Fig. 2: O-linked glycosylation predominantly occurs on Serine residues across the B. cenocepacia glycoproteome. | Communications Biology

Fig. 2: O-linked glycosylation predominantly occurs on Serine residues across the B. cenocepacia glycoproteome.

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

Fig. 2

a Sequence analysis of localised glycosylation sites across B. cenocepacia strains reveals all assigned sites are Serine. b Western analysis of DsbA1Nm-his6 variants reveals substitution of only S36 to Alanine or Threonine results in reduced glycosylation. c Relative amounts of the DsbA1Nm-his6 glycosylated and non-glycosylated peptides 23VQTSVPADSAPAASAAAAPAGLVEGQNYTVLANPIPQQQAGK64 and 23VQTSVPADSAPAATAAAAPAGLVEGQNYTVLANPIPQQQAGK64 observed within K56-2 WT reveals the alteration of S36 to T36 dramatically reduces glycosylation. Glycosylation site within peptides denoted by underlining. Differences in the abundance of glycosylated and non-glycosylated peptides containing S36 to T36 correspond to (N = 3) biologically independent samples assessed using two-sided t-tests resulting in p-values of 0.0054 and 0.036 respectively.

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