O-linked protein glycosylation is a highly conserved process across the Burkholderia genus and mediated by the oligosaccharyltransferase PglL. While our understanding of Burkholderia glycoproteomes has dramatically improved in recent years (1) little is known about the dynamics of bacterial glycosylation and how Burkholderia species respond to modulations in glycosylation levels. Utilising a Rhamnose inducible CRISPRi based system (2) we explore the impact of O-linked glycosylation silencing across four species of Burkholderia (B. cenocepacia K56-2, B. diffusa MSMB375; B. multivorans ATCC17616 and B. thailandensis E264). Across these species proteomic analysis reveals CRISPRi allows the inducible silencing of PglL levels, yet find this does not diminish glycosylation capacity in a proportional manner. Using glycoproteomics we find that even with the reduction of PglL to below detectable levels O-linked glycosylation persists across all Burkholderia species. Comparing B. cenocepacia ΔpglL to glycosylation silenced strains of B. cenocepacia at both low (0.1%) and high (1%) concentrations of Rhamnose reveals that while glycosylation can be inhibited by nearly 90% the proteome and phenotypes associated with the loss of glycosylation, such as motility, are not impacted. Importantly this work also demonstrates that high levels of Rhamnose induction can lead to extensive impacts on Burkholderia proteomes which, without appropriate controls, mask the impacts specifically driven by CRISPRi guides. Combined this work reveals the O-linked glycosylation systems in Burkholderia species appear buffered from modulations in PglL levels and that Burkholderia proteomes appear tolerant to fluctuations in glycosylation capacity.