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ID 34111
フルテキストURL
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著者
Takeuchi, Kasumi National Institute of Agrobiological Sciences
Ono, Hiroshi National Food Research Institute
Yoshida, Mitsuru National Food Research Institute
Ishii, Tadashi Forestry and Forest Products Research Institute
Katoh, Etsuko National Institute of Agrobiological Sciences
Taguchi, Fumiko Graduate School of Natural Science and Technology, Okayama University
Miki, Ryuji Graduate School of Natural Science and Technology, Okayama University
Murata, Katsuyoshi National Institute of Agrobiological Sciences
Kaku, Hanae Faculty of Agriculture, Meiji University
Ichinose, Yuki Graduate School of Natural Science and Technology, Okayama University
抄録
Flagellins from Pseudomonas syringae pv. glycinea race 4 and Pseudomonas syringae pv. tabaci 6605 have been found to be glycosylated. Glycosylation of flagellin is essential for bacterial virulence and is also involved in the determination of host specificity. Flagellin glycans from both pathovars were characterized, and common sites of glycosylation were identified on six serine residues (positions 143, 164, 176, 183, 193, and 201). The structure of the glycan at serine 201 (S201) of flagellin from each pathovar was determined by sugar composition analysis, mass spectrometry, and H-1 and C-13 nuclear magnetic resonance spectroscopy. These analyses showed that the S201 glycans from both pathovars were composed of a common unique trisaccharide consisting of two rhamnosyl (Rha) residues and one modified 4-amino-4,6-dideoxyglucosyl (Qui4N) residue, beta-D-Quip4N(3-hydroxy-1-oxobutyl)2Me-(1 -> 3)-alpha-L-Rhap-(1 -> 2)-alpha-L-Rhap. Furthermore, mass analysis suggests that the glycans on each of the six serine residues are composed of similar trisaccharide units. Determination of the enantiomeric ratio of Rha from the flagellin proteins showed that flagellin from P. syringae pv. tabaci 6605 consisted solely Of L-Rha, whereas P. syringae pv. glycinea race 4 flagellin contained both L-Rha and D-Rha at a molar ratio of about 4:1. Taking these findings together with those from our previous study, we conclude that these flagellin glycan structures may be important for the virulence and host specificity of P. syringae.
キーワード
INNATE IMMUNE-RESPONSE
TOLL-LIKE RECEPTOR-5
PV. TABACI
POSTTRANSLATIONAL MODIFICATION
BACTERIAL FLAGELLIN
STRUCTURAL-ANALYSIS
AMINO-ACIDS
GLYCOSYLATION
AERUGINOSA
IDENTIFICATION
備考
Digital Object Identifer:10.1128/JB.00500-07
Published with permission from the copyright holder. This is the author's copy, as published in Journal of Bacteriology, Oct 2007, Volume 189, Issue 19, Pages 6945-6956.
Publisher URL:http://dx.doi.org/10.1128/JB.00500-07
Direct access to Thomson Web of Science record
Copyright © 2007 American Society for Microbiology
発行日
2007-10
出版物タイトル
Journal of Bacteriology
189巻
19号
出版者
American Society for Microbiology
開始ページ
6945
終了ページ
6956
ISSN
0021-9193
NCID
AA0069403X
資料タイプ
学術雑誌論文
言語
English
著作権者
American Society for Microbiology
論文のバージョン
author
査読
有り
DOI
PubMed ID
Web of Sience KeyUT
Submission Path
microbiology_and_immunology/6