{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250321_FtsZ_ref_4_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250226_FTSZ_ref3_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250320_FtsZ_ref_3_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250225_FTSZ_ref_1_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250320_FtsZ_ref_2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250226_FTSZ_ref_2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250226_CapRel_ref2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250225_GP04_ref_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250226_GP04_ref_2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250320_CapRel_ref_2_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250226_CapRel_ref3_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/250225_CapRel_ref1_IA_final_peptide.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/270225_Gp04_ref_3_IA_final_peptide.csv"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/Complex.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/CapRel_Complex__March2025.DnX","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/GP04.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/FTSZ.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/GP04.DnX","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/CapRel.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065182/FTSZ_Complex_March2025.DnX"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["chloe.martens@ulb.be"],"submitter":["kyo Coppieters"],"technology_type":["Mass Spectrometry","MSE"],"software":["Not available"],"submitter_keywords":["Hdx-ms","Anti-phage defense"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065182"],"sample_protocol":["HDX MS samples were prepared by mixing 4 µL of sample (CapRelEbc, Gp0.4T7, FtsZ(L178E), or their complex at 60-300 µM) with 56 µL of E or L buffer (50 mM HEPES pH 7.6, 500 mM NaCl, 500 mM KCl, 2 mM MgCl2, 1 mM TCEP, 0.002% Mellitic acid) and incubated during labeling time at 20°C on a heat block. After the incubation, samples were quenched with equivalent volume of Quench Buffer (1.2% formic acid, 1 mM TCEP, pH 2.4) and directly flash-frozen in liquid nitrogen. Prior to each injection, the quenched samples were thawed at room temperature and transferred to the Enzymate BEH Pepsin Column (Waters®) where digestion occurs at 200 µL/min with a pressure of 7 kPSI at 20°C. Then, peptic peptides were trapped for 3 min on Acquity UPLC BEH C18 VanGuard Pre-column (Waters®) at 200 µL/min with MS grade water complemented with 0.1% formic acid and then eluated on Acquity UPLC BEH C18 Column (Waters®) with a linear gradient (3-45% gradient of 0.1% formic acid in acetonitrile) at 40 µL/min. At the end of each run, columns were cleaned with - for enzymatic column, three injections of Pepsin Wash buffer (1.5 M Gu-HCl, 4% (v/v) MeOH, 0.8% (v/v) formic acid), - for Pre-column and UPLC column, a saw-tooth gradient. We also performed cleaning run, each three samples to prevent peptide carry-over. Peptides identification was performed on non-deuterated samples (five replicates) on the Synapt G2 with positive ionization with ESI probe in MSE acquisition mode (collision energy ramp in transfer cell: 20-30 eV). Leucine Enkephalin was applied for mass accuracy correction and sodium formate was used as a calibration for the mass spectrometer. All deuterium time points were performed in triplicates."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The no-deuteration reference points were analyzed by PLGS (ProteinLynx Global Server 2.5.1, Waters) to identify the peptic peptides belonging to CapRelEbc, Gp0.4T7, or FtsZ(L178E). Then, all the MSE data including reference and deuterated samples were processed by DynamX 3.0 (Waters) for deuterium uptake determination. We chose the following filtering parameters to make an optimal ratio between quality and quantity of identified peptides: minimum intensity of 1000, minimum and maximum peptide sequence length of 5 and 20, respectively, minimum MS/MS products of 3, minimum products per amino acid of 0.27, minimum score of 5, and a maximum MH+ error threshold of 15 p.p.m. Data were analyzed at peptidic and overall level. All heat maps have been generated in DynamX and Deuteros software was also used to make statistical analysis."],"omics_type":["Proteomics"],"labhead":["Chloé Martens"],"instrument_platform":[""],"labhead_affiliation":["Chloé Martens, Ph.D Chercheuse Qualifiée - FRS.FNRS Group Leader Structure and Function of Biological Membranes - Chemistry Department chloemartenslab.com - sfmb.ulb.be Phone :+32 2 650 53 83 Université Libre de Bruxelles - Campus Plaine. Building BC, Room 1C4 110 - Boulevard du Triomphe, Accès 2 1050 Brussels - Belgium (lab head)"],"submission_type":["PARTIAL"],"species":["Escherichia Coli (strain B / Bl21)"],"publication":["Not available"],"submitter_mail":["coppieterskyo@hotmail.fr"],"submitter_affiliation":["Université Libre de Bruxelles"],"submitter_country":["Belgium"],"additional_accession":[]},"is_claimable":false,"name":"Activation of a bacterial immunity protein by a viral-host factor complex (HDX-MS)","description":"Bacteria have developed sophisticated immune systems to defend against phages, often activating these defenses by detecting specific phage components. In our study, we show that the bacterial defense protein CapRelEbc is activated by a complex between a T7 phage protein (Gp0.4) and the host’s cell division protein FtsZ during infection.  Here, we tried to validate this hypothesis by performing 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