{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LQ_AR_1_Slot2-26_1_10791.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LPAc_CON_2_Slot2-40_1_10835.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LPAc_AR_3_Slot2-38_1_10831.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LQ.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LPAc_CON_1_Slot2-39_1_10833.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LPAc_AR_2_Slot2-37_1_10829.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LQ_CON_2_Slot2-30_1_10796.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LQ_AR_3_Slot2-28_1_10793.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LQ_AR_2_Slot2-27_1_10792.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LQ_CON_3_Slot2-31_1_10797.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LPAc.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LPAc_AR_1_Slot2-36_1_10827.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LPAc_CON_3_Slot2-41_1_10837.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066708/XA04608LQ_CON_1_Slot2-29_1_10795.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["w13834991916@163.com"],"submitter":["Ruikun Wang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["olfactory bulb","lysine acetylation","children","Allergic rhinitis","Allergic rhinitis; children;  olfactory dysfunction; olfactory bulb; lysine acetylation","olfactory dysfunction"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066708"],"tissue":["Olfactory Bulb"],"sample_protocol":["1.Protein extraction, trypsin digestion, and malonylation peptide enrichment Samples were sonicated three times on ice using a high-intensity ultrasonic processor (Scientz) in lysis buffer (8 M urea, 1% Protease Inhibitor Cocktail). (Note: For PTM experiments, inhibitors were also added to the lysis buffer, e.g., 3 μM TSA and 50 mM NAM for acetylation.) The remaining debris was removed by centrifugation at 12,000 × g at 4 °C for 10 min. Finally, the supernatant was collected, and the protein concentration was determined with a BCA kit according to the manufacturer’s instructions. For digestion, the protein solution was reduced with 5 mM dithiothreitol for 30 min at 56 °C and alkylated with 11 mM iodoacetamide for 15 min at room temperature in darkness. The protein sample was then diluted by adding 100 mM NH4HCO3 to a urea concentration less than 2 M. Finally, trypsin was added at a 1:50 trypsin-to-protein mass ratio for the first digestion overnight and a 1:100 trypsin-to-protein mass ratio for a second 4 h digestion. To enrich malonylation-modified peptides, tryptic peptides dissolved in NETN buffer (100 mM NaCl, 1 mM EDTA, 50 mM Tris-HCl, 0.5% NP-40, pH 8.0) were incubated with prewashed antibody beads (PTM-904, PTM Bio) at 4 °C overnight with gentle shaking. Then, the beads were washed four times with NETN buffer and twice with H2O. The bound peptides were eluted from the beads with 0.1% trifluoroacetic acid. Finally, the eluted fractions were combined and vacuum-dried. For LC–MS/MS analysis, the resulting peptides were desalted with C18 ZipTips (Millipore) according to the manufacturer’s instructions. 2. LC–MS/MS analysis of differentially modified proteins The tryptic peptides were dissolved in 0.1% formic acid (solvent A) and directly loaded onto a homemade reversed-phase analytical column (15-cm length, 75 μm i.d.). The gradient comprised an increase from 6% to 23% solvent B (0.1% formic acid in 98% acetonitrile) over 26 min, an increase from 23% to 35% in 8 min, a ramp to 80% in 3 min and then a hold at 80% for the last 3 min, all at a constant flow rate of 400 nL/min on an EASY-nLC 1000 UPLC system. The peptides were subjected to an NSI source followed by tandem mass spectrometry (MS/MS) in a Q ExactiveTM Plus (Thermo) coupled online to the UPLC. The electrospray voltage applied was 2.0 kV. The m/z scan range was 350 to 1800 for the full scan, and intact peptides were detected in the Orbitrap at a resolution of 70,000. Peptides were then selected for MS/MS using an NCE setting of 28, and the fragments were detected in the Orbitrap at a resolution of 17,500. A data-dependent procedure that alternated between one MS scan followed by 20 MS/MS scans with 15.0 s dynamic exclusion. The automatic gain control (AGC) was set at 5E4."