{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-34kDa.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-30kDa.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/20240513_SJ_Frankel_Band_02.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-40kDa.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/20240513_SJ_Frankel_Band_01.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-255kDa.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/20240513_SJ_Frankel_Band_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-34kDa.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-30kDa.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-40kDa.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/20240731_SJ_Frankel_GelBand.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-255kDa.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/20240513_SJ_Frankel_Band_02.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/20240513_SJ_Frankel_Band_02.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-30kDa.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-40kDa.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-255kDa.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/20240513_SJ_Frankel_Band_01.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD080490/PL25-SJ-Frankel-34kDa.pdResult"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["jyoti.choudhary@icr.ac.uk"],"submitter":["Graeme Benstead-Hume"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Citrobacter rodentium","Enteropathogenic escherichia coli"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080490"],"sample_protocol":["Gel pieces were destained twice in 50 mM triethylammonium bicarbonate (TEAB) containing 50% acetonitrile (ACN) for 30 min each with gentle agitation, dehydrated in 100% ACN, and air-dried. Disulfide bonds were reduced with 5 mM tris(2-carboxyethyl)phosphine (TCEP) in 50 mM TEAB for 45 min at room temperature, followed by alkylation with 50 mM iodoacetamide (IAA) in 50 mM TEAB for 45 min in the dark. Gel pieces were washed twice with 50 mM TEAB, dehydrated again in ACN, and air-dried. Proteins were digested o/n (18 h, 37 °C) with sequencing-grade trypsin in 50 mM TEAB. Digestion was quenched with 1% trifluoroacetic acid (TFA), and peptides were sequentially extracted twice with 60% ACN/1% TFA, combining all supernatants. The pooled extracts were dried by vacuum centrifugation, reconstituted in 0.1% TFA, and desalted using C18 StageTips (Thermo Fisher Scientific) prior to LC–MS/MS analysis. LC–MS analysis was performed using a Dionex UltiMate 3000 UHPLC system (Thermo Scientific) coupled to an Orbitrap Ascend mass spectrometer (Thermo Scientific). Peptides were loaded onto a C18 trapping column (Acclaim PepMap 100, 100 µm × 2 cm, 5 µm, 100 Å) at a flow rate of 10 µl/min and subsequently separated on an analytical C18 column (Acclaim PepMap C18, 75 µm × 50 cm, 2 µm, 100 Å) maintained at 50°C using a 120-min linear gradient from 0–35% acetonitrile in 0.1% formic acid at 300 nl/min. The Orbitrap Ascend was operated in positive ion mode using a data-dependent acquisition (DDA) strategy with an expected chromatographic peak width of 30 s. Full MS scans were acquired in the Orbitrap at 120,000 resolution (m/z 375–1500) with quadrupole isolation, an AGC target of 4 × 10⁵, and automatic injection time. The most intense precursor ions (charge states 2–7, intensity > 1 × 10⁴) were selected for collision-induced dissociation (CID) at a normalized collision energy of 32%. MS² spectra were acquired in the ion trap at turbo scan rate using a 0.7 m/z isolation window, AGC target of 1 × 10⁴, and automatic injection time. Dynamic exclusion was enabled for 45 s within ±10 ppm of the precursor m/z, and single isotopes were excluded after one occurrence to improve proteome coverage. ."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw files were processed in Proteome Discoverer 3.0 (Thermo Scientific) using the Sequest HT search engine with Percolator validation. Spectra were searched against the CR ICC168 UniProt FASTA database, including a common contaminant database. Searches assumed full tryptic specificity with up to 2 missed cleavages. Carbamidomethylation of cysteine (+57.021 Da) was set as a fixed modification, while oxidation of methionine (+15.995 Da) and deamidation of asparagine or glutamine (+0.984 Da) were set as variable modifications. The precursor and fragment mass tolerances were 20 ppm and 0.5 Da, respectively. Peptide-spectrum matches were validated using a target-decoy strategy with Percolator, maintaining 1% FDR thresholds at the peptide and protein level"],"omics_type":["Proteomics"],"labhead":["Jytoi Choudhary"],"instrument_platform":[""],"labhead_affiliation":["Functional Proteomics, ICR"],"submission_type":["PARTIAL"],"species":["Escherichia Coli Ko11fl","Citrobacter Rodentium Icc168"],"publication":["Not available"],"submitter_mail":["ghume@icr.ac.uk"],"submitter_affiliation":["ICR"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Design of a live-attenuated bacterial vaccine using effector network engineering","description":"Enteropathogenic Escherichia coli (EPEC) and Citrobacter rodentium (CR) are extracellular enteric attaching and effacing (A/E) pathogens of humans and mice, respectively. Their virulence relies on intimate bacterial attachment and a network of type III secretion system effectors. Here, through systematic reduction and redesign of the effector network in CR, we develop an attenuated strain, CRV (CR Vaccine), encoding a subset of ten effectors. CRV colonises C57BL/6 mice ~100-fold lower than wild type CR (CRWT) without causing overt pathogenesis. Moreover, C3H/HeN mice, which succumb to CRWT infection, survive CRV challenge. Vaccination with CRV confers protection against subsequent CRWT infection in both mouse strains. Serological analysis reveals a repertoire of dominant CR antigens and shows that CRWT and CRV immunisation elicits comparable B cell and antibody responses, which is contingent on intimate bacterial attachment. A corresponding EPEC strain (E. coli Vaccine, ECV) effectively colonises epithelial cells in a gut-on-chip model. These findings establish effector network minimisation as a generalisable strategy for rational attenuation and live-attenuated vaccine design against A/E 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