ID | 34111 |
FullText URL | |
Author |
Takeuchi, Kasumi
Ono, Hiroshi
Yoshida, Mitsuru
Ishii, Tadashi
Katoh, Etsuko
Taguchi, Fumiko
Miki, Ryuji
Murata, Katsuyoshi
Kaku, Hanae
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Abstract | 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.
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Keywords | INNATE IMMUNE-RESPONSE
TOLL-LIKE RECEPTOR-5
PV. TABACI
POSTTRANSLATIONAL MODIFICATION
BACTERIAL FLAGELLIN
STRUCTURAL-ANALYSIS
AMINO-ACIDS
GLYCOSYLATION
AERUGINOSA
IDENTIFICATION
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Note | 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 |
Published Date | 2007-10
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Publication Title |
Journal of Bacteriology
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Volume | volume189
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Issue | issue19
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Publisher | American Society for Microbiology
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Start Page | 6945
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End Page | 6956
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ISSN | 0021-9193
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NCID | AA0069403X
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Content Type |
Journal Article
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language |
English
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Copyright Holders | American Society for Microbiology
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File Version | author
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Refereed |
True
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DOI | |
PubMed ID | |
Web of Science KeyUT | |
Submission Path | microbiology_and_immunology/6
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