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Defense responses of Arabidopsis thaliana inoculated with Pseudomonas syringae pv. tabaci wild type and defective mutants for flagellin (ΔfliC) and flagellin-glycosylation (Δorf1)

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Abstract

Flagellin, an essential component of the bacterial flagellar filament, is capable of inducing a hypersensitive response (HR), including cell death, in a nonhost plant. A flagellin-defective mutant (ΔfliC) of Pseudomonas syringae pv. tabaci lacks both the flagellar filament and motility, whereas a flagellin-glycosylation-defective mutant (Δorf1) retains the flagellar filament but lacks the glycosyl modification of flagellin protein. To investigate the role of flagellin protein and its glycosylation in the interaction with its nonhost Arabidopsis thaliana, we analyzed plant responses after inoculation with these bacteria. Inoculation with wild-type P. syringae pv. tabaci induced HR, with the generation of reactive oxygen species and cell death. In contrast, inoculation with either ΔfliC or Δorf1 mutant induced a low level of HR, and inoculated leaves developed a disease-like yellowing. These mutant bacteria multiplied better than the wild-type bacteria in A. thaliana. These results indicate that A. thaliana expresses a defense reaction in response to the bacterial flagellin with its glycosyl structure.

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Authors and Affiliations

  1. Laboratory of Plant Pathology and Genetic Engineering, Faculty of Agriculture, Okayama University, 1-1-1 Tsushima-naka, Okayama, 700-8530, Japan

    Yasuhiro Ishiga, Kasumi Takeuchi, Fumiko Taguchi, Yoshishige Inagaki, Kazuhiro Toyoda, Tomonori Shiraishi & Yuki Ichinose

  2. Genebank, National Institute of Agrobiological Science, Tsukuba, Japan

    Kasumi Takeuchi

Authors
  1. Yasuhiro Ishiga
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  2. Kasumi Takeuchi
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  3. Fumiko Taguchi
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  4. Yoshishige Inagaki
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  5. Kazuhiro Toyoda
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  6. Tomonori Shiraishi
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  7. Yuki Ichinose
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Correspondence to Yuki Ichinose.

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Ishiga, Y., Takeuchi, K., Taguchi, F. et al. Defense responses of Arabidopsis thaliana inoculated with Pseudomonas syringae pv. tabaci wild type and defective mutants for flagellin (ΔfliC) and flagellin-glycosylation (Δorf1). J Gen Plant Pathol 71, 302–307 (2005). https://doi.org/10.1007/s10327-005-0201-8

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  • DOI: https://doi.org/10.1007/s10327-005-0201-8

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