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Glycosylation is increasingly recognised as a common protein modification within bacterial proteomes. While great strides have been made in identifying species that contain glycosylation systems, our understanding of the proteins and sites targeted by these systems is far more limited. Within this work we explore the conservation of glycoproteins and glycosylation sites across the pan- Burkholderia  glycoproteome. Using a multi-protease glycoproteomic approach, we generate high-confidence glycoproteomes in two widely utilized  B. cenocepacia  strains, K56-2 and H111. This resource reveals glycosylation occurs exclusively at Serine residues and that glycoproteins/glycosylation sites are highly conserved across  B. cenocepacia  isolates. This preference for glycosylation at Serine residues is observed across at least 9  Burkholderia  glycoproteomes, supporting that Serine is the dominant residue targeted by PglL-mediated glycosylation across the  Burkholderia  genus. Combined, this work demonstrates that PglL enzymes of the  Burkholderia  genus are Serine-preferring oligosaccharyltransferases that target conserved and shared protein substrates.

Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus