{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_Band3_36kDa_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/21100_E1_TailsP_FullAnalysis_New.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_NS2_A.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_FL_A.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_S2_80kDa_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_S1_15kDa_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_NS1c2_A.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_Band4_28kDa_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_NS1_A.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/iTRAQ_LabelsUsed.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/21100_E1_TailsP_120A.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/21100_E1_TailsP_150A_32.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/21100_E1_TailsP_150B_33.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/21100_E1_TailsP_90A.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_FL.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_NS1c2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_S1_15kDa_1.RAW","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_S2_80kDa_1.RAW","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_NS1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_Band3_36kDa_1.RAW","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/22078_Band4_28kDa_1.RAW","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_E1_PRM_NS2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_PRMassay_B.sky","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_PRMassay_B.sky.view","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074184/24012_PRMassay_B.skyd"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["vernon.ward@otago.ac.nz"],"submitter":["Torsten Kleffmann"],"technology_type":["SRM/MRM","Data-dependent acquisition","Mass Spectrometry","Gel-based experiment","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Norovirus","Protease cleavage","Non-structural polyprotein","Tails"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074184"],"sample_protocol":["Murine norovirus (MNV) Pro, ProPol or ppdko were incubated with soluble RAW264.7 cell lysate at a ratio of 1 µg enzyme to 50 µg lysate in cleavage assay reaction buffer with 5 µg of NS1-2.TM added into each reaction. The reactions were incubated at 37 °C for 17.5 hr. Cleavage products were either analysed by iTRAQ-TAILS as described by Keifeld et al. (Nat Protoc. 2011;6(10):1578-611) or by gel electrophoresis and data-dependent acquisition mass spectrometry as well as parallel reaction monitoring (PRM)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Identification of N-terminal peptides using TAILS iTRAQ-TAILS methodology was performed as described by Keifeld et al. (Nat Protoc. 2011;6(10):1578-611). Murine norovirus (MNV) Pro, ProPol or ppdko were incubated with soluble RAW264.7 cell lysate at a ratio of 1 µg enzyme to 50 µg lysate in cleavage assay reaction buffer with 5 µg of NS1-2.TM added into each reaction. After the reactions were incubated at 37 °C for 17.5 hr, the terminal amines were blocked and labelled with 8-plex iTRAQ reagents. The experiment was performed in duplicate with the following iTRAP labelling: label 113 - Pro replicate 1, label 114 - ProPol replicate 1, label 115 - ppdko replicate 1, label 116 - Pro replicate 2, label 117 - ProPol replicate 2, label 118 - ppdko replicate 2. The labelled peptides were analysed by nanoflow-uHPLC (ultra high-performance liquid chromatography) coupled to a nano-spray source of a 5600+ TripleTOF mass spectrometer (AB Sciex). Therefore, the peptides were separated on an emitter tip column with a gradient increasing from 5% ACN [v/v], 0.1% FA [v/v] to 45% ACN [v/v], 0.1% FA [v/v] to 95% ACN [v/v], 0.1% FA [v/v] in water followed by column washing at 98% ACN and re-equilibration at 5% ACN. The sample was injected in four technical replicates, each running separate liquid chromatography gradients (90, 120 and 2 times 150 min) at 400 nL/min. Over the entire gradient time the mass spectrometer acquired one precursor ion scan followed by 20 fragment ion scans for the 90 and 120 min methods or 30 fragment ion scans for the 150 min method, per acquisition cycle. The fragmentation energy was adjusted for the iTRAQ reporter ion detection.  Results were searched against a murine proteome database with the MNV-1.CW3 NS1-2 sequence added using Proteome Discoverer v.2.2 software (Thermo Scientific). Peptide identification parameters included semi-tryptic peptides with a maximum of two missed cleavage sites, the precursor ion and fragment mass tolerances set to 0.1 Da and the false discovery rate of <1%. DDA and PRM on NS1-2.TM cleavage products separated by SDS PAGE NS1-2.TM was incubated with increasing amounts of ProPol and Pro for 4 hr at 37 °C in reaction buffer containing 10 mM HEPES pH 8, 30% glycerol, 0.1% CHAPs and 2 mM DTT. Reactions were stopped with the addition of an equal volume of 2x SDS-PAGE sample buffer containing 8 M Urea. The samples were visualised on 15% SDS-PAGE with Coomassie brilliant blue G250 stain. To identify where cleavage of the NS1-2.TM occurred, the protein bands corresponding to different cleavage products the full-length NS1-2.TM were excised from the gel and digested in-gel with trypsin. The peptide samples were injected on an in-house packed emitter-tip column filled with Luna™ 3μM C18 beads (Phenomenex) at a flow rate of 400 nL/min using an Ultimate 3000 nano uHPLC-system (Thermo Scientific) and separated by a gradient from 2% [v/v] acetonitrile (ACN), 0.05% [v/v] formic acid (FA) in water to 95% [v/v] ACN, 0.05% [v/v] FA in water over 45 min for data-dependent acquisition tandem mass