{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000101_DIA-NN_output_and_imputed_matrix.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000100_Experimental_Design_protein_ID.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000045_Experimental_design_protein_ID.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000045_DIA-NN_output_and_imputed_matrix.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000100_DIA-NN_output_and_imputed_matrix.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000101_Experimental_desin_protein_ID.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000100_BW25113_Active_Kinetics.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000101_EPEC.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD075099/PCF000045_BW25113.7z"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["lily.karamanou@kuleuven.be"],"submitter":["Haitham Abdallah"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075099"],"sample_protocol":["Bacteria were treated with either 0.2% DMSO or with, HSI#6\"active\" or HSI#11 \"inactive\" (for E. coli BW25113 3 µM compound was used; for EPEC 10 µM) and lysed by using the radioimmunoprecipitation assay (RIPA buffer #R0278, Sigma-Aldrich) according to manufacturer’s instructions. Protein concentration was determined using the Pierce bicinchoninic acid protein assay kit (#23227, Thermo Fisher Scientific). Samples were analysed using liquid-chromatography-mass-spectrometry (LC-MS; loading 50 µg of total protein / sample) and the S-Trap micro sample prep kit (K02-micro-160, ProtiFi, Fairport, NY, USA) according to manufacturer’s instructions."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Quantification was performed using robust LC (high precision). Cross-run normalization was retention time-dependent, and library generation used smart profiling. Statistical analysis was performed using an R script (available as a shinny app at https://analyst-suites.org/apps/dia-analyst ) based on the protein-level data file. Contaminant proteins and reverse sequences were filtered out. The DIA abundance data was converted to log2 scale, samples were grouped by conditions and missing values were imputed using the “Perseus type” also named ‘Missing not At Random’ (MNAR) method), which uses random draws from a left-shifted Gaussian distribution of 1.8 StDev (standard deviation) apart with a width of 0.3. For the differential expression analysis, protein-wise linear models combined with empirical Bayes statistics were used. The limma package from R Bioconductor was used to generate a list of differentially expressed proteins for each pair-wise comparison"],"omics_type":["Proteomics"],"labhead":["Lily Karamanou"],"instrument_platform":[""],"labhead_affiliation":["LAb of molecular bacteriology, Rega Institute, KU Leuven"],"submission_type":["PARTIAL"],"species":["Escherichia Coli","Bacteria"],"submitter_mail":["haitham.abdallah@kuleuven.be"],"publication":["Not available"],"submitter_affiliation":["Lab. of Molecular bacteriology, Rega Institute, KU Leuven"],"submitter_country":["Belgium"],"additional_accession":[]},"is_claimable":false,"name":"Integrated omics-based mechanistical insights into a membrane-targeting antibacterial","description":"Here, we investigated HSI#6, a small-molecule antibacterial previously identified as a SecA activator, using integrated omics and functional assays. HSI#6 exhibits broad-spectrum bacteriostatic activity and acts through a dual-phase mechanism: transient activation of SecA-dependent secretion followed by membrane perturbation and global stress reprogramming. Time-resolved transcriptomics and proteomics revealed early activation of envelope stress regulons (Cpx, Rcs, Pho), efflux systems, and oxidative stress pathways, followed by suppression of ribosome biogenesis and central metabolism. Comparative analysis and biomarker-based principle component analysis (PCA) positioned HSI#6 within the envelope stress mechanistic space, closely aligned with membrane-active antibiotics yet displaying a distinct signature. Adaptive laboratory evolution (ALE) combined with whole-genome sequencing (WGS) revealed compensatory mutations in topoisomerase 1A gene (topA) and transcriptional regulators, without adaptive resistance emerged even under prolonged selection pressure. These findings establish HSI#6 as a mechanistically unique antibacterial targeting membrane homeostasis with low resistance 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