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Elucidation of the glycan structure of the b-type flagellin ofPseudomonas aeruginosaPAO1
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AbstractFlagella are essential for motility and pathogenicity in many bacteria. The main component of the flagellar filament, flagellin, often undergoes post-translational modifications, with glycosylation being a common occurrence. InPseudomonas aeruginosaPAO1, the b-type flagellin isO-glycosylated with a structure that includes a rhamnose, a phospho-group and a previous unknown moiety. This structure resembles the well-characterized glycan (Type A) inClostridioides difficilestrain 630, which features anN-acetylglucosamine linked to anN-methylthreonine via a phosphodiester bond.This study aimed to characterize the b-type glycan structure inPseudomonas aeruginosaPAO1 using a set of mass spectrometry experiments. For this purpose, we used wildtypeP. aeruginosaPAO1 and several gene mutants from the b-type glycan biosynthetic cluster. Moreover, we compared the mass spectrometry characteristics of the b-type glycan with those ofin vitromodified Type A-peptides fromC. difficilestrain 630Δerm.Our results demonstrate that the thus far unknown moiety of the b-type glycan inP. aeruginosaconsists of anN,N-dimethylthreonine. These data allowed us to refine our model of the flagellin glycan biosynthetic pathway in bothP. aeruginosaPAO1 andC. difficilestrain 630.
Cold Spring Harbor Laboratory
Title: Elucidation of the glycan structure of the b-type flagellin ofPseudomonas aeruginosaPAO1
Description:
AbstractFlagella are essential for motility and pathogenicity in many bacteria.
The main component of the flagellar filament, flagellin, often undergoes post-translational modifications, with glycosylation being a common occurrence.
InPseudomonas aeruginosaPAO1, the b-type flagellin isO-glycosylated with a structure that includes a rhamnose, a phospho-group and a previous unknown moiety.
This structure resembles the well-characterized glycan (Type A) inClostridioides difficilestrain 630, which features anN-acetylglucosamine linked to anN-methylthreonine via a phosphodiester bond.
This study aimed to characterize the b-type glycan structure inPseudomonas aeruginosaPAO1 using a set of mass spectrometry experiments.
For this purpose, we used wildtypeP.
aeruginosaPAO1 and several gene mutants from the b-type glycan biosynthetic cluster.
Moreover, we compared the mass spectrometry characteristics of the b-type glycan with those ofin vitromodified Type A-peptides fromC.
difficilestrain 630Δerm.
Our results demonstrate that the thus far unknown moiety of the b-type glycan inP.
aeruginosaconsists of anN,N-dimethylthreonine.
These data allowed us to refine our model of the flagellin glycan biosynthetic pathway in bothP.
aeruginosaPAO1 andC.
difficilestrain 630.
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