Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/PXD079900_community_annotated.sdrf.tsvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/Glycan_bead.sdrf.tsvftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/2025_10_reanalysis_Man_Gal_Lac_replicate_imputation_ANOVA_abundance_based.mzMLftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/20241218_Exploris_TS25_LouridoLab_DV_Sample_6_DDA.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/20241218_Exploris_TS25_LouridoLab_DV_Sample_3_DDA.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/20241218_Exploris_TS25_LouridoLab_DV_Sample_2_DDA.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/20241218_Exploris_TS25_LouridoLab_DV_Sample_7_DDA.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/20241218_Exploris_TS25_LouridoLab_DV_Sample_1_DDA.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/20241218_Exploris_TS25_LouridoLab_DV_Sample_5_DDA.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079900/2025_10_reanalysis_Man_Gal_Lac_replicate_imputation_ANOVA_abundance_based.mzidprimary200OKlourido@wi.mit.eduDylan ValleauData-dependent acquisitionMass SpectrometryBottom-up proteomicsLactoseMicronemeToxoplasma gondiiMannoseGalactoseInvasionhttps://www.ebi.ac.uk/pride/archive/projects/PXD079900T. gondii RH/Δku80/Δhxgprt/dTomato parasites were grown in 15 cm2 plates of confluent HFF cells for 2 days. Parasites were harvested, filtered with 5 μm pore filters to remove host cells and debris, washed 2X with PBS via pelleting (5 min, 2000 g) and resuspension. After the final PBS wash was removed, the pellet was flash frozen in liquid N2. Pellets were lysed on ice by thawing directly into cold SugarAP buffer (PBS with 1 mM CaCl2, MgCl2, 0.5% Igepal CA-630, 1 mM benzonase [Millipore; E1014-25KU], and 1X protease inhibitor cocktail [Thermo; 87786]). While parasites were lysing, 200 μL bead slurry (100 μL final bed) of D-mannose agarose (Sigma; M6400), D-galactose agarose (Pierce; PI20372), and α-lactose agarose were added to empty spin columns (Pierce; 89879) and prepared by washing with 10 gel-bed volumes (4x250 μL) of SugarAP buffer; 40 g spins were used throughout for all steps. The parasite lysate was clarified by a centrifugation to remove insoluble debris (4°C, 11000 g, 10 min), and the soluble lysate flowed over each resin. Resins were washed for a total of 20 gel-bed volumes (8x 250 μL) using SugarAP buffer. Bound proteins were then specifically eluted by 100 mM of the free cognate sugar in SugarAP buffer (i.e. mannose, galactose, lactose), using 7.5 gel-bed volumes (3x 250 μL). Eluted proteins were prepared for mass spectrometry by SP3 bead digestion and clean-up as previously described (Hughes et al, 2019). Briefly, proteins were reduced with TCEP (Pierce, PI20490) and alkylated with chloroacetamide (Thermo, 148415000), precipitated onto hydrophilic and hydrophobic SP3 beads using ethanol, washed in 80% ethanol, and digested overnight with Trypsin/LysC mix (Thermo, A40007). Eluted peptides were lyophilized and directly injected without further cleanup in for DDA mass spectrometry on a Thermo Exploris 480 Orbitrap mass spectrometer equipped with a FAIMS Pro Interface. Two biological replicates were prepared and injected for each sugar sample condition.PrideNot availableRaw files for each condition and replicate were analyzed using Proteome Discoverer 2.4 (Thermo Fisher Scientific). The sequence database search was performed using Sequest HT with the optional search modifications including Oxidation (M), Deamidation (N,Q), Phosphorylation (S,T,Y), and Hexose (S,T,W). Precursor ions-based quantification was used with low abundance resampling for missing value imputation.ProteomicsSebastian LouridoWhitehead Institute for Biomedical Research and Department of Biology, Massachusetts Institute of Biology, Cambridge, MA, USACOMPLETEToxoplasma Gondii Rh42791346 Valleau D, Goyal M, Roberts JM, Male F, Ward GE, Lourido S. Clustering of host