-fold molar excess of crosslinker over the protein concentration. After an incubation of 45 minutes at room temperature, the reaction was stopped with Tris buffer (resulting in a final Tris concentration of 0.1M) for 5 min and the beads were washed 3x with PBS and stored frozen before analysis. All bead samples were handed over to the Proteomics and Mass Spectrometry Core Facility of the University of Bern for tryptic digests and peptide analysis.  Proteins captured on the pull-down beads were denatured in 30 μL 8 M urea, 50 mM Tris/HCl pH 8, and cysteines alkylated with 50 mM iodoacetamide for 30 min in the dark after reduction with 10 mM DTT for 30 min at 37°C. The urea concentration was lowered by adding 60 μL 20mM Tris/HCl pH 8 containing 2 mM CaCl2, followed by digestion with 100 ng LysC for 2 hours at 37°C. Urea was further diluted to 1.6 M and digestion continued by addition of 100 ng trypsin over night at room temperature. After acidification with 1% TFA end concentration, aliquots of 5 μL were analyzed by nano-liquid reversed phase chromatography coupled to tandem mass spectrometry on an Orbitrap Fusion LUMOS mass spectrometer that was coupled with a Dionex Ultimate 3000 nano-UPLC system (ThermoFischer Scientific, Reinach, Switzerland). For non-crosslinked samples a standard data-dependent acquisition method as described elsewhere (Buchs et al., 2018, Frontiers in Plant Science. 9:1735. 10.3389/fpls.2018.01735) was used with a homemade C18 CSH Waters separation column (1.7 μm, 130 Å, 75 μm × 20 cm) at a flow rate of 250 nL/min. The cross-linked samples were analyzed on the same system using a MS2-MS3-MS2 method. Full MS scans in the orbitrap in the range of 375-1500 m/z were acquired every 5 s. In between data-dependent CID MS2 scans on peptide ions with charge 3-8 were acquired in the orbitrap with resolution 30’000, a fixed relative collision energy of 25%, precursor isolation window of 1.6 m/z, and a MIT of 54 ms. Two MS3 CID fragmentations were triggered on MS2 fragments which formed an ion pair spaced by the DSSO-specific 31.9721 Da at a mass tolerance of 10ppm. Relative collision energy was set at 35%, normalized automatic gain control to 200%, and MIT to 120 ms. If no ion pair was detected in the MS2 CID spectrum another MS2 scan with HCD fragmentation was recorded in the orbitrap at a relative collision energy of 30% and MIT of 100 ms."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The non-cross-linked data was interpreted with MaxQuant (version 2.3.1.0) applying strict trypsin cleavage rule with maximum 3 missed cleavages, carbamidomethylation of cysteines as fixed, oxidation of methionines and protein n-terminal acetylation as variable modifications allowing a maximum of three modifications per peptide, a first round search precursor mass tolerance of 15 ppm, and fragment mass tolerance of 0.4 Da, against the Giardia lamblia Assemblage AWB protein sequence database from GiardiaDB (version 55) together with a small database of 230 proteins commonly found as contaminants and the reversed versions of both databases. A false discovery rate on the peptide and protein level of 1% was applied and only proteins identified with at least two unique peptides were accepted. The data of the crosslinked samples was interpreted against the same protein sequence database using ProteomeDiscoverer version 3.1.0.638 with built-in Sequest HT and XlinkX again using a decoy search strategy to control the false discovery rate at 1% for non- and cross-linked peptide identifications."],"omics_type":["Proteomics"],"labhead":["Carmen Faso"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Institute of Cell Biology, University of Bern"],"species":["Giardia Intestinalis Assemblage A"],"publication":["10.64898/2026.01.09.697555"],"submitter_mail":["pmscf.dbmr@unibe.ch"],"submitter_affiliation":["Proteomics and Mass Spectrometry Core Facility,\nDepartement for Biomedical Research,\nUniversity of Berne"],"submitter_country":["Switzerland"],"additional_accession":[]},"is_claimable":false,"name":"The N’ terminus of Alpha-1 Giardin, a parasitic annexin orthologue, is essential for oligomerization and lipid-binding activity","description":"We present a functional analysis of alpha-giardins (αGs), with a particular focus on α1-giardin (α1G), a leading vaccine candidate against giardiasis and a putative virulence-associated UPS substrate. We show that αGs localize to peripheral endocytic compartments (PECs), specialized endo-lysosomal organelles implicated in protein release, and engage in multiprotein complexes enriched in UPS substrates. Using lipid-binding assays, cross-linking mass spectrometry (XL-MS), and structural modelling, we define conserved and divergent features of αG membrane interactions. Focusing on α1G, we combine site-directed mutagenesis, confocal microscopy, and mass photometry to demonstrate a critical role for its short N-terminal region in oligomerization and membrane association. Integration of these data with molecular dynamics simulations reveals how α1G oligomeric state and membrane occupancy are regulated at PEC membranes. Together, our findings establish a mechanistic framework for annexin-mediated UPS in Giardia and provide structural insights relevant to parasite virulence and vaccine development.","dates":{"publication":"2026-06-11","submission":"2026-02-12"},"accession":"PXD074377","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:2736291","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:166340","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:111225","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:2767846","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:468822","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:709964","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:156974","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:29022","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:9006","NEWT:33548","NEWT:52299","NEWT:1883426","NEWT:8165","NEWT:96794","NEWT:10401","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:141469","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:291146","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:911022","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:1255232","NEWT:11723","NEWT:445","NEWT:153009","NEWT:1004879","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:156981","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:219799","NE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