Flagellin from Listeria monocytogenes is glycosylated with beta-O-linked N-acetylglucosamine.
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.
Schirm
M
M
Department of Chemistry, University of Montreal, Montreal, Quebec, Canada.
Kalmokoff
M
M
Aubry
A
A
Thibault
P
P
Sandoz
M
M
Logan
S M
SM
D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D005408:Flagellin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D008089:Listeria monocytogenes / Q000235:genetics / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D011134:Polysaccharides; D005408:Flagellin; D000117:Acetylglucosamine