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Journal of Bacteriology, December 2003, p. 7092-7102, Vol. 185, No. 24
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.24.7092-7102.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

XopC and XopJ, Two Novel Type III Effector Proteins from Xanthomonas campestris pv. vesicatoria

Laurent Noël,{dagger} Frank Thieme, Jana Gäbler,{ddagger} Daniela Büttner, and Ulla Bonas*

Institute of Genetics, Martin-Luther-University Halle-Wittenberg, D-06099 Halle (Saale), Germany

Received 23 July 2003/ Accepted 18 September 2003

Pathogenicity of the gram-negative plant pathogen Xanthomonas campestris pv. vesicatoria depends on a type III secretion (TTS) system which translocates bacterial effector proteins into the plant cell. Previous transcriptome analysis identified a genome-wide regulon of putative virulence genes that are coexpressed with the TTS system. In this study, we characterized two of these genes, xopC and xopJ. Both genes encode Xanthomonas outer proteins (Xops) that were shown to be secreted by the TTS system. In addition, type III-dependent translocation of both proteins into the plant cell was demonstrated using the AvrBs3 effector domain as a reporter. XopJ belongs to the AvrRxv/YopJ family of effector proteins from plant and animal pathogenic bacteria. By contrast, XopC does not share significant homology to proteins in the database. Sequence analysis revealed that the xopC locus contains several features that are reminiscent of pathogenicity islands. Interestingly, the xopC region is flanked by 62-bp inverted repeats that are also associated with members of the Xanthomonas avrBs3 effector family. Besides xopC, a second gene of the locus, designated hpaJ, was shown to be coexpressed with the TTS system. hpaJ encodes a protein with similarity to transglycosylases and to the Pseudomonas syringae pv. maculicola protein HopPmaG. HpaJ secretion and translocation by the X. campestris pv. vesicatoria TTS system was not detectable, which is consistent with its predicted Sec signal and a putative function as transglycosylase in the bacterial periplasm.

* Corresponding author. Mailing address: Institute of Genetics, Martin-Luther-University Halle-Wittenberg, D-06099 Halle (Saale), Germany. Phone: (49) 345 5526290. Fax: (49) 345 5527277. E-mail: bonas{at}genetik.uni-halle.de.

{dagger} Present address: Max-Planck-Institute for Plant Breeding Research, D-50829 Cologne, Germany.

{ddagger} Present address: Division of Cellular Immunology, German Cancer Research Center, D-69120 Heidelberg, Germany.

Journal of Bacteriology, December 2003, p. 7092-7102, Vol. 185, No. 24
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.24.7092-7102.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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