The magnaporthe oryzae effector avrpiz-t targets the RING E3 ubiquitin ligase APIP6 to suppress pathogen-associated molecular pattern-triggered immunity in rices W OA

Chan Ho Park, Songbiao Chen, Gautam Shirsekar, Bo Zhou, Chang Hyun Khang, Pattavipha Songkumarn, Ahmed Afzal, Yuese Ning, Ruyi Wang, Maria Bellizzi, Barbara Valent, Guo Liang Wang

Research output: Contribution to journalArticle

Abstract

Although the functions of a few effector proteins produced by bacterial and oomycete plant pathogens have been elucidated in recent years, information for the vast majority of pathogen effectors is still lacking, particularly for those of plant-pathogenic fungi. Here, we show that the avirulence effector AvrPiz-t from the rice blast fungus Magnaporthe oryzae preferentially accumulates in the specialized structure called the biotrophic interfacial complex and is then translocated into rice (Oryza sativa) cells. Ectopic expression of AvrPiz-t in transgenic rice suppresses the flg22- and chitin-induced generation of reactive oxygen species (ROS) and enhances susceptibility to M. oryzae, indicating that AvrPiz-t functions to suppress pathogen-associated molecular pattern (PAMP)-triggered immunity in rice. Interaction assays show that AvrPiz-t suppresses the ubiquitin ligase activity of the rice RING E3 ubiquitin ligase APIP6 and that, in return, APIP6 ubiquitinates AvrPiz-t in vitro. Interestingly, agroinfection assays reveal that AvrPiz-t and AvrPiz-t Interacting Protein 6 (APIP6) are both degraded when coexpressed in Nicotiana benthamiana. Silencing of APIP6 in transgenic rice leads to a significant reduction of flg22-induced ROS generation, suppression of defense-related gene expression, and enhanced susceptibility of rice plants to M. oryzae. Taken together, our results reveal a mechanism in which a fungal effector targets the host ubiquitin proteasome system for the suppression of PAMP-triggered immunity in plants.

Original languageEnglish (US)
Pages (from-to)4748-4762
Number of pages15
JournalPlant Cell
Volume24
Issue number11
DOIs
StatePublished - Nov 1 2012

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Magnaporthe
Magnaporthe oryzae
ubiquitin-protein ligase
Ubiquitin-Protein Ligases
Immunity
immunity
rice
pathogens
Proteins
proteins
ubiquitin
reactive oxygen species
genetically modified organisms
blast disease
Nicotiana benthamiana
Oomycetes
plant pathogenic fungi
proteasome endopeptidase complex
assays
chitin

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology

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The magnaporthe oryzae effector avrpiz-t targets the RING E3 ubiquitin ligase APIP6 to suppress pathogen-associated molecular pattern-triggered immunity in rices W OA . / Park, Chan Ho; Chen, Songbiao; Shirsekar, Gautam; Zhou, Bo; Khang, Chang Hyun; Songkumarn, Pattavipha; Afzal, Ahmed; Ning, Yuese; Wang, Ruyi; Bellizzi, Maria; Valent, Barbara; Wang, Guo Liang.

In: Plant Cell, Vol. 24, No. 11, 01.11.2012, p. 4748-4762.

Research output: Contribution to journalArticle

Park, CH, Chen, S, Shirsekar, G, Zhou, B, Khang, CH, Songkumarn, P, Afzal, A, Ning, Y, Wang, R, Bellizzi, M, Valent, B & Wang, GL 2012, ' The magnaporthe oryzae effector avrpiz-t targets the RING E3 ubiquitin ligase APIP6 to suppress pathogen-associated molecular pattern-triggered immunity in rices W OA ', Plant Cell, vol. 24, no. 11, pp. 4748-4762. https://doi.org/10.1105/tpc.112.105429
Park, Chan Ho ; Chen, Songbiao ; Shirsekar, Gautam ; Zhou, Bo ; Khang, Chang Hyun ; Songkumarn, Pattavipha ; Afzal, Ahmed ; Ning, Yuese ; Wang, Ruyi ; Bellizzi, Maria ; Valent, Barbara ; Wang, Guo Liang. / The magnaporthe oryzae effector avrpiz-t targets the RING E3 ubiquitin ligase APIP6 to suppress pathogen-associated molecular pattern-triggered immunity in rices W OA In: Plant Cell. 2012 ; Vol. 24, No. 11. pp. 4748-4762.
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AU - Chen, Songbiao

AU - Shirsekar, Gautam

AU - Zhou, Bo

AU - Khang, Chang Hyun

AU - Songkumarn, Pattavipha

AU - Afzal, Ahmed

AU - Ning, Yuese

AU - Wang, Ruyi

AU - Bellizzi, Maria

AU - Valent, Barbara

AU - Wang, Guo Liang

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