N-glycans by the microneme MIC1/4/6 complex licenses Toxoplasma rhoptry discharge. EMBO J. 2026 10.1038/s44318-026-00911-zvalleau@wi.mit.eduWhitehead Institute for Biomedical ResearchUnited States10.6019/PXD079900To initiate the process of invasion, apicomplexan parasites must discharge the contents of specialized organelles called rhoptries into host cells. This process requires prior recognition and binding of the host cell by proteins released from another set of parasite organelles, the micronemes. However, the host-parasite interactions required for rhoptry discharge are largely unknown. Here, we performed a host cell-directed genome-wide screen for factors that mediate rhoptry discharge from Toxoplasma gondii, the causative agent of toxoplasmosis. The screen identified host N-glycosylation and cholesterol biosynthesis as pathways required for normal rhoptry discharge. A trimeric microneme complex, MIC1/4/6, interfaces with both pathways by binding host N-glycans to cluster proteins in a process dependent on host plasma membrane cholesterol. The process can be inhibited by depletion of host cholesterol or competition with exogenous glycans. This clustering of host factors by MIC1/4/6 likely prepares the host membrane for rhoptry discharge, delineating a new step in the Toxoplasma invasion process.Clustering of host N-glycans by the microneme MIC1/4/6 complex licenses Toxoplasma rhoptry discharge.Valleau Dylan D, Goyal Mudita M, Roberts Justin M JM, Male Frances F, Ward Gary E GE, Lourido Sebastian SfalseGlycan bead precipitation of proteins from Toxoplasma gondii lysateApicomplexan parasites use two sets of specialized organelles to invade mammalian host cells, the micronemes and the rhoptries. Microneme proteins mediate adhesion and interaction with host cell surfaces and upon appropriate contact mediate discharge of rhoptry organelles. Injection of rhoptry contents into host cells prepares the host cell for invasion and intracellular replication. We discovered that host galactose-containing N-glycans are required for rhoptry discharge from the apicomplexan Toxoplasma gondii, though the corresponding interacting microneme protein was unknown. Here, we identify the parasite proteins able interact with galactose and lactose. We used agarose beads coated with lactose and galactose to precipitating the specific interactors from whole-parasite lysate. Mannose coated beads were used as a negative control due to host mannose being inconsequential in the rhoptry discharge process. The microneme proteins MIC1, MIC4, and MIC6 were identified as the primary strong interactors of both galactose and lactose. Follow up analysis confirmed their importance to rhoptry discharge and parasite invasion via their interactions with galactose-containing N-glycans. This is the first such host-parasite interaction discovered in Toxoplasma to regulate rhoptry discharge.2026-08-182026-06-18PXD079900NEWT:3555NEWT:71647NEWT:330879NEWT:35554NEWT:32046NEWT:544496NEWT:2042546NEWT:32049NEWT:1392696NEWT:259447NEWT:295546NEWT:45351NEWT:445974NEWT:43179NEWT:180454NEWT:5722NCBITaxon:1280NEWT:1129NEWT:309807NEWT:55153NEWT:10244NEWT:309800NEWT:281395NEWT:1211601NEWT:876138NEWT:44271NEWT:10036NEWT:1590NEWT:498019NEWT:1351NEWT:1438992NEWT:1352NEWT:2649997NEWT:1147161NEWT:638632NEWT:263737NEWT:224326NEWT:1333499NCBITaxon:79857NEWT:1096976NEWT:5702NEWT:95648NEWT:1589NEWT:135622NEWT:1349NEWT:96731NEWT:383379NEWT:10029NEWT:913645NEWT:44491NEWT:556484NEWT:317447NEWT:4688NEWT:7955NEWT:7959NEWT:2261NEWT:31156NEWT:3112NEWT:4442NEWT:31155NEWT:192875NEWT:1214915NEWT:12637NEWT:59729NEWT:2164133NEWT:108061NEWT:1316931NEWT:224308NEWT:3347NEWT:511145NEWT:931281NEWT:4432NEWT:658457NEWT:1310161NEWT:77133NEWT:295358NEWT:145481NCBITaxon:79824NEWT:2246NCBITaxon:4563NEWT:5755NEWT:44689NEWT:44447NEWT:752555NEWT:498211NEWT:5759NEWT:1736231NEWT:5518NEWT:398007NEWT:1392NEWT:498217NEWT:498216NEWT:2242NEWT:11320NEWT:286NEWT:391619NEWT:246196NEWT:287NEWT:246197