Exploring metalloproteome remodeling in calprotectin-stressed <i>Acinetobacter baumannii</i> using chemoproteomics.

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, Acinetobacter baumannii, 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 A. baumannii is challenged with physiological CP in liquid culture relative to an untreated WT control. Changes in protein abundan

SUBMITTER: Osterberg MK 

PROVIDER: S-EPMC12458113 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature