{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD073688/metadata.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD073688/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD073688/Search_output_Slice.parquet","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD073688/DistalColon_metaP.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD073688/ProximalColon_metaP.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD073688/Search_output_DIA.parquet"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["manuela_schmidt@univie.ac.at"],"submitter":["Feng Xian"],"technology_type":["Mass Spectrometry","Data-independent acquisition","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Metaproteomics","Pasef"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD073688"],"tissue":["Colon","Feces"],"sample_protocol":["For protein preparation, ~30 mg of fecal samples were mixed with 200 μL of lysis buffer (5% SDS, 2M Urea, 50mM Tris-HCl, Protease Inhibitor 1x) and vortexed vigorously for 1 min. Following, samples were placed in a Thermomixer (Serial Number: 5382JR638726, Eppendorf, Hamburg, Germany) for 15 minutes at 1,200 rpm and 70°C. When finished, samples were ultrasonicated using a Bioruptor Pico (Diagenode, Seraing, Belgium; program: 15 cycles of 30 seconds “ON” and 30 seconds “OFF”, frequency level: Low, water temperature: +20°C). Afterwards, tubes were centrifuged at 16,000 g for 5 minutes at room temperature. Supernatants were saved in new tubes and submitted to a new round of centrifugation. The saved supernatants were stored at -80°C until SP3-assisted protein digestion.  For protein clean-up and digestion, a modified version of the single-pot, solid-phase-enhanced sample preparation (SP3) method from Hughes et al. was used(27). Briefly, 50 µg protein was taken into a 1.5 mL LoBind tube (Eppendorf, Hamburg, Germany), and the sample volume was added up to 50 µL with lysis buffer. The fecal sample was subjected to protein reduction (5 mM Dithiothreitol, DTT, 30 minutes incubation at +60°C) and alkylation (20 mM Iodoacetamide, IAA, 30 minutes at room temperature in the dark). The remaining IAA in the sample was quenched with the addition of DTT to a final concentration of 5 mM. 10 µL of pre-mixed Sera-Mag SpeedBead beads (50 mg/ml, Cytiva, Marlborough, Massachusetts) were added to 50 µg protein sample. To initiate the binding of proteins to the beads, one volume of absolute ethanol was added immediately, followed by incubation on a Thermomixer (Eppendorf) at 24°C for 5 minutes with 1,000 rpm agitation. The supernatant was removed after 2 minutes resting on a magnetic rack, and the beads were rinsed three times with 500 μL of 80% ethanol. Rinsed beads were reconstituted in 50 μL digestion buffer (50 mM ammonium bicarbonate, pH 8). Protein digestion was performed with 2 μg of sequencing-grade trypsin/LysC (Promega, Madison, USA) for 18 hours at 37°C with 950 rpm agitation. After digestion, ACN was added to each sample to a final concentration of 95%. Mixtures were incubated for 8 minutes at room temperature and then placed on a magnetic rack for 2 minutes. The supernatant was discarded, and the beads were rinsed with 900 μL of 100% ACN. Rinsed beads were reconstituted in 20 μL LC-MS grade water to elute the peptides. The peptide concentration was measured in duplicate using NanoPhotometer N60 (Serial number: TG2022, Implen, Munich, Germany) at 205 nm. Peptide samples were acidified with FA to a final concentration of 0.1% and stored at -20°C until LC-MS/MS analysis."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["To generate a sample-specific microbial database for the colonic samples, we followed the recently published strategy of novoMP22. Briefly, a total of 60 µg pooled peptides (from both proximal and distal regions) were fractionated (Fisher Scientific, Cat. 84868) according manufactures instruction. Eight peptide factions were dried using vacuum centrifugation and then re-suspended in 30 µL of MS-grade water. The peptide concentration was measured in duplicate using NanoPhotometer N60 (Implen, Munich, Germany) at 205 nm. Peptide samples were acidified with formic acid to a final concentration of 0.1% and were stored at -20°C until LC-MS/MS analysis. 50 ng of each peptide fraction (a total of 8 fractions) were loaded on an AuroraTM ULTIMATE column (25 cm x 75 µm) packed with 1.6 µm C18 particles (IonOpticks, Fitzroy, Australia) with a total separation time of 60 minutes in DDA-PASEF mode.  The TIMS analyzer was operated in a 100% duty cycle with equal accumulation and ramp times of 100 ms each. Specifically, 10 PASEF scans were set per acquisition cycle (cycle time of 1.17 s) with ion mobility range from 0.7 to 1.3 (1/k0). The target intensity and intensity threshold were set to 20000 and 500 respectively. Dynamic exclusion was applied for 0.4 minutes. Ions with m/z between 100 and 1700 were recorded in the mass spectrum. Collision energies were dependent on ion mobility values with a linear increase in collision energy from 1/K0 = 0.6 Vs/cm² at 20 eV to 1/K0 = 1.6 Vs/cm² at 63 eV. Fractionated DDA files were submitted to MSfragger35 (version 4.3) integrated in FragPipe computational platform (version 23.1), searching against the MGnify mouse gut protein catalogue (https://www.ebi.ac.uk/metagenomics/genome-catalogues/mouse-gut-v1-0). The decoy database was generated with reversed sequences. Trypsin was specified with a maximum of two missed cleavages allowed. The search included variable modifications of methionine oxidation and N-terminal acetylation and a fixed modification of carbamidomethyl on cysteine. The mass tolerances of 20 ppm were set for precursor and fragment. Peptide length was set to 7 to 50 amino acids with a mass range from 500 to 5000 Da. The remaining parameters were kept as default settings. During the validation, MSBooster (version 1.3.17) was used for rescoring and Percolator37 (version 3.7.1, default parameters) was used for PSM validation. FDR level was set to 1% for PSM, peptide and protein. The identified proteins from the search formed a sample-specific protein database, containing 97249 protein sequences. In addition, DDA raw files were subjected to de novo sequencing as previously described 22. As a result, a total of 232863 protein sequences were included in the microbial database. This database was combined with the standard Mus musculus proteome (https://www.uniprot.org/proteomes/UP000000589, accessed on 2023-04-27) to process acquired datasets. pooled peptide samples (generated by combining all proximal or distal colon samples) were repeatedly analyzed using both DIA- and Slice-PASEF to monitor LC–MS performance and to support generation of a sample-specific experimental spectral library. In addition, fractionated pooled samples were acquired in DIA-PASEF mode to further increase spectral coverage. These datasets were processed using DIA-NN (v2.3.0) with a predicted library comprising 26,374,776 precursors derived from a reduced microbial database (232,863 protein sequences), the standard Mus musculus proteome (UniProt UP000000589, accessed 2023-04-27), and DIA-NN contaminant sequences. Trypsin/P digestion was specified with a maximum of one missed cleavage and N-terminal methionine excision enabled. Carbamidomethylation of cysteine was used as a fixed modification, while methionine oxidation and N-terminal acetylation were allowed as variable modifications, permitting a maximum of one variable modification per peptide. Peptide length was restricted to 7–30 amino acids, precursor m/z values were set to 250–1200 with charge states of 2–3, and fragment ions were considered between 100 and 1700 m/z. Proteotypicity was set to “Isoform IDs,” and protein inference was disabled. The resulting experimental spectral library contained 184,884 precursors corresponding to 85,044 protein groups and was used for DIA- and Slice-PASEF analysis of individual samples."],"omics_type":["Proteomics"],"labhead":["Manuela Schmidt"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Division of Pharmacology & Toxicology, Department of Pharmaceutical Sciences, Faculty of Life Sciences, University of Vienna"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["feng.xian@univie.ac.at"],"submitter_affiliation":["Division of Pharmacology and Toxicology, Department of Pharmaceutical Sciences, University of Vienna"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"Systematic evaluation of PASEF acquisition strategies in complex metaproteomes","description":"Trapped ion mobility spectrometry coupled with parallel accumulation–serial fragmentation (PASEF) has enabled multiple acquisition strategies for proteomics, yet their comparative performance in complex metaproteomes remains unclear. Here we benchmark five modes—DDA-, DIA-, Slice-, Synchro- and midia-PASEF (PentaPASEF)—using human fecal samples spiked with defined bacterial references across three chromatographic gradients and input levels, comprising 540 LC–MS acquisitions. DIA-based strategies consistently delivered greater peptide and protein coverage than DDA-PASEF, particularly for low-abundance microbial features, and maintained stable performance under high-throughput conditions. Slice- and DIA-PASEF provided the lowest quantitative variability, minimal ratio compression and the most consistent species-level abundance scaling, while functional analysis revealed expanded dynamic range for DIA-based methods. Biological validation in a murine colonic epithelial injury model showed that DIA- and Slice-PASEF capture concordant host and microbial responses. This study establishes a unified reference for selecting PASEF acquisition strategies for sensitive and reproducible metaproteomics.","dates":{"publication":"2026-07-03","submission":"2026-01-28"},"accession":"PXD073688","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","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:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:109376","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","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:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:305400","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:32224","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:3710","NEWT:65125","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:32201","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:3707","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:2709072","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:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:1195466","NEWT:2483192","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:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","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:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","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:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","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: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