{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_170-O_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_170-PW_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_156-O_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_166-O_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_156-HL_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_165-O_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_165-MA_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_166-HL_800ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_Y1-C_300ng_180min_Wat25cmBEH_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/20230211_jcl_NVijayan_Nyholm_Y1-MD_300ng_180min_Wat25cmBEH_1.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/jlb20201207_NVijayan_E_Scolopes_peptides.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/jlb20200304_McAnulty20180723EupfinalDB_plus_Uniprot-proteome_Octopusbimaculoides_UP000053454_updated2019Dec01.fasta"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/mzTab.mzTab"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/MaxQuant_1_6_10_43.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074352/combined.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jeremy.balsbaugh@uconn.edu"],"submitter":["Jen Liddle"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Symbiosis","Metabolomics","Proteomics","euprymna scolopes","magnetic nanoparticles","Symbiosis; euprymna scolopes","Hemocytes","Hemocytes; magnetic nanoparticles"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074352"],"tissue":["Hemocyte"],"sample_protocol":["For untargeted proteomic analysis, subsets of pelleted cells from two hemocyte treatment groups (n = 5 biological replicates each) (i.e., untreated hemocyte controls and hemocytes exposed to MNPs) were extracted in triplicate by adding 1X lysis (5% SDS, 50 mM triethylammonium using a BCA Assay. Proteomic analysis was conducted at the Proteomics and Metabolomics Facility at the University of Connecticut. The ten samples were suspended in 2 mM MgCl2 and then treated with benzonase for 15 min on ice. Next, samples were dried, resuspended in 10% SDS, and processed with S-Trap columns (ProtiFi, LLC, Fairport, NY) before incubating for 1 h at 25°C with dithiothreitol, alkylated in the dark with iodoacetamide for 30 min at 25°C, acidified with phosphoric acid, and finally diluted at 1 1:6 ratio with binding/wash buffer containing 90% methanol and 100 mM TEAB. Samples were loaded onto S-trap micro columns, washed 4x with binding/wash buffer, and digested at 25°C overnight with trypsin/LysC at 1:10 enzyme:protein (w/w, Promega #V5073). Elution of peptides was carried out using a series of washes: first with 50 mM ammonium bicarbonate, followed by 0.2% formic acid in water, and finally with 0.2% formic acid in 50% acetonitrile. The resulting peptides were thoroughly dried and desalted by reverse-phase chromatography with Pierce peptide desalting spin columns (Thermo Fisher, Waltham, MA). After another drying step, peptides were reconstituted in Solvent A containing 0.1% formic acid in Optima LC/MS grade water (Fisher Chemical, Pittsburgh, PA). The peptide concentrations in each sample were determined spectrophotometrically (A280 nm), and sample injection volumes were adjusted to ensure equal amounts were analyzed.  Analysis was performed using a Thermo Scientific Ultimate 3000 RSLCnano UPLC system in tandem with a high-resolution Thermo Scientific Eclipse Tribrid Orbitrap mass spectrometer. Individual samples were introduced to a nanoEase M/Z Peptide BEH C18 column (Waters Corporation, Milford MA) and separated over 150 min under reversed-phase conditions with a 4-30% gradient of Solvent B  containing 0.1% formic acid in Optima LC/MS grade acetonitrile followed by an increase to 30-90% Solvent B during a subsequent 30-min ramp, totaling 180 min of gradient separation using a flow rate of 300 nL per min.  Peptide elution proceeded by nanoflow electrospray ionization in the positive mode at a capillary voltage of 2200 V, delivering samples to the Eclipse. MS1 spectra were recorded at 120,000 resolution, using an AGC target of 4e5, RF lens at 30%, maximum ion time set to Auto, and a scan range of 300-1800 m/z. MS2 data-dependent acquisition operated at a 15,000 resolution in the Orbitrap for precursor ions exceeding a 5.0e4 intensity threshold; AGC target was Standard, mass range and ion time were set to Auto, and a 1.6 m/z isolation window was applied. Each cycle lasted 3 sec. Peptides were fragmented by HCD with 30% energy, and dynamic exclusion was enabled for 30 seconds following a single detection, targeting ions with charge states 2-8."