| Download | - View final version: Flagellin from Listeria monocytogenes Is Glycosylated with β-O-Linked N-Acetylglucosamine (PDF, 748 KB)
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| DOI | Resolve DOI: https://doi.org/10.1128/JB.186.20.6721-6727.2004 |
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| Author | Search for: LLLL, N,; Search for: Schirm, M.; Search for: Kalmokoff, M.; Search for: Aubry, A.1; Search for: Thibault, P.1; Search for: Sandoz, M.; Search for: Logan, S. M.1 |
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| Name affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Abstract | 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 β-O-linked GlcNAc confirmed that the linkage was in the β configuration, this residue being a posttranslational modification commonly observed in eukaryote nuclear and cytoplasmic proteins. |
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| Publication date | 2004-10 |
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| Publisher | American Society for Microbiology |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 23002074 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction |
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| Record identifier | 268aea41-1541-4849-91fb-6cea440218a5 |
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| Record created | 2017-08-08 |
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| Record modified | 2020-05-30 |
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