Valdiazen Derivatives for Chemoproteomic Studies in Burkholderia Cenocepacia H111

Quorum sensing allows bacteria to coordinate community-wide behaviours such as biofilm formation, virulence, and symbiosis. The diazeniumdiolate valdiazen has been identified in the opportunistic pathogen Burkholderia cenocepacia H111 as a novel quorum-sensing signal, yet its protein interactome has remained unexplored. In this study, we employed a chemoproteomic pulldown approach to identify potential valdiazen-binding proteins. For these pulldown experiments, a series of alkyne-linked and biotin-conjugated valdiazen probes were synthesised. Affinity-based pulldown experiments using biotin-valdiazen conjugates successfully identified 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 quorum sensing.