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The structural basis for activation of plant immunity by bacterial effector protein AvrPto

Author

Listed:
  • Weiman Xing

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China
    Institute of Biophysics)

  • Yan Zou

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China
    Institute of Genetics and Developmental Biology, Chinese Academy of Sciences)

  • Qun Liu

    (Cornell High-Energy Synchrotron Source, Cornell University, Ithaca, New York 14853, USA)

  • Jianing Liu

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

  • Xi Luo

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

  • Qingqiu Huang

    (Institute of Genetics and Developmental Biology, Chinese Academy of Sciences)

  • She Chen

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

  • Lihuang Zhu

    (Institute of Genetics and Developmental Biology, Chinese Academy of Sciences)

  • Ruchang Bi

    (Institute of Biophysics)

  • Quan Hao

    (Cornell High-Energy Synchrotron Source, Cornell University, Ithaca, New York 14853, USA)

  • Jia-Wei Wu

    (Tsinghua University, 100084, Beijing, China)

  • Jian-Min Zhou

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

  • Jijie Chai

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

Abstract

Plant versus microbe Many microbial plant pathogens have evolved effector proteins that enhance virulence by neutralizing host-plant defences. Plants have countered by developing highly specific resistance proteins that recognize an effector and limit the infection, often by inducing localized cell death. The crystal structure of one of these effectors, AvrPto from Pseudomonas syringae, bound to the Pto kinase that confers resistance to bacterial speck disease in tomato plants has now been determined. The nature of their interaction suggests that Pto may have evolved as a mimic of the virulence target of AvrPto.

Suggested Citation

  • Weiman Xing & Yan Zou & Qun Liu & Jianing Liu & Xi Luo & Qingqiu Huang & She Chen & Lihuang Zhu & Ruchang Bi & Quan Hao & Jia-Wei Wu & Jian-Min Zhou & Jijie Chai, 2007. "The structural basis for activation of plant immunity by bacterial effector protein AvrPto," Nature, Nature, vol. 449(7159), pages 243-247, September.
    • Handle: RePEc:nat:nature:v:449:y:2007:i:7159:d:10.1038_nature06109
    DOI: 10.1038/nature06109
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