<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Osterberg MK</submitter><funding>NIAID NIH HHS</funding><funding>NIGMS NIH HHS</funding><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, &lt;i>Acinetobacter baumannii&lt;/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 &lt;i>A. baumannii&lt;/i> is challenged with physiological CP in liquid culture relative to an untreated WT control. Changes in protein abundan</pubmed_abstract><journal>bioRxiv : the preprint server for biology</journal><pagination>2025.09.16.676631</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12458113</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Exploring metalloproteome remodeling in calprotectin-stressed &amp;lt;i&amp;gt;Acinetobacter baumannii&amp;lt;/i&amp;gt; using chemoproteomics.</pubmed_title><pmcid>PMC12458113</pmcid><funding_grant_id>R01 AI127793</funding_grant_id><funding_grant_id>R35 GM134964</funding_grant_id><funding_grant_id>R35 GM118157</funding_grant_id><funding_grant_id>T32 GM131994</funding_grant_id><funding_grant_id>R01 AI101171</funding_grant_id><pubmed_authors>Bak DW</pubmed_authors><pubmed_authors>Andreini C</pubmed_authors><pubmed_authors>Giedroc DP</pubmed_authors><pubmed_authors>Trinidad JC</pubmed_authors><pubmed_authors>Akizuki T</pubmed_authors><pubmed_authors>Weerapana E</pubmed_authors><pubmed_authors>Osterberg MK</pubmed_authors><pubmed_authors>Cornish PV</pubmed_authors><pubmed_authors>Chazin WJ</pubmed_authors><pubmed_authors>Critchlow JM</pubmed_authors><pubmed_authors>Skaar EP</pubmed_authors></additional><is_claimable>false</is_claimable><name>Exploring metalloproteome remodeling in calprotectin-stressed &amp;lt;i&amp;gt;Acinetobacter baumannii&amp;lt;/i&amp;gt; using chemoproteomics.</name><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, &lt;i>Acinetobacter baumannii&lt;/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 &lt;i>A. baumannii&lt;/i> is challenged with physiological CP in liquid culture relative to an untreated WT control. Changes in protein abundan</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Sep</publication><modification>2026-06-05T03:12:18.373Z</modification><creation>2026-06-05T03:06:52.821Z</creation></dates><accession>S-EPMC12458113</accession><cross_references><pubmed>41000871</pubmed><doi>10.1101/2025.09.16.676631</doi></cross_references></HashMap>