{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075040/20231009_SoL_ERV165_YX_pghi-4_12.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["hhang@scripps.edu"],"submitter":["Kyong Fam"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":["Not available"],"submitter_keywords":["Chemoproteomics","Peptidoglycan hydrolase","Antibiotic adjuvant","Vancomycin-resistant enterococcus faecium","Covalent inhibitor"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075040"],"sample_protocol":["The protocol was adapted from Njomen E. et al. Nat. Chem. 2024. VREfm ERV165 were grown from overnight culture in 15 mL of fresh BHI till OD600~0.6. Bacteria were then centrifuged and resuspended in 1 mL of BHI (OD600~9), followed by incubation with pghi-4 (10, 25 or 50 μM) for 1 hour at 37°C and 200 RPM shaking. Bacterial pellets were collected by centrifugation (4,800 × g for 10 min), washed twice with PBS and immediately processed or stored at −80 °C. Bacterial pellets were resuspended in 360 μL PBS and lysed with 0.1 mm glass beads (BioSpec) using FastPrep system (MP Biomedicals, settings: 6 m/s, 2 cycles, 45 s for each cycle). Proteins were quantified by Pierce™ BCA Protein Assay (ThermoFisher) and normalized to 2 mg/mL. 1 mg/0.5 mL of bacterial proteome was incubated with iodoacetamide-desthiobiotin (IA-DTB, 100 μM) for 1 hour at room temperature agitating. Bacterial proteins were precipitated by cold methanol (600 μL), chloroform (200 μL), and water (100 μL), followed by vortexing and centrifugation at 16,000 × g for 10 min at 4°C. Liquids were carefully aspirated, proteins were washed with cold methanol, pelleted by centrifugation (16,000 × g for 10 min at 4°C) and air-dried for 5 min. Protein pellets were resuspended in 90 μL of buffer (9 M urea, 10 mM DTT, 50 mM triethylammonium bicarbonate (TEAB) pH 8.5), heated at 65°C for 20 min, followed by treatment with iodoacetamide (50 mM) for 30 min at 37°C. The insoluble residues were pelleted by centrifugation and clear solutions were sonicated. Samples were diluted with 300 μL TEAB buffer and trypsinized (5 μL of 0.4 μg/μL trypsin in trypsin buffer supplemented with 25 mM CaCl2) overnight at 37°C. Samples were treated with 400 µL of wash buffer (50 mM TEAB, 150 mM NaCl, 0.2% NP-40) containing 50 µL of streptavidin agarose to the peptide samples, followed by rotation at room temp for 2 hours. Suspensions were briefly centrifuged, and beads-containing suspensions were loaded on BioSpin columns. The beads were sequentially washed with 3 × 1 mL wash buffer, 3 × 1 mL PBS, 3 × 1 mL MiliQ water. Beads-bound peptides were eluted by addition of 2 × 200 µL of 80% acetonitrile (0.1% formic acid) and the eluate was concentrated by SpeedVac. Peptides were resuspended in 70 μL EPPS buffer (200 mM, pH 8.0), supplemented with 30% acetonitrile, vortexed and sonicated for 5 min. Peptides were tandem mass tag (TMT)-labeled by adding 3 μL of 10 mg/mL TMT10plex tag and incubating for 1 hour at room temperature. The reaction was quenched by sequential addition of hydroxylamine (3 μL of a 5% aqueous solution, 15 min at room temperature) and formic acid (5 μL), followed by concentration using SpeedVac. Samples were resuspended in 500 μL Velos buffer A (95% water, 5% acetonitrile, 0.1% formic acid), acidified with 20 μL of formic acid, desalted (Sep-Pak C18 Cartridge) and concentrated by SpeedVac. Desalted and concentrated samples were redissolved in 500 μL Velos buffer A and HPLC-fractionated. Fractionation and TMT LC-MS analysis was followed as previously described (Njomen E. et al. Nat. Chem. 2024)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["RAW file uploaded here were further analyzed as previously described (Njomen E. et al. Nat. Chem. 2024) with small modifications regarding the proteome dataset Enterococcus faecium ERV165 UniProt database (UP000005678)."],"omics_type":["Proteomics"],"labhead":["Howard C. Hang"],"instrument_platform":[""],"labhead_affiliation":["Department of Immunology & Microbiology, Scripps Research, USA"],"submission_type":["PARTIAL"],"species":["Enterococcus Faecium Erv165"],"submitter_mail":["tfam@scripps.edu"],"publication":["41889990 Fam KT, Chodisetti PK, Wang Z, Homer JA, Smedley CJ, Kitamura S, Silva B, Xiong Y, Hansel-Harris A, Holcomb M, Babarinde S, Turner AM, Van Tyne D, Wilson IA, Forli S, Cravatt BF, Park D, Wolan DW, Moses JE, Hang HC. Genetic and pharmacological inactivation of peptidoglycan remodeling increases antibiotic susceptibility of vancomycin-resistant &lt;i&gt;Enterococcus faecium&lt;/i&gt;. bioRxiv. 2026:2025.09.11.675460 10.1101/2025.09.11.675460"],"submitter_affiliation":["Scripps Research"],"submitter_country":["United States"],"pubmed_abstract":["Vancomycin-resistant <i>Enterococcus faecium</i> (VREfm) is a leading cause of healthcare-associated infections globally and demands new approaches for treatment. Here we show that genetic and pharmacological inactivation of a highly conserved NlpC/P60 peptidoglycan hydrolase, secreted antigen A (SagA), enhanced vancomycin susceptibility of VREfm <i>ex vivo</i> and <i>in vivo</i>. Notably, genetic deletion of <i>sagA</i> impaired VREfm peptidoglycan remodeling, growth and increased the activity of vancomycin. We then identified first-in-class covalent NlpC/P60 peptidoglycan hydrolase inhibitors and demonstrated that pharmacological inactivation of SagA activity also impaired peptidoglycan remodeling and increased the efficacy of vancomycin across genetically distinct VREfm clinical isolates. Our study reveals peptidoglycan hydrolases are druggable targets whose inactivation improves the efficacy of vancomycin against VREfm."],"pubmed_title":["Genetic and pharmacological inactivation of peptidoglycan remodeling increases antibiotic susceptibility of vancomycin-resistant &lt;i&gt;Enterococcus faecium&lt;/i&gt;."],"pubmed_authors":["Fam Kyong T KT, Chodisetti Pavan Kumar PK, Wang Zifei Z, Homer Joshua A JA, Smedley Christopher J CJ, Kitamura Seiya S, Silva Benjamin B, Xiong Yijun Y, Hansel-Harris Althea A, Holcomb Matthew M, Babarinde Simeon S, Turner Adrianna M AM, Van Tyne Daria D, Wilson Ian A IA, Forli Stefano S, Cravatt Benjamin F BF, Park Donghyun D, Wolan Dennis W DW, Moses John E JE, Hang Howard C HC"],"additional_accession":[]},"is_claimable":false,"name":"Genetic and pharmacological inactivation of peptidoglycan remodeling increases antibiotic susceptibility of vancomycin-resistant Enterococcus faecium","description":"Vancomycin-resistant Enterococcus faecium (VREfm) is a leading cause of healthcare-associated infections globally and demands new approaches for treatment. Here we show that genetic and pharmacological inactivation of a highly conserved NlpC/P60 peptidoglycan hydrolase, secreted antigen A (SagA), enhanced vancomycin susceptibility of VREfm ex vivo and in vivo. Notably, genetic deletion of sagA impaired VREfm peptidoglycan remodeling, growth and increased the activity of vancomycin. We then identified first-in-class covalent NlpC/P60 peptidoglycan hydrolase inhibitors and demonstrated that pharmacological inactivation of SagA activity also impaired peptidoglycan remodeling and increased the efficacy of vancomycin in several VREfm clinical isolates. Our study reveals peptidoglycan hydrolases are druggable targets whose inactivation improves the efficacy of vancomycin against 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