Dataset Information

C. difficile strain 630 flagellin C modifications

ABSTRACT: In proteomics, the study of post-translational modifications often relies on some type of enrichment strategy. Here, we show that an approach that is commonly used in phosphoproteomics (Immobilised Metal Affinity Chromatography (Fe3+-IMAC)) also enriches for peptides with a unique post-translational modification, known as type A, in the human pathogen Clostridioides difficile. The type A modification consists of a monosaccharide (GlcNAc) that is linked to an N-methylated threonine through a phosphodiester bond. This structure has previously been described on flagellin C of several C. difficile strains and is important for bacterial motility. Using LC-MS/MS analyses of IMAC-captured tryptic peptides, we not only observed Type A modified C. difficile flagellin peptides but also a variety of truncated/modified Type A structures on these peptides. Using an elaborate set of mass spectrometry analyses, we demonstrate that one of these modifications consists of a Type A structure containing a phosphonate (2-aminoethylphosphonate, 2-AEP), a modification that is rarely observed and has hitherto not been described in C. difficile.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Peptoclostridium Difficile (strain 630) (clostridium Difficile)

SUBMITTER: Yassene Mohammed

LAB HEAD: Paul J. Hensbergen

PROVIDER: PXD029552 | Pride | 2022-04-04

REPOSITORIES: pride

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Dataset's files

Source:

			Action	DRS
	Flagellin_Type_A_modification.msf	Msf
	Flagellin_Type_modifications.pdResult	Other
	L20182002792b.raw	Raw
	L20182002877c.raw	Raw
	L20182002877j.raw	Raw

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Publications

New insights into the type A glycan modification of Clostridioides difficile flagellar protein flagellin C by phosphoproteomics analysis.

Hensbergen Paul J PJ de Ru Arnoud H AH Friggen Annemieke H AH Corver Jeroen J Smits Wiep Klaas WK van Veelen Peter A PA

The Journal of biological chemistry 20220120 3

The type A glycan modification found in human pathogen Clostridioides difficile consists of a monosaccharide (GlcNAc) that is linked to an N-methylated threonine through a phosphodiester bond. This structure has previously been described on the flagellar protein flagellin C of several C. difficile strains and is important for bacterial motility. The study of post-translational modifications often relies on some type of enrichment strategy; however, a procedure for enrichment of this modification ...[more]

PMID: 35065968

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