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. 2024 May 6;12(6):e00346-24. doi: 10.1128/spectrum.00346-24

Fig 3.

Fig 3

Impact of the loss of glycosylation on the B. cenocepacia K56-2 glycoproteome. (A and B) 2D scatter plots comparing glycoprotein levels observed within WT versus ΔpglL and ΔpglL amrAB::native-pglL-his versus ΔpglL. Glycoproteins observed to undergo alterations are color-coded according to the growth condition if the observed alteration has a fold change greater than ±1 fold (log2) and a −log10(P value) > 2. (C) Peptide-centric analysis of glycoproteins FliF , BCAL1086, BCAL2974, MotB, and BCAM0505 observed to undergo alterations in response to the loss of glycosylation reveals a marked decrease in peptide intensities within these proteins which is restored by the re-introduction of glycosylation within the complement ΔpglL amrAB::native-pglL-his.