spectrometry (DIA-MS/MS) or 60 min for targeted parallel reaction monitoring (PRM). DDA-MS/MS was performed on an LTQ Orbitrap XL (Thermo Scientific) and PRM on an Orbitrap Exploris 240 (ThermoScientific) mass spectrometer. For the PRM analysis the tryptic peptide 82VLIFNEWEER91 ([M+2H]2+ = 667.8406) being present in both NS1 and NS1c-2, and the semi-tryptic peptide 67GPLAGLPVTR76 ([M+2H]2+ = 490.7980) specific for the N-terminus of the NS1c-2 fragment were targeted. Data analysis was performed using the Proteome Discoverer software (version 2.5, Thermo Scientific) for DDA-MS/MS data and the Skyline software for PRM data."],"omics_type":["Proteomics"],"labhead":["Vernon Ward"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Microbiology and Immunology, University of Otago, New Zealand"],"species":["Murine Norovirus 1"],"submitter_mail":["torsten.kleffmann@otago.ac.nz"],"publication":["42054099 Ward VK, McKenzie-Goldsmith GM, Edwards MJ, Young VL, Kleffmann T, Stubbing LA, Siow A, Brimble MA. The MNV-1 protease-polymerase precursor cleaves a novel site in the NS1-2 protein. J Gen Virol. 2026 107(4) 10.1099/jgv.0.002263"],"submitter_affiliation":["Department of Biochemistry, University of Otago"],"submitter_country":["New Zealand"],"pubmed_abstract":["Human noroviruses (HuNVs) are members of the <i>Caliciviridae</i> family and are a significant cause of gastroenteritis worldwide. Cell culture models are challenging for studying the intracellular replication of HuNV, with murine norovirus (MNV) routinely used to study norovirus replication. Norovirus genomes contain a non-structural (NS) polyprotein that is processed by the viral protease, generating precursor and mature proteins during replication. We identified a putative viral protease cleavage site at E<sup>66</sup>/G<sup>67</sup> in the MNV-1 NS1-2 protein by sequence analysis that was cleaved by the protease-polymerase (ProPol) precursor but not Pro <i>in vitro</i> and during MNV-1 replication, with the cleavage site confirmed by MS. The P4-P4' LHAE<sup>66</sup>/G<sup>67</sup>PLA cleavage site of MNV-1 is conserved in some MNV strains, while other strains contain a predicted caspase cleavage site (LHAD<sup>66</sup>/G<sup>67</sup>PHA) at this position, indicating that cleavage of NS1 is widely conserved in MNV. Mutation of the ProPol cleavage site in MNV-1 NS1-2 to the caspase motif reduced viral protein expression and replication in Huh7CD300lf and BV2 cells, while removal of the site via an E<sup>66</sup>A mutation caused a 100-fold reduction in viral yield in the naturally permissive BV-2 cell line. This study demonstrates that the protease function of the MNV-1 ProPol precursor has an important role during replication that is distinct to the mature protease and that cleavage of NS1-2 by ProPol at E<sup>66</sup>/G<sup>67</sup> is important for MNV-1 replication."],"pubmed_title":["The MNV-1 protease-polymerase precursor cleaves a novel site in the NS1-2 protein."],"pubmed_authors":["Ward Vernon K VK, McKenzie-Goldsmith Geena M GM, Edwards Matt J MJ, Young Vivienne L VL, Kleffmann Torsten T, Stubbing Louise A LA, Siow Andrew A, Brimble Margaret A MA"],"additional_accession":[]},"is_claimable":false,"name":"The MNV-1 ProPol precursor Cleaves a Novel Site in the NS1-2 Protein","description":"Human noroviruses (HuNV) are members of the Caliciviridae family and are a significant cause of gastroenteritis worldwide. Cell culture models are challenging for studying the intracellular replication of HuNV, with murine norovirus (MNV) routinely used to study norovirus replication. Norovirus genomes contain a non-structural (NS) polyprotein that is processed by the viral protease generating precursor and mature proteins during replication. We identified a putative viral protease cleavage site at E66/G67 in the MNV-1 NS1-2 protein by sequence analysis that was cleaved by the precursor ProPol but not Pro in vitro and during MNV-1 replication. We used mass spectrometry to confirm the cleavage site and the protease activity being specific to ProPol but not Pro. We used the TAILS method (Kleifeld et al. Nat Protoc. 2011;6(10):1578-611) with iTRAQ labelling to identify new N-termini after protease cleavage and data-dependent acquisition mass spectrometry as well as parallel reaction monitoring of tryptically digested gel bands of cleavage products to confirm the new N-terminus at E66/G67 in the MNV-1 NS1-2 protein.","dates":{"publication":"2026-06-08","submission":"2026-02-08"},"accession":"PXD074184","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:1126","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:1367493","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:46429","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:656061","NEWT:37965","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:44250","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:55350","NEWT:1916073","NEWT:1310161","NEWT:1230383","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:99802","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:1549675","NEWT:177437","NEWT:717966","NEWT:9014","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:96795","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:9005","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:215451","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:329032","NEWT:56636","NEWT:2499525","NEWT:55307","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:2830","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:1578","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:278161","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:1092586","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","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