TY - JOUR
T1 - Evolutionarily distinct resistance proteins detect a pathogen effector through its association with different host targets
AU - Wang, Haixia
AU - Trusch, Franziska
AU - Turnbull, Dionne
AU - Aguilera-Galvez, Carolina
AU - Breen, Susan
AU - Naqvi, Shaista
AU - Jones, Jonathan D. G.
AU - Hein, Ingo
AU - Tian, Zhendong
AU - Vleeshouwers, Vivianne
AU - Gilroy, Eleanor
AU - Birch, Paul R. J.
N1 - Funding Information: We are thankful for financial support from the Biotechnology and Biological Sciences Research Council (BBSRC) grants BB/P020569/1, BB/N009967/1 and BB/L026880/1, ERC‐Advanced grant PathEVome (787764), the Scottish Government Rural and Environment Science and Analytical Services Division (RESAS) and the National Natural Science Foundation of China (31761143007).
PY - 2021/11
Y1 - 2021/11
N2 - Knowledge of the evolutionary processes which govern pathogen recognition is critical to understanding durable disease resistance. We determined how Phytophthora infestans effector PiAVR2 is recognised by evolutionarily distinct resistance proteins R2 and Rpi-mcq1. We employed yeast two-hybrid, co-immunoprecipitation, virus-induced gene silencing, transient overexpression, and phosphatase activity assays to investigate the contributions of BSL phosphatases to R2- and Rpi-mcq1-mediated hypersensitive response (R2 HR and Rpi-mcq1 HR, respectively). Silencing PiAVR2 target BSL1 compromises R2 HR. Rpi-mcq1 HR is compromised only when BSL2 and BSL3 are silenced. BSL1 overexpression increases R2 HR and compromises Rpi-mcq1. However, overexpression of BSL2 or BSL3 enhances Rpi-mcq1 and compromises R2 HR. Okadaic acid, which inhibits BSL phosphatase activity, suppresses both recognition events. Moreover, expression of a BSL1 phosphatase-dead (PD) mutant suppresses R2 HR, whereas BSL2-PD and BSL3-PD mutants suppress Rpi-mcq1 HR. R2 interacts with BSL1 in the presence of PiAVR2, but not with BSL2 and BSL3, whereas no interactions were detected between Rpi-mcq1 and BSLs. Thus, BSL1 activity and association with R2 determine recognition of PiAVR2 by R2, whereas BSL2 and BSL3 mediate Rpi-mcq1 perception of PiAVR2. R2 and Rpi-mcq1 utilise distinct mechanisms to detect PiAVR2 based on association with different BSLs, highlighting central roles of these effector targets for both disease and disease resistance.
AB - Knowledge of the evolutionary processes which govern pathogen recognition is critical to understanding durable disease resistance. We determined how Phytophthora infestans effector PiAVR2 is recognised by evolutionarily distinct resistance proteins R2 and Rpi-mcq1. We employed yeast two-hybrid, co-immunoprecipitation, virus-induced gene silencing, transient overexpression, and phosphatase activity assays to investigate the contributions of BSL phosphatases to R2- and Rpi-mcq1-mediated hypersensitive response (R2 HR and Rpi-mcq1 HR, respectively). Silencing PiAVR2 target BSL1 compromises R2 HR. Rpi-mcq1 HR is compromised only when BSL2 and BSL3 are silenced. BSL1 overexpression increases R2 HR and compromises Rpi-mcq1. However, overexpression of BSL2 or BSL3 enhances Rpi-mcq1 and compromises R2 HR. Okadaic acid, which inhibits BSL phosphatase activity, suppresses both recognition events. Moreover, expression of a BSL1 phosphatase-dead (PD) mutant suppresses R2 HR, whereas BSL2-PD and BSL3-PD mutants suppress Rpi-mcq1 HR. R2 interacts with BSL1 in the presence of PiAVR2, but not with BSL2 and BSL3, whereas no interactions were detected between Rpi-mcq1 and BSLs. Thus, BSL1 activity and association with R2 determine recognition of PiAVR2 by R2, whereas BSL2 and BSL3 mediate Rpi-mcq1 perception of PiAVR2. R2 and Rpi-mcq1 utilise distinct mechanisms to detect PiAVR2 based on association with different BSLs, highlighting central roles of these effector targets for both disease and disease resistance.
KW - avirulence
KW - cell death
KW - effector-triggered immunity
KW - NLR
KW - plant immunity
KW - plant pathogen co-evolution
KW - potato late blight
KW - resistance protein
UR - http://www.scopus.com/inward/record.url?scp=85112796147&partnerID=8YFLogxK
U2 - 10.1111/nph.17660
DO - 10.1111/nph.17660
M3 - Article
C2 - 34339518
AN - SCOPUS:85112796147
SN - 0028-646X
VL - 232
SP - 1368
EP - 1381
JO - New Phytologist
JF - New Phytologist
IS - 3
ER -