{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_3_peptides.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_2_peptides.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Legumin_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Legumin_2_peptides.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Legumin_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Legumin_3_peptides.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Legumin_1_peptides.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_2_CID_30eV_291.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_1_22eV_279.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Legumin_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_1_peptides.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Vicilin_Search.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD078377/Legumin_Search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["vcunsolo@unict.it"],"submitter":["Vincenzo Cunsolo"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Top-down proteomics","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Orbitrap® mass spectrometry","N-glycosylated plant proteins","Bottom-up and top-down approaches","Chickpea proteins proteolysis","Legumins and vicilins"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD078377"],"sample_protocol":["The chickpea flour was defatted using hexane of analytical grade to eliminate the lipid fraction from the chickpea flour by solvent extraction at a ratio of 1:3 weight: volume (flour: solvent). The legumin and vicilin-enriched fractions were extracted from the defatted chickpea flour as reported by Chang et al. 2022 with some modifications. The extraction was carried out in the presence of cOmplete Protease Inhibitor Cocktail, aimed to protect proteins from aminopeptidases, metalloproteases, and serine, cysteine, and aspartic acid proteases. An aliquot corresponding to 50 µg of both enriched-protein fractions of vicilins and legumins was suspended in bicarbonate buffer (50 mM, pH 8), reduced, and alkylated as previously reported by Di Francesco et al. 2021. The aliquot for top-down analysis and for bottom-up analysis were dried in a speed vacuum and finally suspended in 2% FA. LC-MS/MS analyses of the peptide mixtures were carried out on a ThermoFisher Scientific Orbitrap Lumos Tribrid® mass spectrometer (ThermoFisher Scientific, Bremen, Germany) coupled with a ThermoFisher Scientific EASY-nLC 1000 system (Sunnyvale, CA) liquid chromatography. A total of 5 µL of the peptide mixture were loaded into a homemade pre-column packed with ReproSil-Pur 120 C18-AQ, (75 µm i. d. x 5 cm, 5 µm particle size, 120 Å) [29] and after separated by a homemade analytical-column packed with Reprosil-Pur 120 C18-AQ (75µm i.d. x 24 cm, 3 µm particle size, 120 Å) [29]. Elution was carried out at a flow rate of 300 nL/min by a linear gradient of solvent B (ACN+0.1%FA) in the solvent A (H2O+0.1%FA). Peptides were mass analyzed and sequenced by electrospray ionization using a heated ion transfer tube (275 °C). Survey scans of peptide precursors from 200 to 1700 m/z were performed at 120 K resolution (@ 200 m/z). Tandem MS was performed by isolation at 1.6 m/z with the quadrupole, HCD fragmentation with a normalized collision energy of 30, and high-resolution MS analysis of fragments in the Orbitrap (50 K resolution). Only those precursors with charge states 2-4 and intensity above the threshold of 5000 were sampled for MS2. The dynamic exclusion duration was set to 20 s with a 10 ppm tolerance around the selected precursor and its isotopes. Monoisotopic precursor election was turned on. The instrument was running top speed mode with 3 s cycles, meaning it would continuously perform MS2 events until the list of non-excluded precursors diminished to zero or 3 s, whichever is shorter. Top-down mass spectrometry analysis of the enriched vicilin protein fraction was carried out on a Thermo Fisher Scientific Orbitrap Fusion Lumos mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) coupled online with the Thermo Scientific EASY-nLC 1000 nanosystem (Sunnyvale, CA, USA). In detail, 2 μL of the reduced and alkylated vicilin-enriched fraction were loaded onto a homemade C4 column packed with ReproSil-Pur 100 C4 (100 μm i.d. x 25 cm, 1.8 μm particle size, 100 Å) [29]. The proteins were separated by elution at a flow rate of 250 nL/min at room temperature by a linear gradient of solvent B (ACN+0.1%FA) in the solvent A (H2O+0.1%FA). Proteins were analyzed by electrospray ionization using a heated ion transfer tube (275 °C). Mass spectra of all the precursor ions were acquired at 120 K resolution at m/z 200, in the range m/z 200-1800. MS/MS analyses were performed by CID fragmentation with a normalized collision energy of 30, and the MS fragment ions were analyzed in the Orbitrap (high-resolution MS/MS analysis) at 60 K resolution in cycle time mode set to 3s. Top-down analysis of the enriched legumin protein fraction was carried out in duplicate on Orbitrap Fusion Tribrid  (ThermoFisher Scientific, Bremen, Germany) coupled online with the UHPLC ThermoFisher Scientific Dionex UltiMate 3000 RSLCnano system (Sunnyvale, CA). In detail, 1 μL of the reduced and alkylated protein fraction, corresponding to 5 