Flagellin from Listeria monocytogenes Is Glycosylated with β-O-Linked N-Acetylglucosamine

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DOIResolve DOI: https://doi.org/10.1128/JB.186.20.6721-6727.2004
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  1. National Research Council Canada. NRC Institute for Biological Sciences
FormatText
TypeArticle
Journal titleJournal of Bacteriology
ISSN0021-9193
1098-5530
Volume186
Issue20
Pages6721–6727
Abstract
Glycan staining of purified flagellin from Listeria monocytogenes serotypes 1/2a, 1/2b, 1/2c, and 4b suggested that the flagellin protein from this organism is glycosylated. Mass spectrometry analysis demonstrated that the flagellin protein of L. monocytogenes is posttranslationally modified with O-linked N-acetylglucosamine (GlcNAc) at up to six sites/monomer. The sites of glycosylation are all located in the central, surface-exposed region of the protein monomer. Immunoblotting with a monoclonal antibody specific for β-O-linked GlcNAc confirmed that the linkage was in the β configuration, this residue being a posttranslational modification commonly observed in eukaryote nuclear and cytoplasmic proteins.
Publication date
PublisherAmerican Society for Microbiology
LanguageEnglish
Peer reviewedYes
NPARC number23002074
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