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptide identification was conducted using MaxQuant software (v 2.0.2.0) using the integrated Andromeda search engine, and quantification utilized a label-free approach 55. The raw mass spectrometry data were compared against both the Euprymna scolopes genome 56 and the MaxQuant contaminants database. During analysis, peptides were required to have at least five amino acids and a maximum mass of 4600 Da. The search allowed up to five possible variable modifications per peptide, including N-terminal protein acetylation, asparagine or glutamine deamidation, methionine oxidation; the carbamidomethylation of cysteine was identified as a fixed modification. Tryptic digestion was defined with trypsin/P specificity, permitting up to two missed cleavages. A 1% false discovery rate for both peptides and proteins was used as a filter for the results using the target-decoy method, whereas other settings remained as defaults. The MaxQuant results were then imported into the program Scaffold (Proteome Software, Inc.) for visualization and further analysis."],"omics_type":["Proteomics"],"labhead":["Jeremy Balsbaugh"],"instrument_platform":[""],"labhead_affiliation":["University of Connecticut Proteomics and Metabolomics Facility"],"submission_type":["COMPLETE"],"species":["Euprymna Scolopes (hawaiian Bobtail Squid)"],"submitter_mail":["jennifer.liddle@uconn.edu"],"publication":["41922716 Guillen Matus DG, Koch EJ, Vijayan N, Good HJ, Samples RM, Rinaldi-Ramos CM, Arnold DP, Nyholm SV, Balunas MJ, Foster JS. Using magnetic nanoparticles to explore symbiotic interactions. Sci Rep. 2026 16(1):15377 10.1038/s41598-026-46489-8"],"submitter_affiliation":["University of Connecticut"],"submitter_country":["United States"],"doi":["10.6019/PXD074352"],"pubmed_abstract":["All plants and animals form symbiotic associations with microbes, yet many of the underlying mechanisms associated with these interactions remain uncharacterized. There are inherent challenges to studying the cellular and metabolic interactions between eukaryotes and their microbial symbionts, thus new methodologies that enable the discovery of symbiotic processes are continually needed. Here, we explored the use of magnetic nanoparticles (MNPs) as a tool to track aspects of the host innate immune response to symbionts under both ex vivo and in vivo conditions. The symbiotic association between the Hawaiian bobtail squid Euprymna scolopes and its bioluminescent partner Vibrio fischeri was used as a model to explore the potential of MNPs as non-toxic, manipulable agents to investigate aquatic symbiotic associations. Results suggest that host cells can be effectively labeled with MNPs under ex vivo conditions and that the particles can be visualized and tracked within the host animal in vivo using magnetic particle imaging. Proteomic and metabolomic analyses also revealed minimal changes to the host innate immune cells after uptake of MNPs in the presence and absence of V. fischeri. Together, these results suggest that MNPs have minimal biochemical impact on the host cells and can serve as an effective tool to explore aquatic symbiotic interactions."],"pubmed_title":["Using magnetic nanoparticles to explore symbiotic interactions."],"pubmed_authors":["Guillen Matus Dulce G DG, Koch Eric J EJ, Vijayan Nidhi N, Good Hayden J HJ, Samples Robert M RM, Rinaldi-Ramos Carlos M CM, Arnold David P DP, Nyholm Spencer V SV, Balunas Marcy J MJ, Foster Jamie S JS"],"additional_accession":[]},"is_claimable":false,"name":"Using magnetic nanoparticles to explore symbiotic interactions","description":"All plants and animals form symbiotic associations with microbes, yet many of the underlying mechanisms associated with these interactions remain uncharacterized. There are inherent challenges to studying the cellular and metabolic interactions between eukaryotes and their microbial symbionts, thus new methodologies that enable the discovery of symbiotic processes are continually needed. Here, we explored the use of magnetic nanoparticles (MNPs) as a tool to track aspects of the host innate immune response to symbionts under both ex vivo and in vivo conditions. The symbiotic association between the Hawaiian bobtail squid Euprymna scolopes and its bioluminescent partner Vibrio fischeri was used as a model to explore the potential of MNPs as non-toxic, manipulable agents to investigate aquatic symbiotic associations. Results suggest that host cells can be effectively labeled with MNPs under ex vivo conditions and that the particles can be visualized and tracked within the host animal in vivo using magnetic particle imaging. Proteomic and metabolomic analyses also revealed minimal changes to the host innate immune cells after uptake of MNPs in the presence and absence of V. fischeri. Together, these results suggest that MNPs have minimal biochemical impact on the host cells and can serve as an effective tool to explore aquatic symbiotic 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