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

Institute for Biological Sciences, National Research Council,³ Bureau of Microbial Hazards, Health Products and Foods Branch, Health Canada, Ottawa, Ontario,⁵ Department of Chemistry, University of Montreal, Montreal, Quebec,¹ Canada Bureau of Microbial Hazards, Atlantic Food and Horticulture Research Centre, Agriculture and Agri-Food Canada, Kentville, Nova Scotia,² Caprion Pharmaceuticals, Montreal, Canada⁴

Received 7 June 2004/ Accepted 19 July 2004

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

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