Valdiazen Derivatives for Chemoproteomic Studies in Burkholderia cenocepacia H111.

Abstract

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.