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Statistical analysis The resulting MS/MS data were processed using the MaxQuant search engine (v.1.5.2.8). Tandem mass spectra were searched against the Swiss-Prot human database concatenated with a reverse decoy database. Trypsin/P was specified as a cleavage enzyme with allowance of up to 4 missing cleavages. The mass tolerance for precursor ions was set as 20 ppm in the first search and 5 ppm in the main search, and the mass tolerance for fragment ions was set as 0.02 Da. Carbamidomethyl on Cys was specified as a fixed modification, and malonylation modification and oxidation on Met were specified as variable modifications. The label-free quantification (LFQ) method was used, the FDR was adjusted to < 1%, and the minimum score for modified peptides was set to > 40. Gene Ontology (GO) annotation was performed via the UniProt-GOA database (http://www.ebi.ac.uk/GOA/). The GO annotations of proteins are divided into three major categories: biological process, cellular composition and molecular function. Fisher's exact two-terminal test was used to test the enrichment degrees of the differentially expressed proteins in each GO classification against the background of identified proteins. A corrected p value < 0.05 was considered to indicate significance."],"omics_type":["Proteomics"],"labhead":["Ruikun Wang"],"instrument_platform":[""],"labhead_affiliation":["Capital Institute of Pediatrics-Peking University Teaching Hospital"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["w13834991916@163.com"],"publication":["41668279 Wang R, Xu Z, Zhang Y, Wang Q, Li M, Liang J, Zhan X, Lu Y, Yuan J, Wang S, Gu Q. Acetylome Analyses Provide New Insights Into the Effects of Childhood Allergic Rhinitis on Olfactory Bulb-Dependent Olfactory Impairment. Allergy. 2026 81(5):1891-1894 10.1111/all.70254"],"submitter_affiliation":["Capital Institute of Pediatrics-Peking University Teaching Hospital Beijing"],"submitter_country":["China"],"pubmed_title":["Acetylome Analyses Provide New Insights Into the Effects of Childhood Allergic Rhinitis on Olfactory Bulb-Dependent Olfactory Impairment."],"pubmed_authors":["Wang Ruikun R, Xu Ziying Z, Zhang Yimin Y, Wang Qian Q, Li Mengyao M, Liang Jieqiong J, Zhan Xiaojun X, Lu YinXia Y, Yuan Jing J, Wang Shan S, Gu Qinglong Q"],"additional_accession":[]},"is_claimable":false,"name":"Acetylome Analyses Provide New Insights into the Effects of Childhood Allergic Rhinitis on Olfactory Bulb-Dependent Olfactory Impairment","description":"Background: Allergic rhinitis (AR) is a global health burden affecting 20% of the pediatric population and is characterized by nasal inflammation and frequent olfactory dysfunction. Protein acetylation, which is a frequently occurring posttranslational modification, plays pivotal roles in the regulation of olfactory bulb (OB) function. However, the role of lysine acetylation in OB pathophysiology in pediatric AR-induced olfactory dysfunction remains unexplored. Methods: In this cross-sectional study, we enrolled pediatric patients (7–18 years) diagnosed with AR and age-matched healthy controls from the Children's Hospital affiliated with the Capital Institute of Pediatrics. Olfaction was assessed using the Universal Sniff (U-Sniff) test. An ovalbumin-induced AR mouse model was established. Olfactory function was assessed via buried food and odor discrimination tests. Proteomic and acetylomic profiling of OB tissue was performed using LC‒MS/MS, with bioinformatic analyses (GO, KEGG, STRING PPI, Motif). Key acetylation enzymes were validated by immunohistochemistry. Results: A total of 162 children in the AR and healthy groups were included in this study. A decreased score on “U-Sniff” and a greater incidence of olfactory dysfunction were observed in the AR group than in the healthy group (p<0.0001). AR model mice presented severe nasal symptoms, elevated sIgE levels, and significant olfactory deficits in odor detection and discrimination. Proteomic results revealed that the expression of proteins involved in glycolysis/gluconeogenesis and propanoate metabolism was significantly dysregulated. Critically, we observed dysregulation of key acetylation-modifying enzymes, characterized by reduced expression of the acetyl-CoA generator ACSS2 and deacetylase SIRT1, alongside elevated levels of acetyltransferase P300 and deacetylase HDAC2. Global acetylome profiling revealed 3,875 lysine acetylation sites across 1,707 proteins, indicating predominant hyperacetylation (436 significantly upregulated sites on 319 proteins versus 42 downregulated sites). These acetylated proteins disrupted olfactory transduction, the synaptic vesicle cycle, the citrate cycle (TCA cycle), glycolysis/gluconeogenesis, and propanoate metabolism. Our findings provide critical insights into how nasal inflammatory processes disrupt protein acetylation networks in the olfactory bulb, advancing our understanding of the molecular basis for smell disorders in children and informing future targeted interventions.","dates":{"publication":"2026-06-08","submission":"2025-07-29"},"accession":"PXD066708","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","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:460523","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","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:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","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:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","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:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","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:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:13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