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

Schirm M, Kalmokoff M, Aubry A, Thibault P, Sandoz M, Logan SM

Department of Chemistry, University of Montreal, Montreal, Quebec, Canada.

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.

J. Bacteriol. 2004;186(20):6721-7.

Pubmed ID: 15466023

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