{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357_Ainslie.msf"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/PC1357_metadata.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_Pool_r1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_9_r2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/20241017_PHCOQEHF_PC1357-Ainslie_Pool_r2.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077329/Uniprot_Bos_taurus_UP000009136_rev_unrev_37Kseq_May2024.FASTA"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ainsliek@email.unc.edu"],"submitter":["Scott Lyons"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Dextran","Microparticle","Complement","Protein corona"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077329"],"sample_protocol":["Proteomics Sample Preparation Samples were dried down via vacuum centrifugation, then resuspended to 1 µg/µl in 1M urea, 50 mM ammonium bicarbonate. For each sample, 25 µg of protein lysate was reduced with 5 mM DTT at 37°C for 45 min and alkylated with 15 mM IAA at room temperature for 45 min. Samples were then digested with 2 μL of 0.5 mAU/mL LysC for 2 hours at 37 °C, followed by an overnight digestion with 4 ug of trypsin incubated in a thermomixer at 37°C, shaking at 400rpm. The resulting peptides were acidified to 0.5% trifluoroacetic acid (TFA) and desalted using Pierce desalting spin columns using manufacturer's recommendations. Eluates were dried via vacuum centrifugation and resuspended in 2% acetonitrile with 0.1% formic acid prior to determining peptide concentration using the Pierce Quantitative Fluorometric Assay. All samples were normalized to 0.1 μg/μl and subjected to LC-MS/MS analysis.   LC-MS/MS  The peptide samples were analyzed by LC-MS/MS using an Easy nLC 1200 coupled to a QExactive HF mass spectrometer (Thermo Scientific). Samples were injected onto an Easy Spray PepMap C18 column (75 μm id × 25 cm, 2 μm particle size) (Thermo Scientific) and separated over a 2 hr method. The gradient for separation consisted of a 107-minute linear gradient from 5–48% mobile phase B (MPB) at a 250 nl/min flow rate, and a constant 100% MPB for 13 minutes, where mobile phase A was 0.1% formic acid in water and mobile phase B consisted of 0.1% formic acid in 80% ACN. The QExactive HF was operated in data-dependent mode, where the 15 most intense precursors were selected for subsequent fragmentation. Resolution for the precursor scan (m/z 350–1700) was set to 60,000, while MS/MS scans resolution was set to 15,000. The normalized collision energy was set to 27% for HCD. Peptide match was set to preferred, and precursors with unknown charge or a charge state of 1 and ≥ 7 were excluded."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data analysis Raw data files were searched against the Uniprot reviewed and unreviewed Bos taurus database (containing 37,506 entries, downloaded May 2024), using the Sequest HT search engine node within Proteome Discoverer (v3.1, Thermo Fisher). Enzyme specificity was set to trypsin, up to two missed cleavage sites were allowed, methionine oxidation and N-terminus acetylation were set as variable modifications, and cysteine carbamidomethylation was set as a static modification. Acetylation, Methionine loss, and Methionine loss + acetylation were set as variable modifications on the protein terminus. The Minora node was used to extract label-free quantification (LFQ) intensities. A 1% peptide-level false discovery rate (FDR) and a 5% protein-level FDR was used to filter all data. Match between runs was enabled. Proteins were filtered out if there was no quantification in at least one sample. Statistical analysis was performed in Perseus software (version 1.6.14.0). Imputation was performed by drawing random numbers drawn from a normal distribution downshifted 1.8 with a width of 0.3. P-values were calculated using a two-sided Student’s T-test."],"omics_type":["Proteomics"],"labhead":["Kristy Ainslie"],"instrument_platform":[""],"labhead_affiliation":["Division of Pharmacoengineering and Molecular Pharmaceutics, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill"],"submission_type":["PARTIAL"],"species":["Bos Taurus (bovine)"],"submitter_mail":["scott_lyons@med.unc.edu"],"publication":["Not available"],"submitter_affiliation":["UNC Chapel Hill"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Complement proteins enriched in dextran-based microparticle","description":"Autoimmunity affects ~10% of the global population. Current therapies suppress protective immunity and are non-curative. Antigen-specific therapies can selectively suppress autoreactive cells, preserving protective immunity. B cell dysregulation, a major driver of autoimmunity, remains largely untargeted. We hypothesized that targeting B cells with antigen-loaded microparticles enhances therapeutic efficacy. Here, we demonstrate that antigen-loaded acetalated dextran microparticles (AMP) surface-associate with B cells and enhance IL-10 secretion and MHCII expression, promoting tolerogenic antigen presentation. Leveraging this property, we developed a therapy using myelin oligodendrocyte (MOG35-55) peptide-loaded AMPs associated with B cells (MOG-AMP-B). Administering MOG-AMP-Bs in a late therapeutic model of multiple sclerosis resulted in unprecedented recovery, reducing central nervous system (CNS) inflammation, downregulating activated dendritic cells and macrophages and increasing regulatory T- and B cells. MOG-AMP-Bs did not reduce the ability of animals to respond to a viral infection, representing a highly effective antigen-specific therapy for restoring immune balance in autoimmunity. This study includes proteomics on the AMP particles after serum exposure, identifying complement proteins enriched on its protein 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