4.4 Article

Flagellin from Listeria monocytogenes is glycosylated with β-O-linked N-acetylglucosamine

Journal

JOURNAL OF BACTERIOLOGY
Volume 186, Issue 20, Pages 6721-6727

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.186.20.6721-6727.2004

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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 beta-O-linked GlcNAc confirmed that the linkage was in the beta configuration, this residue being a posttranslational modification commonly observed in eukaryote nuclear and cytoplasmic proteins.

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