NEWT:1367269NEWT:633149NEWT:10239NEWT:44685NEWT:161934NEWT:4897NEWT:1148NEWT:5508NEWT:3329NEWT:5507NEWT:410661NEWT:55571NEWT:35500NEWT:1140NCBITaxon:2157NEWT:1143NEWT:4896NEWT:1287689NEWT:1390NEWT:11557NEWT:1094343NEWT:1462472NEWT:1336795NEWT:644042NEWT:294NEWT:1773NEWT:1182590NEWT:3712NEWT:82380NEWT:3711NEWT:935293NEWT:375146NEWT:2065263NEWT:118698NEWT:1616117NEWT:263NEWT:118696NEWT:52283NEWT:284812NEWT:8175NEWT:43330NEWT:980415NEWT:1603293NEWT:408169NEWT:44664NEWT:47946NEWT:3702NEWT:243277NEWT:7067NEWT:118694NEWT:2850NEWT:118691NEWT:33548NEWT:274NEWT:408172NEWT:408170NEWT:96794NEWT:3708NEWT:332648NEWT:44670NEWT:536231NEWT:376219NEWT:1436733NEWT:460519NEWT:1247411NEWT:572307NEWT:1432138NEWT:1424507NEWT:1194599NEWT:272844NEWT:9483NEWT:333760NEWT:1513458NEWT:1233681NCBITaxon:40559NEWT:506599NEWT:84588NEWT:1679718NEWT:480NEWT:67767NEWT:46835NEWT:109757NEWT:582580NEWT:300852NEWT:1502NEWT:376686NEWT:95486NEWT:508771NEWT:1883446NEWT:253NCBITaxon:2759NEWT:1233435NEWT:93061NEWT:93062NCBITaxon:4932NEWT:644223NEWT:235443NEWT:108458NEWT:272623NEWT:272624NEWT:320637NEWT:2719099NEWT:983964NEWT:118499NEWT:11706NEWT:32644NEWT:527796NEWT:499175NEWT:109779NEWT:3745NEWT:1715989NCBITaxon:4751NEWT:476272NEWT:3747NEWT:195051NEWT:3988NEWT:1255228NEWT:649908NEWT:410289NEWT:373153NEWT:3983NEWT:352472NEWT:1071661NEWT:360094NEWT:470NEWT:41364NEWT:1313NEWT:39491NCBITaxon:5811NEWT:29491NEWT:2014887NEWT:33952NEWT:261756NEWT:571256NEWT:40483NEWT:63366NEWT:63367NEWT:215402NEWT:272634NEWT:9031NEWT:1872122NEWT:7091NEWT:141262NEWT:108931NEWT:1055524NEWT:4087NEWT:9778NEWT:306NEWT:150475NEWT:303NEWT:267872NEWT:7111NEWT:347515NEWT:9534NEWT:5180NEWT:256737NEWT:4090NEWT:4092NEWT:9541NEWT:8694NEWT:4093NEWT:4096NEWT:8692NEWT:185579NEWT:941442NEWT:13076NEWT:1226408NEWT:7108NEWT:40479NEWT:43989NEWT:4076NEWT:317NEWT:1006581NEWT:885318NEWT:39488NEWT:550NEWT:4081NEWT:273068NEWT:554NEWT:98334NEWT:451516NEWT:4084NEWT:63577NEWT:36185NEWT:1225786NEWT:7574NEWT:1715256NEWT:30640NEWT:575412NEWT:929793NEWT:29204NEWT:28112NEWT:114155NEWT:6494NEWT:6491NEWT:507601NEWT:186441NEWT:643680NEWT:214092NCBITaxon:6157NEWT:6239NEWT:162425NEWT:216257NEWT:102169NEWT:9986NEWT:4054NEWT:8654NEWT:8658NEWT:1268063NEWT:8655NEWT:1263854NEWT:118503NEWT:2059687NEWT:160488NEWT:28104NEWT:207559NEWT:407821NCBITaxon:2NEWT:985076NEWT:1215323NEWT:986NEWT:52641NEWT:7159NEWT:28532NEWT:198618NEWT:353152NEWT:8496NEWT:27448NEWT:40674NEWT:1194669NEWT:51329NEWT:243230NEWT:1080772NEWT:519NEWT:8479NEWT:8485NEWT:6063NEWT:49240NEWT:104395NEWT:9557NEWT:6289NEWT:6287NEWT:300641NEWT:727NEWT:9796NEWT:725NEWT:469008NEWT:256318NEWT:9321NEWT:206411NCBITaxon:6191NEWT:596153NEWT:229533NEWT:1836NEWT:2925NEWT:214053NEWT:80863NEWT:90675NEWT:105231NEWT:74649NEWT:52638NEWT:57075NEWT:4097NEWT:8697NEWT:8695NEWT:884204NEWT:9785NEWT:6279NEWT:1123869NEWT:9544NEWT:9545NEWT:7370NEWT:83906NCBITaxon:780NCBITaxon:1502NEWT:6282NEWT:1134506NEWT:255470NEWT:38783NEWT:4006NEWT:6426NCBITaxon:5476NEWT:6669NEWT:9935NEWT:89453NEWT:287889NEWT:1114301NEWT:51515NEWT:588596NEWT:51511NEWT:8845NEWT:92867NEWT:92866NEWT:5334NEWT:51750NEWT:202950NEWT:382352NEWT:413071NCBITaxon:10239NCBITaxon:714NEWT:295027NEWT:632957NEWT:11051NEWT:9925NEWT:89462NCBITaxon:9606NEWT:8839NEWT:90690NEWT:1436183NEWT:4232NEWT:2758385NEWT:11298NEWT:171101NEWT:714NEWT:5322NEWT:421932NEWT:312017NEWT:196627NEWT:200308NEWT:553470NEWT:242507NEWT:200302NEWT:870435NEWT:284593NEWT:100392NEWT:5315NEWT:9913NEWT:265872NEWT:105841NEWT:337330NEWT:2666255NEWT:2285NEWT:999810NCBITaxon:5693NEWT:1392998NEWT:380394NEWT:114796NEWT:981087NEWT:180066NEWT:226900NEWT:231490NEWT:7725NEWT:430615NEWT:563041NEWT:326423NEWT:452467NEWT:198822NEWT:36111NEWT:326424NEWT:1416333NEWT:35024NEWT:135461NEWT:1678078NEWT:749906NEWT:418985NEWT:1817808NEWT:749907NEWT:145263NEWT:69014NEWT:142809NEWT:694569NEWT:27606NEWT:9739NEWT:59202NEWT:9975NEWT:8643NEWT:51953NEWT:3197NEWT:860688NEWT:13443NEWT:8644NEWT:36329NEWT:62615NCBITaxon:3044782NEWT:1333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