Technique(s) used for Glycosylation Detection | Rapid migration on SDS-PAGE after chemical deglycosylation with TFMS, glycoprotein staining using GelCode-glycoprotein staining kit. |
Technique(s) used for Glycosylated Residue(s) Detection | Site-directed mutagenesis and MALDI-TOF MS (matrix assisted laser desorption/ionization time of flight mass spectrometry) analysis |
Protein Glycosylation- Implication | The flagellin glycan structures have a role to play in the virulence and host specificity of P. syringae. Glycosylation is important for the HR-inducing (hypersensitive reaction, a rapid and strong plant defence response) ability of the flagellin in plants. |
Glycan Information |
Glycan Annotation | Linkage: Rha-Ser. S201 carries a unique trisaccharide consisting of two rhamnosyl (Rha) residues and one modified 4-amino-4,6-dideoxyglucosyl (Qui4N; named as viosamine) residue, ß-D-Quip4N(3-hydroxy-1-oxobutyl)2Me-(1→3)-α-L-Rhap-(1→2)-α-L-Rhap. The trisaccharide is present as the major glycan on each Ser residue. The glycans contain both L-Rha and D-Rha at a molar ratio of about 4:1. Heterogeneity due to the addition of one or two units of mass value 147 is also observed. |
BCSDB ID | 21440 |
GlyTouCan | G82631IS |
Technique(s) used for Glycan Identification | Sugar composition analysis using an ABEE (p-aminobenzoic acid ethyl ester) labeling kit, MALDI-TOF MS (matrix-assisted laser desorption ionization?time-of-flight mass spectrometry), determination of D-Rha/L-Rha ratios using gas chromatography (GC), and 1H-NMR analyses including 1H-1H correlation spectra [DQF-COSY (double quantum filtered correlation spectroscopy), TOCSY (total correlation spectroscopy), and NOESY (nuclear Overhauser and exchange spectroscopy)] and 1H-13C correlation spectra [HSQC (heteronuclear single-quantum coherence) and HMBC (heteronuclear multiple bond connectivity)]. |
Protein Glycosylation linked (PGL) gene(s) |
Characterized Accessory Gene(s) | Orf1 and Orf2 are putative glycosyltransferases encoded in the flagellin glycosylation island. |
Literature |
Year of Identification | 2003 |
Year of Identification Month Wise | 2003.3.1 |
Year of Validation | 2006 |
Reference | Takeuchi, K., Ono, H., Yoshida, M., Ishii, T., Katoh, E., Taguchi, F., Miki, R., Murata, K., Kaku, H. and Ichinose, Y., 2007. Flagellin glycans from two pathovars of Pseudomonas syringae contain rhamnose in D and L configurations in different ratios and modified 4-amino-4, 6-dideoxyglucose. Journal of bacteriology, 189(19), pp.6945-6956. |
Corresponding Author | Kasumi Takeuchi |
Contact | National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan. |
Reference | Taguchi, F., Takeuchi, K., Katoh, E., Murata, K., Suzuki, T., Marutani, M., Kawasaki, T., Eguchi, M., Katoh, S., Kaku, H. and Yasuda, C., 2006. Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cellular microbiology, 8(6), pp.923-938. |
Corresponding Author | Yuki Ichinose |
Contact | Laboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama, 700-8530 Japan. |
Reference | Taguchi, F., Shimizu, R., Inagaki, Y., Toyoda, K., Shiraishi, T. and Ichinose, Y., 2003. Post-translational modification of flagellin determines the specificity of HR induction. Plant and cell physiology, 44(3), pp.342-349. |
Corresponding Author | Yuki Ichinose |
Contact | Laboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama, 700-8530 Japan. |