JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Takeuchi, K.
Right arrow Articles by Ichinose, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Takeuchi, K.
Right arrow Articles by Ichinose, Y.
Journal of Bacteriology, November 2003, p. 6658-6665, Vol. 185, No. 22
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.22.6658-6665.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Flagellin Glycosylation Island in Pseudomonas syringae pv. glycinea and Its Role in Host Specificity

Kasumi Takeuchi,1,2 Fumiko Taguchi,1 Yoshishige Inagaki,1 Kazuhiro Toyoda,1 Tomonori Shiraishi,1 and Yuki Ichinose1*

Laboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama 700-8530,1 Laboratory of Microorganism Genetic Resources, Genebank, National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan2

Received 30 May 2003/ Accepted 17 August 2003

The deduced amino acid sequences of the flagellins of Pseudomonas syringae pv. tabaci and P. syringae pv. glycinea are identical; however, their abilities to induce a hypersensitive reaction are clearly different. The reason for the difference seems to depend on the posttranslational modification of the flagellins. To investigate the role of this posttranslational modification in the interactions between plants and bacterial pathogens, we isolated genes that are potentially involved in the posttranslational modification of flagellin in P. syringae pv. glycinea (glycosylation island); then defective mutants with mutations in these genes were generated. There are three open reading frames in the glycosylation island, designated orf1, orf2, and orf3. orf1 and orf2 encode putative glycosyltransferases, and mutants with defects in these open reading frames, {Delta}orf1 and {Delta}orf2, secreted nonglycosylated and slightly glycosylated flagellins, respectively. Inoculation tests performed with these mutants and original nonhost tobacco leaves revealed that {Delta}orf1 and {Delta}orf2 could grow on tobacco leaves and caused symptom-like changes. In contrast, these mutants failed to cause symptoms on original host soybean leaves. These data indicate that putative glycosyltransferases encoded in the flagellin glycosylation island are strongly involved in recognition by plants and could be the specific determinants of compatibility between phytopathogenic bacteria and plant species.


* Corresponding author. Mailing address: Laboratory of Plant Pathology & Genetic Engineering, Faculty of Agriculture, Okayama University, Tsushima-naka 1-1-1, Okayama 700-8530, Japan. Phone and fax: (81) 86-251-8308. E-mail: yuki{at}cc.okayama-u.ac.jp.


Journal of Bacteriology, November 2003, p. 6658-6665, Vol. 185, No. 22
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.22.6658-6665.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2003 by the American Society for Microbiology. All rights reserved.