
pmid: 40084497
Quorum sensing (QS) allows bacteria to coordinate community‐wide behaviors such as biofilm formation, virulence, and symbiosis. The diazeniumdiolate valdiazen is identified in the opportunistic pathogen Burkholderia cenocepacia H111 as a novel quorum‐sensing signal, yet its protein interactome remains unexplored. In this study, a chemoproteomic pulldown approach is used to identify potential valdiazen‐binding proteins. For these pulldown experiments, a series of alkyne‐linked and biotin‐conjugated valdiazen probes are synthesized. Affinity‐based pulldown experiments using biotin‐valdiazen conjugates successfully identify several putative proteins including an ATP synthase subunit, a succinylglutamate desuccinylase/aspartoacylase, a granule‐associated protein, an acetyl‐CoA hydrolase, a serine protease and an OmpA/MotB precursor. Overall, this study provides insights into the valdiazen–protein interactome in Burkholderia cenocepacia H111, advancing our understanding of the role of valdiazen in bacterial QS.
10120 Department of Chemistry, Proteomics, 1303 Biochemistry, 10126 Department of Plant and Microbial Biology, Bacterial Proteins, Burkholderia cenocepacia, 1313 Molecular Medicine, 540 Chemistry, 1312 Molecular Biology, Quorum Sensing, 580 Plants (Botany), 1605 Organic Chemistry
10120 Department of Chemistry, Proteomics, 1303 Biochemistry, 10126 Department of Plant and Microbial Biology, Bacterial Proteins, Burkholderia cenocepacia, 1313 Molecular Medicine, 540 Chemistry, 1312 Molecular Biology, Quorum Sensing, 580 Plants (Botany), 1605 Organic Chemistry
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