ng, was injected into an Easy-Spray PepMap HPLC capillary column C4 (1500 Å, 4 µm, 150 µm x 150 mm). The proteins were separated by elution at a flow rate of 800 nL/min, at 40 °C, by a linear gradient of solvent B (ACN+0.1%FA) in the solvent A (H2O+0.1%FA). Eluted proteins were converted to gas-phase by electrospray ionization, source voltage 1.3 kV, and introduced into the mass spectrometer through a heated (275 °C) ion transfer tube. Mass spectra of all the precursor ions were acquired in a range from 200 to 1800 m/z at a resolution of 120K (@ 200 m/z) using the following parameters: RF lens, 80%; Auto Gain Control: 200000; maximum injection time, 100 ms. Top-down MS/MS (TD-MS2) analyses were performed by HCD fragmentation at a normalized collision energy of 10, 12, 15, and 22, and by CID fragmentation at a normalized collision energy of 30. MS fragment ions were analyzed in the Orbitrap (high-resolution MS/MS analysis) at 120 K resolution in cycle time mode set to 3s."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The peptide-level LC-/MSMS data were processed by PEAKS Xpro de novo sequencing software (Bioinformatics Solutions Inc., Waterloo, ON, Canada; https://www.bioinfor.com//), which provides automated and accurate de novo peptide sequencing. The de novo amino acid sequences generated by PEAKS were searched against a custom protein database, including only the eighteen legumins and vicilins entries of Cicer arietinum L. (chickpeas) downloaded from the UniProt database (release May 2025). The database search was carried out setting trypsin as a proteolytic enzyme, semispecific as digestion mode, and 3 as the maximum number of allowed missed cleavages. In the first step of the database search, carbamidomethylation of cysteines was set as a fixed modification, whereas the oxidation of methionine, the acetylation (N-terminal protein), formylation, and the transformation of N-terminal glutamine and N-terminal glutamic acid residue into the pyroglutamic acid form were considered as variable amino acid modifications. The de novo amino acid sequences unmatched during the first round of the database search were searched, enabling the PEAKS PTM tool to identify as additional modifications the methionine dioxidation, cysteine dioxidation, and cysteine trioxidation. Database search was carried out, setting the precursor mass tolerance threshold at 10 ppm and the max fragment mass error at 0.006 Da. Peptide Spectral Matches (PSMs) were validated using a Target Decoy PSM Validator node based on q-values at a False Discovery Rate (FDR) ≤ 1%. PEAKS score thresholds for PSMs were set to achieve FDR values below 1% for PSMs, Peptide sequences, and Proteins identified from each database search. For both samples analyzed using the shotgun approach, the relative abundance of each identified protein was determined. The Full scan MS and MS/MS data obtained from the top-down analyses were initially processed by the MASH Native software in ‘Discovery mode’ (Ge Research Group, University of Wisconsin-Madison) and searched against a protein database including all the reviewed and unreviewed entries of Cicer arietinum L. (chickpea) of the UniProt database (Swiss-Prot and TrEMBL sections, release February 2023, 31239 entries). This preliminary database search aimed to find what kind of proteins were present in the sample under investigation. The database searches were carried out using the TopFD as a deconvolution algorithm and the TopPIC as a Database Search algorithm. The number of unexpected PTMs was set to 1, the precursor mass tolerance threshold was set to 15 ppm, whereas the max fragment mass error was set to 0.020 Da. Then, to validate the results, a Decoy Database Searching was carried out, with a Spectrum Cutoff value based on E-Value set to 0.01. Finally, a freely available tool coined ClipsMS (Comprehensive Localization of Internal Protein Sequences) (https://github.com/loolab2020/ClipsMS-Version-1.0.0) [30], and developed to assign both terminal and internal fragments resulting from a top-down mass spectrometry experiment, was used to in-depth characterize the sequence of each polypeptide detected and identified in the preliminary database search. In detail, the raw MS/MS spectra obtained by CID fragmentation of polypeptides were first deconvoluted using the Xtract® deconvolution algorithm (Thermo Scientific); then, every deconvoluted mass list was uploaded into the ClipsMS program together with the selected sequence entry to obtain a matched fragments list. The error for fragment matching was set at 10 ppm, and the smallest internal fragment size was set at 5 amino acids. All the terminal fragments were assigned before considering internal fragments. Then, only “by” internal fragments were searched for and used as putative candidates of uninterpreted signals. The possible existence of many theoretical fragments with overlapping masses introduces a high risk of false-positive annotation. To prevent false-positive assignments , after the matching process, all putative “by” internal fragment assignments were manually verified, and the following criteria were applied: (i) the putative internal fragments were real peaks rather than noise or isotopes; (ii) when both a terminal and an internal fragment matched the same peak, the terminal fragment was the preferential assignment; (iii) when two terminal fragments matched the same peak, the internal fragment with the lower mass error was selected; (iv) when two terminal fragments matched the same peak with identical mass error, both assignments were reported; however, whenever possible, preference was given to cleavages occurring N-terminal to proline and C-terminal to acidic residues. The last criterion was adopted because it is well known that in the fragmentation of peptides and whole proteins, fragment ions produced N-terminal to proline (proline effect) and cleavage C-terminal to acidic residues, mainly aspartic acid, are over-represented in the MS/MS spectra."],"omics_type":["Proteomics"],"labhead":["Vincenzo Cunsolo"],"instrument_platform":[""],"labhead_affiliation":["Laboratory of Organic Mass Spectrometry, Department of Chemical Sciences, University of Catania"],"submission_type":["PARTIAL"],"species":["Cicer Arietinum (chickpea) (garbanzo)"],"publication":["42213123 Di Francesco A, Lanzoni A, Pittalà MGG, Saletti R, Jensen ON, Cunsolo V. Proteoform analysis by mass spectrometry reveals post-translational processing of legumins and vicilins in chickpeas (Cicer arietinum L.). Anal Bioanal Chem. 2026 10.1007/s00216-026-06577-0"],"submitter_mail":["vcunsolo@unict.it"],"submitter_affiliation":["University of Catania"],"submitter_country":["Italy"],"pubmed_abstract":["The most abundant proteins in pulse seed, including chickpea (Cicer arietinum L.), are the 7S globulins (vicilins) and 11S globulins (legumins), which play key roles in plant reproduction and human nutrition and are also recognized as potential allergens. During seed maturation, legumins and vicilins undergo limited proteolysis. Legumins are processed into α- and β-polypeptide chains that remain linked by a disulfide bond, whereas vicilins are cleaved at two sites, generating three lower-molecular-mass polypeptides (α-, β-, and γ-chains). An integrated mass spectrometry approach, combining bottom-up and top-down strategies, was applied to characterize the post-translational processing of legumins and vicilins. Our data suggest that (i) proteolytic cleavages in both legumins and vicilins occur at conserved sequence motifs; (ii) legumin processing is catalyzed by an asparaginyl endopeptidase, whereas vicilin processing is mediated by legumains, a family of cysteine endopeptidases; and (iii) one chickpea vicilin is N-glycosylated and carries a high-mannose oligosaccharide side chain. Limited proteolysis process represents a key physiological mechanism regulating storage protein assembly, stability, and mobilization during seed development and germination while preserving storage functions. Glycosylation of vicilins further modulates their structural and functional properties, although it may also influence digestibility and allergenic potential. The mass spectrometry data have been deposited with the ProteomeXchange with the identifier <PXD078377>."],"pubmed_title":["Proteoform analysis by mass spectrometry reveals post-translational processing of legumins and vicilins in chickpeas (Cicer arietinum L.)."],"pubmed_authors":["Di Francesco Antonella A, Lanzoni Aldo A, Pittalà Maria Gaetana Giovanna MGG, Saletti Rosaria R, Jensen Ole N ON, Cunsolo Vincenzo V"],"additional_accession":[]},"is_claimable":false,"name":"Proteoform analysis by mass spectrometry reveals post-translational processing of legumins and vicilins in chickpeas (Cicer arietinum L.)","description":"The most abundant proteins in pulse seed, including chickpea (Cicer arietinum L.), are the 7S globulins (vicilins) and 11S globulins (legumins), which play key roles in plant reproduction and human nutrition and are also recognized as potential allergens. During seed maturation, legumins and vicilins undergo limited proteolysis. Legumins are processed into α- and β-polypeptide chains that remain linked by a disulfide bond, whereas vicilins are cleaved at two sites, generating three lower-molecular-mass polypeptides (α, β, and γ chain). An integrated mass spectrometry approach, combining bottom-up and top-down strategies, was applied to characterize the post-translational processing of legumins and vicilins. Our data suggest that: (i) proteolytic cleavages in both legumins and vicilins occur at conserved sequence motifs; (ii) legumin processing is catalyzed by an asparaginyl endopeptidase, whereas vicilin processing is mediated by legumains, a family of cysteine endopeptidases; and (iii) one chickpea vicilin is N-glycosylated and carries a high-mannose oligosaccharide side chain. Limited proteolysis process represents a key physiological mechanism regulating storage protein assembly, stability, and mobilization during seed development and germination while preserving storage functions. Glycosylation of vicilins further modulates their structural and functional properties, although it may also influence digestibility and allergenic potential.","dates":{"publication":"2026-06-01","submission":"2026-05-14"},"accession":"PXD078377","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:37003","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903"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