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Hawkins"],"technology_type":["Glycoproteomics","Mass Spectrometry","Bottom-up proteomics","MSE"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062381"],"tissue":["Permanent Cell Line Cell"],"sample_protocol":["Glycoproteomics   3 µg of 6 biological replicates of Nipah GM ectodomain were ran on 4-12% Bis-Tris SDS PAGE gel (Invitrogen). Gel bands of interest were extracted and de-stained in 50 mM AmBic 50% MeCN and incubated at 37 °C for 30 mins, before washing in 50 mM AmBic 50% MeCN. Dehydrated gel bands in 100% MeCN then reduced proteins with 10 mM dithiothreitol in 100 mM AmBic and incubated for 30 min at 56°C. Dehydrated gel bands in 80% MeCN for 10 mins at room temperature (RTP). Replaced solution with 50 mM iodoacetamide in 100 mM AmBic and incubated in the dark for 30 mins. Removed liquid and washed gel bands sequentially with 100% MeCN and 50 mM AmBic. Dehydrated gel pieces 100% MeCN then added 12.5 ng/µL protease (trypsin (Promega), chymotrypsin (Promega) or alpha-lytic (New England Bioscience)) in 50 mM AmBic, before incubating at 37°C for 1 hr. Solution was replaced with fresh 50 mM AmBic, incubating at 37°C 18 hrs.  Peptide solution was pooled and sequential washes of 5% (v/v) formic acid (FA) in H2O and MeCN. Samples were dried and reconstituted in 2% MeCN, 0.05% TFA and analysed by LC-MS/MS.  Differential Endoglycosidase treatment with 18O labelling    5 µg of Nipah GM ectodomain was denatured in 4M Urea, 1% SDS for 1hr at RTP. Protein was reduced in 10 mM TCEP (pH 7.5) for 30 mins RTP and labelled with 50 mM IAA in 100 mM AmBic for 30 mins in the dark, RTP. Protein solution was added to 250 µg of 50:50 mix of Speed Bead Magnetic Carboxylate Modified Particles (Cytiva: 65152105050250 and 45152105050250). MeCN was added to a final concentration of ~90% and incubated for 30 mins, 37C, 1000 rpm. A magnetic plate was used to aspirate the supernatant before and during sequential washes of 80% EtOH (x2) and 100% MeCN. Replaced washes with 0.2 µg of trypsin/LysC (Promega) in 50 mM (NH4)HCO3 in H2O and incubated overnight at 37 °C. Peptide solution was kept and 5% DMSO H2O was added to beads for 2 mins, before pooling solution with peptides. Half of the peptides were further treated with 0.2 µg of GluC (NEB) in 50 mM AmBic for 5.5 hrs at 37 °C, after which all peptides were dried. Peptides were resuspended in 50 mM ammonium acetate (pH 5.5) (1000 rpm, 10 mins, 37 °C) before addition of 313 NEB units of Endo-H (New England Bioscience) per sample. Samples were incubated for 1 hr at 37 °C before drying and sealing. PNGase F (New England Bioscience) was lyophilised and resuspended in 50 mM AmBic in H218O before adding to peptides, with a 160 NEB units per sample. Samples were incubated for 30 mins 37 °C before heat inactivation (10 min, 100 °C) and drying. Labelled peptides were reconstituted in 2% MeCN 0.05% TFA and analysed by LC-MS/MS.  HDX-MS analysis of WT, T483A, N481D and WT-EB2 complex   NiVG WT head, T483A and N481D were diluted to 5.9 µM and deuterated PBS (pD 7.4) was added to a deuterium fraction of 88% to initiate the exchange reaction.  At selected time intervals (15 s, 150 s , 1500 s, 15000 s, 24 hrs), a fraction of reaction mixture containing the equivalent of 23 pmol of protein sample was withdrawn and quenched with an ice-cold phosphate buffer containing 2M urea and 40 mM TCEP, which dropped the pH/D to 2.3 and the deuterium fraction to 50%. Quenched samples were kept for 30 s on ice then flash frozen in LN2, and stored at -80 °C before LC-MS analysis. For WT-EB2 complexing, NiVG WT head was incubated in a 1:1.2 molar ratio with ephrin B2 (28-165), or an equivalent volume of PBS. Deuterium labelling was carried out as specified above, and the equivalent of 46 pmol of protein samples were quenched. Maximally labelled samples (MaxD) were produced by labelling NiVG WT head, T483A and N481D at 37 °C in the presence of 4 M deuterated Urea in D2O and 2.4 mM TCEP, keeping the deuterium fraction at 88%. The maximally labelled samples were quenched after 18 hrs with ice-cold phosphate buffer (1.4 % FA) in a similar manner as for the other labelled samples and stored in the same fashion. Timepoints were repeated in triplicate, but duplicates were recorded for WT (mutant analysis) 15 s, WT (ephrin B2 analysis) 1500 s, N481D 150 s, T483A 150 s. For LC-MS analysis, samples were quickly thawed and injected into an Acquity UPLC M-Class System with HDX Technology (Waters), on-line digested at 20 °C into a hand packed pepsin column, prior to online deglycosylation with a PNGAse Rc column5 (Affipro). Peptides were trapped/desalted with solvent A (0.23% formic acid in water) for 4 min at 120 μL/min and at 1 °C through an Acquity BEH C18 VanGuard pre-column (1.7 μm, 2.1 mm × 5 mm, Waters). Peptides were eluted from the trap column into an Acquity UPLC BEH C18 analytical column (1.7 μm, 1 mm × 100 mm, Waters) with a 7 min-linear gradient raising from 8 to 35% of solvent B (0.23% formic acid in acetonitrile) at a flow rate of 40 μL/min and at 1 °C. Eluted peptides went through electrospray ionization in positive mode and underwent MS analysis onto a Synapt-G2 Si, TWIMS-TOF (Waters) with ion mobility separation."