{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/naive_LPS_IL4_setup.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/naive_LPS_IL4_Report.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/AH-LP3-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/AH-LP3-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/Naive_BR2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/AH-LP3-R4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/Naive_BR1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/Naive_BR3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/AH-LP3-R2.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057739/mouse_swiss_trembl_nov_23.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["j.s.c.arthur@dundee.ac.uk"],"submitter":["Andrew Howden"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057739"],"tissue":["B Cell","Lymph Node"],"sample_protocol":["Liquid chromatography mass spectrometry analysis (LC- MS/MS) Peptides were analysed by single shot data independent acquisition (DIA) as described previously (doi: 10.1038/s41467-023-39046-8, doi: 10.1016/j.isci.2023.106829 and doi: 10.1038/s41598-024-56163-6). 1.5 g of peptides was injected onto a nanoscale C18 reverse-phase chromatography system (UltiMate 3000 RSLC nano, Thermo Scientific) and electrosprayed into an Orbitrap Exploris 480 Mass Spectrometer (Thermo Fisher). The following liquid chromatography buffers were used: buffer A (0.1% formic acid in Milli-Q water (v/v)) and buffer B (80% acetonitrile and 0.1% formic acid in Milli-Q water (v/v). Samples were loaded at 10 μl/min onto a trap column (100 μm × 2 cm, PepMap nanoViper C18 column, 5 μm, 100 Å, Thermo Scientific) equilibrated in 0.1% trifluoroacetic acid (TFA). The trap column was washed for 3 min at the same flow rate with 0.1% TFA then switched in-line with a Thermo Scientific, resolving C18 column (75 μm × 50 cm, PepMap RSLC C18 column, 2 μm, 100 Å). Peptides were eluted from the column at a constant flow rate of 300 nl/min with a linear gradient from 3% buffer B to 6% buffer B in 5 min, then from 6% buffer B to 35% buffer B in 115 min, and finally to 80% buffer B within 7 min. The column was then washed with 80% buffer B for 4 min and re-equilibrated in 3% buffer B for 15 min. Two blanks were run between each sample to reduce carry-over. The column was kept at a constant temperature of 50 °C.   The data was acquired using an easy spray source operated in positive mode with spray voltage at 2.445 kV, and the ion transfer tube temperature at 250 °C. The MS was operated in DIA mode. A scan cycle comprised a full MS scan (m/z range from 350 to 1650), with RF lens at 40%, AGC target set to custom, normalised AGC target at 300%, maximum injection time mode set to custom, maximum injection time at 20 ms, microscan set to 1 and source fragmentation disabled. MS survey scan was followed by MS/MS DIA scan events using the following parameters: multiplex ions set to false, collision energy mode set to stepped, collision energy type set to normalized, HCD collision energies set to 25.5, 27 and 30%, orbitrap resolution 30,000, first mass 200, RF lens 40%, AGC target set to custom, normalized AGC target 3000%, microscan set to 1 and maximum injection time 55 ms. Data for both MS scan and MS/MS DIA scan events were acquired in profile mode."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Proteomics data processing and analysis Data independent (DIA) mass spectrometry raw files were searched using Spectronaut (Biognosys) version 19. Raw mass spec files were searched against a mouse data base (Swissprot Trembl November 2023) with the following parameters: directDIA, false discovery rate set to 1%, protein N-terminal acetylation and methionine oxidation were set as variable modifications and carbamidomethylation of cysteine residues was selected as a fixed modification. Copy numbers and concentration were calculated using the proteomic ruler (Wisniewski et al., 2014) using Perseus software."],"omics_type":["Proteomics"],"labhead":["Professor Simon"],"instrument_platform":[""],"labhead_affiliation":["School of Life Sciences, University of Dundee, Dundee, UK"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["a.howden@dundee.ac.uk"],"publication":["Not available"],"submitter_affiliation":["University of Dundee"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Lipopolysaccharide stimulates dynamic changes in B cell metabolism to promote cell proliferation - naive and LPS data","description":"Following activation, naïve B cells exit quiescence and enter a proliferative phase before becoming mature antibody-producing or memory B cells. One method of activation is to use Lipopolysaccharide (LPS), a well-established B cell mitogen that can drive proliferation ex vivo. Using quantitative proteomics, we identify an upregulation of proteins following LPS stimulation involved in metabolic pathways including amino acid uptake and cholesterol biosynthesis. We highlight the large amino acid transporter SLC7A5 as a target of LPS-induced activation, and by utilising SLC7A5 conditional knockout mice, we demonstrate the requirement of this transporter for B cell proliferation ex vivo. Inhibition of the rate-limiting enzymes HMG-CoA-reductase (HMGCR) and Squalene monooxygenase in the cholesterol biosynthesis pathway significantly reduced proliferation. The role of the cholesterol biosynthetic pathway was not limited to LPS.  Stimulation via TLR7, TLR9, CD40 and the B Cell Receptor also increased cholesterol levels and inhibition of HMGCR reduced proliferation. Together these results suggest a common requirement for metabolic rewiring in B cells to allow proliferation in response to 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