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Distinct regions of the Phytophthora essential effector Avh238 determine its function in cell death activation and plant immunity suppression

New Phytol. 2017 Apr;214(1):361-375. doi: 10.1111/nph.14430. Epub 2017 Jan 30.

Abstract

Phytophthora pathogens secrete effectors to manipulate host innate immunity, thus facilitating infection. Among the RXLR effectors highly induced during Phytophthora sojae infection, Avh238 not only contributes to pathogen virulence but also triggers plant cell death. However, the detailed molecular basis of Avh238 functions remains largely unknown. We mapped the regions responsible for Avh238 functions in pathogen virulence and plant cell death induction using a strategy that combines investigation of natural variation and large-scale mutagenesis assays. The correlation between cellular localization and Avh238 functions was also evaluated. We found that the 79th residue (histidine or leucine) of Avh238 determined its cell death-inducing activity, and that the 53 amino acids in its C-terminal region are responsible for promoting Phytophthora infection. Transient expression of Avh238 in Nicotiana benthamiana revealed that nuclear localization is essential for triggering cell death, while Avh238-mediated suppression of INF1-triggered cell death requires cytoplasmic localization. Our results demonstrate that a representative example of an essential Phytophthora RXLR effector can evolve to escape recognition by the host by mutating one nucleotide site, and can also retain plant immunosuppressive activity to enhance pathogen virulence in planta.

Keywords: Phytophthora sojae; RXLR effector; cell death; immunosuppression; localization; virulence.

MeSH terms

  • Amino Acid Sequence
  • Cell Death
  • Cell Nucleus / metabolism
  • Phytophthora / isolation & purification
  • Phytophthora / metabolism*
  • Plant Diseases / immunology
  • Plant Diseases / microbiology
  • Plant Immunity*
  • Plants / immunology*
  • Plants / microbiology*
  • Polymorphism, Genetic
  • Protein Transport
  • Proteins / chemistry
  • Proteins / metabolism*

Substances

  • Proteins