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Glycoproteomics Data were analysed in Byos (Protein Metrics). Digestion was set to RK, FYWML and TASV for trypsin, chymotrypsin and alpha-lytic protease digests respectively with maximum of two missed cleavages. Fixed modifications were carbamidomethylation (57.02 Da). And variable modifications were methionine oxidation (15.99 Da) and deamidation (N or Q) (0.98 Da). Byos in-built common human N-linked (132 glycans) and O-linked glycan (6 glycans) glycan libraries were used. FDR was set to 0.01. For analysis, a minimum Byos threshold score of 300 was used for glycopeptide filtering, with the exception of peptides covering site N72 for which a score of 100 was used. Glycopeptides were manually validated, and one peptide sequence per glycosite was chosen as representative for that site (Table S4). For quantification, the extracted ion chromatogram intensities for each glycopeptide of that sequence were summed and plotted relative to the total intensity for each glycosite.    Differential Endoglycosidase treatment with 18O labelling   Data were analysed in Proteome Discoverer (Thermo Fisher Scientific). Digestion was set to RK, and RKED for trypsin or trypsin/gluC protease digests respectively with maximum two missed cleavages. Static modifications werecarbamidomethylation (57.02 Da) and dynamic modifications were methionine oxidation (15.99 Da) and 18O deamidation (N only) (2.98 Da). Strict FDR was set to 0.01. The library searched consisted of the Nipah GM sequence lacking a signal sequence, supplemented with the CRAPome4. The same peptide sequences were used for quantification. For quantification, the extracted ion chromatogram intensities for each peptide of that sequence were summed and plotted relative to the total intensity for each glycosite.    HDX-MS analysis of WT, T483A, N481D and WT-EB2 complex  MSE runs were analysed with ProteinLynx Global Server (PLGS) 3.0 (Waters) and peptides identified in 3 out of 4 replicates, with at least 0.2 fragments per amino acid (at least 2 fragments in total), with mass error below 10 ppm were selected in DynamX 3.0 (Waters). Using both retention time and drift time, spectra of deuterated peptides were matched to the peptide map, and manually annotated to calculate peptide deuterium incorporation."],"omics_type":["Proteomics"],"labhead":["Weston Struwe"],"instrument_platform":[""],"labhead_affiliation":["Biochemistry Department, Kavli Institute for Nanoscience Discovery, University of Oxford, UK"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["tia.hawkins@chem.ox.ac.uk"],"publication":["41713789 Hawkins TÉ, Calvaresi V, Burnap SA, Demyanenko Y, Wu L, Struwe WB. An Evolutionary Distinct Nipah Virus N-Glycosylation Site Provides Stability for Receptor Engagement. Mol Cell Proteomics. 2026 25(4):101531 10.1016/j.mcpro.2026.101531"],"submitter_affiliation":["The Rosalind Franklin Institute & University of Oxford"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Nipah G glycosylation site provides stability for receptor engagement","description":"Nipah virus is a deadly paramyxovirus with 40-75% mortality and >750 cases since 1998. Currently there are no clinically approved vaccines or therapeutics to target infection. Nipah is an enveloped virus with two surface glycoproteins, the trimeric fusion (F) and tetrameric attachment glycoprotein (G). G is responsible for cellular attachment via binding to ephrin B2/B3. Glycosylation of Nipah G and its effects on receptor engagement has not previously been studied but is important as glycosylation impacts immunogenicity, receptor binding and structural conformations for other enveloped virus glycoproteins. Our phylogenetic and mass spectrometry analysis of sitespecific N-glycans of the Nipah G Malaysia strain revealed how N-glycosylation has evolved since the appearance of the virus in 1998. We discovered that the N481 N-glycosite is not conserved and although the glycan does not directly contribute to receptor binding, the threonine/serine in the glycosylation sequon is critical for maintaining long-range stability of individual G subunits that facilitates ephrin B2 binding affinity. Together, these data reveal plasticity of N-glycosylation sites across Nipah species and the presence of hydrogen bonding networks that contribute to G stability and host engagement, which is valuable information for understanding virus attachment/entry mechanisms as well as the rationale design of structure-based vaccines.","dates":{"publication":"2026-03-30","submission":"2025-03-30"},"accession":"PXD062381","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","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: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","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","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: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:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","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: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: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: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","NEWT:219798","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT: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