{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M3.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M7.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M12.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M6.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M11.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M1.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M5.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M9.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M10.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M2.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M4.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/protein_M8.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M1.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M5.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M9.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M11.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M2.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M12.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M4.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M8.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M3.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M7.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M6.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD050998/RAvendano_M10.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["reavendano@yahoo.com"],"submitter":["Guillermo Nourdin"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD050998"],"tissue":["Cell Culture"],"sample_protocol":["Protein extraction and digestion for nLC-MS/MS The protein samples were cleaned using a chloroform/methanol extraction, followed by centrifugation at 15,000 x g for 5 min. The aqueous phase was removed, and the disc was rinsed three times with 100% methanol, dried using a cold rotary evaporator at 4 °C, and finally resuspended in 8 M urea containing 25 mM of ammonium bicarbonate (NH4HCO3, pH 8.0). The proteins were quantified using the Qubit™ protein assay (Sigma-Aldrich), where 100 µg were reduced with 20 mM dithiothreitol for 30 minutes, alkylated with 20 mM iodoacetamide in the dark for 60 min, diluted tenfold with 25 mM ammonium bicarbonate pH 8.0, and digested with trypsin/LyC (Promega, Madison, WI, USA) at a 1:50 ratio overnight at 37 °C. Finally, the reaction was stopped by adding 10% formic acid (CH2O2, pH 3.0). Peptides were cleaned using Sep-Pak® C18 Cartridges (Water Corporation, USA) according to the manufacturer’s protocol. The eluted peptides were dried using a rotary concentrator at 4 °C and subsequently resuspended in 0.1% (v/v) formic acid (Merck, Germany). Quantification was performed using a Direct Detect Spectrometer (Merck Millipore).  Liquid chromatography Digested peptides (200 ng) were injected into the nanoElute® liquid chromatography system (Bruker Daltonics). The peptides were separated within 90 min at a flow rate of 400 nL/min at 50 °C on a reversed-phase column Aurora Series CSI (250 mm x 75µm i.d. C18 1.6 µm) (IonOpticks, Australia). Mobile phases A and B were water and acetonitrile with 0.1% (v/v) formic acid, respectively. The B percentage was linearly increased from 2 to 17% within 57 min, followed by an increase to 25% within 21 min and then to 35% within 13 min, followed by a washing step at 85% and re-equilibration.  timsTOF Pro mass spectrometry The bacterial samples were analyzed on a hybrid trapped ion mobility spectrometry (TIMS) quadrupole time-of-flight mass spectrometer (MS) (timsTOF Pro, Bruker Daltonics) via a CaptiveSpray nano-electrospray ion source. The MS was operated in data-dependent mode for the ion mobility-enhanced spectral library generation. The accumulation and ramp times were set at 100 ms each, and mass spectra were recorded in the range from 100–1,700 m/z in positive electrospray mode. The ion mobility was scanned from 0.6 to 1.6 Vs/cm². The overall acquisition cycle of 1.16 s comprised one full TIMS-MS scan and 10 parallel accumulation-serial fragmentation MS/MS scans."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Database searching Tandem mass spectra were extracted by TIMS Control v2.0 (Bruker Daltonics). All MS/MS samples were analyzed using the search engine MSFragger v3.5 (Kong et al., 2017) through the FragPipe v18.0 platform. The parameters used were a precursor mass tolerance of -20 to 20 ppm and a fragment mass tolerance of 20 ppm Da. Digestion options included trypsin as the enzyme and specific digestion mode, and a maximum of 2 missing cleavages per peptide. The following post-translational modifications were assigned: carbamidomethylation of cysteine (fixed post-translational modification); and the oxidation of methionine (M) and N-terminal acetylation (variable post-translational modifications). The predicted proteome of the sequenced genomes for strains T. dicentrarchi CECT 7612T (2,425 proteins) and the Chilean TdCh05 (2,538 proteins) were used for identification based on available data in public databases; according to the accession numbers GCA_900239455.1 and GCA_900239345.1 (Saldarriaga-Córdoba et al., 2021). The false discovery rate estimate was included using a decoy database. A false discovery rate ≥ 1% and one minimum unique peptide per protein were used as filters for identification.  Label Free Quantification and differential expression analysis The result of the MSFragger intensity matrix was used. The identification results obtained were concatenated, and the resulting missing values (NA) were imputed using multivariate imputation by chained equations (van Buuren & Groothuis-Oudshoorn, 2010). To determine which proteins were differentially and significantly expressed in the treatments (2.2′-dipyridyl or control), a Fisher’s exact test was applied to data with a Benjamini-Hochberg correction using DESeq2 (Love et al., 2014). Any protein associated with p-adjusted value < 0.05 was considered significant. Using these proteins, comparisons were made between T. dicentrarchi under DIP and control conditions, resulting in the identification of differentially expressed proteins (DEPs). To ensure a higher level of certainty, DEPs were considered evaluable where the rate of change was at least 2 (log2FC < -0.2 for under expression and log2 FC > 0.2 for over expression). Graphical representations related to quantification results were created using the statistical environment R v3.6.0 with EnhancedVolcano (Blighe et al., 2019), Complex Heatmap v2.0.0 (Gu et al., 2016), GOplot (Walter et al., 2015), and the base packages of R."],"omics_type":["Proteomics"],"labhead":["Ruben Avendaño-Herrera"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Universidad Andrés Bello, Laboratorio de Patología de Organismos Acuáticos y Biotecnología Acuícola, Facultad de Ciencias de la Vida, Viña del Mar, Chile"],"species":["Tenacibaculum Dicentrarchi"],"publication":["10.1111/JFD.13984"],"submitter_mail":["gnourdin@melisainstitute.org"],"submitter_affiliation":["MELISA Institute"],"submitter_country":["Chile"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic characterization of Tenacibaculum dicentrarchi under iron limitation reveals an upregulation of proteins related to iron oxidation and reduction metabolism, iron uptake systems and gliding motility","description":"A strategy for vaccine design involves identifying proteins that could be involved in the pathogen-host interaction. The aim of this proteomic study was to determine how iron limitation affects the protein expression of Tenacibaculum dicentrarchi, with a primary focus on virulence factors and proteins associated with iron uptake. Our findings revealed differences in the proteins expressed by the type strain CECT 7612T and the Chilean strain TdCh05 of T. dicentrarchi. Nonetheless, both share a common response to iron deprivation, with an increased expression of proteins associated with iron oxidation and reduction metabolism, siderophore transport, heme compound biosynthesis, and iron transporters under iron limitation. Proteins involved in gliding motility, such as GldL and SprE, were also upregulated in both strains. A negative differential regulation of metabolic proteins, particularly those associated with amino acid biosynthesis, was observed under iron limitation, reflecting the impact of iron availability on bacterial metabolism. Additionally, the TdCh05 strain exhibited unique proteins associated with gliding motility machinery and phage infection control compared to the type strain. These groups of proteins have been identified as virulence factors within the Flavobacteriaceae family, including the genus Tenacibaculum. These results build upon our previous report on iron acquisition mechanisms and could lay the groundwork for future studies aimed at elucidating the role of some of the described proteins in the infectious process of tenacibaculosis, as well as in the development of potential 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