Phytophthora infestans RXLR effector SFI5 requires association with calmodulin for PTI/MTI suppressing activity

Xiangzi Zheng, Nadine Wagener, Hazel McLellan, Petra C. Boevink, Chenlei Hua, Paul R. J. Birch, Frédéric Brunner (Lead / Corresponding author)

Research output: Contribution to journalArticle

6 Citations (Scopus)
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Abstract

Pathogens secrete effector proteins to interfere with plant innate immunity, in which Ca2+ /calmodulin (CaM) signalling plays key roles. Thus far, few effectors have been identified that directly interact with CaM for defence suppression. Here, we report that SFI5, an RXLR effector from Phytophthora infestans, suppresses microbe-associated molecular pattern (MAMP)-triggered immunity (MTI) by interacting with host CaMs. We predicted the CaM-binding site in SFI5 using in silico analysis. The interaction between SFI5 and CaM was tested by both in vitro and in vivo assays. MTI suppression by SFI5 and truncated variants were performed in a tomato protoplast system. We found that both the predicted CaM-binding site and the full-length SFI5 protein interact with CaM in the presence of Ca2+ . MTI responses, such as FRK1 upregulation, reactive oxygen species accumulation, and mitogen-activated protein kinase activation were suppressed by truncated SFI5 proteins containing the C-terminal CaM-binding site but not by those without it. The plasma membrane localization of SFI5 and its ability to enhance infection were also perturbed by loss of the CaM-binding site. We conclude that CaM-binding is required for localization and activity of SFI5. We propose that SFI5 suppresses plant immunity by interfering with immune signalling components after activation by CaMs.

Original languageEnglish
Pages (from-to)1433-1446
Number of pages14
JournalNew Phytologist
Volume219
Issue number4
Early online date22 Jun 2018
DOIs
Publication statusPublished - 1 Sep 2018

Fingerprint

Phytophthora infestans
calmodulin
Calmodulin
Immunity
immunity
binding sites
Plant Immunity
Binding Sites
calcium
proteins
Protoplasts
Lycopersicon esculentum
Protein C
Mitogen-Activated Protein Kinases
mitogen-activated protein kinase
Innate Immunity
Computer Simulation
protoplasts
reactive oxygen species
Reactive Oxygen Species

Keywords

  • calcium
  • calmodulin
  • MAMP-triggered immunity (MTI)
  • RXLR effector
  • SFI5
  • tomato protoplast
  • virulence

Cite this

Zheng, Xiangzi ; Wagener, Nadine ; McLellan, Hazel ; Boevink, Petra C. ; Hua, Chenlei ; Birch, Paul R. J. ; Brunner, Frédéric. / Phytophthora infestans RXLR effector SFI5 requires association with calmodulin for PTI/MTI suppressing activity. In: New Phytologist. 2018 ; Vol. 219, No. 4. pp. 1433-1446.
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Phytophthora infestans RXLR effector SFI5 requires association with calmodulin for PTI/MTI suppressing activity. / Zheng, Xiangzi; Wagener, Nadine; McLellan, Hazel; Boevink, Petra C.; Hua, Chenlei; Birch, Paul R. J.; Brunner, Frédéric (Lead / Corresponding author).

In: New Phytologist, Vol. 219, No. 4, 01.09.2018, p. 1433-1446.

Research output: Contribution to journalArticle

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T1 - Phytophthora infestans RXLR effector SFI5 requires association with calmodulin for PTI/MTI suppressing activity

AU - Zheng, Xiangzi

AU - Wagener, Nadine

AU - McLellan, Hazel

AU - Boevink, Petra C.

AU - Hua, Chenlei

AU - Birch, Paul R. J.

AU - Brunner, Frédéric

N1 - © 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.

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Y1 - 2018/9/1

N2 - Pathogens secrete effector proteins to interfere with plant innate immunity, in which Ca2+ /calmodulin (CaM) signalling plays key roles. Thus far, few effectors have been identified that directly interact with CaM for defence suppression. Here, we report that SFI5, an RXLR effector from Phytophthora infestans, suppresses microbe-associated molecular pattern (MAMP)-triggered immunity (MTI) by interacting with host CaMs. We predicted the CaM-binding site in SFI5 using in silico analysis. The interaction between SFI5 and CaM was tested by both in vitro and in vivo assays. MTI suppression by SFI5 and truncated variants were performed in a tomato protoplast system. We found that both the predicted CaM-binding site and the full-length SFI5 protein interact with CaM in the presence of Ca2+ . MTI responses, such as FRK1 upregulation, reactive oxygen species accumulation, and mitogen-activated protein kinase activation were suppressed by truncated SFI5 proteins containing the C-terminal CaM-binding site but not by those without it. The plasma membrane localization of SFI5 and its ability to enhance infection were also perturbed by loss of the CaM-binding site. We conclude that CaM-binding is required for localization and activity of SFI5. We propose that SFI5 suppresses plant immunity by interfering with immune signalling components after activation by CaMs.

AB - Pathogens secrete effector proteins to interfere with plant innate immunity, in which Ca2+ /calmodulin (CaM) signalling plays key roles. Thus far, few effectors have been identified that directly interact with CaM for defence suppression. Here, we report that SFI5, an RXLR effector from Phytophthora infestans, suppresses microbe-associated molecular pattern (MAMP)-triggered immunity (MTI) by interacting with host CaMs. We predicted the CaM-binding site in SFI5 using in silico analysis. The interaction between SFI5 and CaM was tested by both in vitro and in vivo assays. MTI suppression by SFI5 and truncated variants were performed in a tomato protoplast system. We found that both the predicted CaM-binding site and the full-length SFI5 protein interact with CaM in the presence of Ca2+ . MTI responses, such as FRK1 upregulation, reactive oxygen species accumulation, and mitogen-activated protein kinase activation were suppressed by truncated SFI5 proteins containing the C-terminal CaM-binding site but not by those without it. The plasma membrane localization of SFI5 and its ability to enhance infection were also perturbed by loss of the CaM-binding site. We conclude that CaM-binding is required for localization and activity of SFI5. We propose that SFI5 suppresses plant immunity by interfering with immune signalling components after activation by CaMs.

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JF - New Phytologist

SN - 0028-646X

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