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Journal of Bacteriology, October 2004, p. 6721-6727, Vol. 186, No. 20
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.20.6721-6727.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

M. Schirm,1 M. Kalmokoff,2 A. Aubry,3 P. Thibault,1,4 M. Sandoz,5 and S. M. Logan3*

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.

* Corresponding author. Mailing address: Institute for Biological Sciences, National Research Council, 100 Sussex Dr., Ottawa, Ontario, Canada K1A OR6. Phone: (613) 990-0839. Fax: (613) 952-9092. E-mail: susan.logan{at}nrc-cnrc.gc.ca.

Journal of Bacteriology, October 2004, p. 6721-6727, Vol. 186, No. 20
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.20.6721-6727.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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