{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Osterberg MK"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pubmed_abstract":["The growth of bacterial pathogens is limited by nutritional immunity, where the infected host deploys metal scavenging proteins to starve the pathogen of essential transition metals. An important transition metal-sequestering protein is the S100A8-S100A9 heterotetramer, calprotectin (CP). Prior work reveals that CP induces a significant Zn- and Fe-starvation response in the Gram-negative opportunistic pathogen, <i>Acinetobacter baumannii</i>, in liquid culture. Here, we employ a quantitative chemoproteomics platform to pinpoint changes in abundance-corrected cysteine reactivity, and by extension cellular metal occupancy in metalloenzymes, that occur when <i>A. baumannii</i> is challenged with physiological CP in liquid culture relative to an untreated WT control. Changes in protein abundan"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.09.16.676631"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12458113"],"repository":["biostudies-literature"],"pubmed_title":["Exploring metalloproteome remodeling in calprotectin-stressed &lt;i&gt;Acinetobacter baumannii&lt;/i&gt; using chemoproteomics."],"pmcid":["PMC12458113"],"funding_grant_id":["R01 AI127793","R35 GM134964","R35 GM118157","T32 GM131994","R01 AI101171"],"pubmed_authors":["Bak DW","Andreini C","Giedroc DP","Trinidad JC","Akizuki T","Weerapana E","Osterberg MK","Cornish PV","Chazin WJ","Critchlow JM","Skaar EP"],"additional_accession":[]},"is_claimable":false,"name":"Exploring metalloproteome remodeling in calprotectin-stressed &lt;i&gt;Acinetobacter baumannii&lt;/i&gt; using chemoproteomics.","description":"The growth of bacterial pathogens is limited by nutritional immunity, where the infected host deploys metal scavenging proteins to starve the pathogen of essential transition metals. An important transition metal-sequestering protein is the S100A8-S100A9 heterotetramer, calprotectin (CP). Prior work reveals that CP induces a significant Zn- and Fe-starvation response in the Gram-negative opportunistic pathogen, <i>Acinetobacter baumannii</i>, in liquid culture. Here, we employ a quantitative chemoproteomics platform to pinpoint changes in abundance-corrected cysteine reactivity, and by extension cellular metal occupancy in metalloenzymes, that occur when <i>A. baumannii</i> is challenged with physiological CP in liquid culture relative to an untreated WT control. Changes in protein abundan","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-05T03:12:18.373Z","creation":"2026-06-05T03:06:52.821Z"},"accession":"S-EPMC12458113","cross_references":{"pubmed":["41000871"],"doi":["10.1101/2025.09.16.676631"]}}