TY - JOUR
T1 - Tomato I2 immune receptor can be engineered to confer partial resistance to the oomycete phytophthora infestans in addition to the fungus fusarium oxysporum
AU - Giannakopoulou, Artemis
AU - Steele, John F C
AU - Segretin, Maria Eugenia
AU - Bozkurt, Tolga O.
AU - Zhou, Ji
AU - Robatzek, Silke
AU - Banfield, Mark J.
AU - Pais, Marina
AU - Kamoun, Sophien
PY - 2015/12
Y1 - 2015/12
N2 - Plants and animals rely on immune receptors, known as nucleotide-binding domain and leucine-rich repeat (NLR)-containing proteins, to defend against invading pathogens and activate immune responses. How NLR receptors respond to pathogens is inadequately understood. We previously reported single-residue mutations that expand the response of the potato immune receptor R3a to AVR3aEM, a stealthy effector from the late blight oomycete pathogen Phytophthora infestans. I2, another NLR that mediates resistance to the wilt-causing fungus Fusarium oxysporum f. sp. lycopersici, is the tomato ortholog of R3a. We transferred previously identified R3a mutations to I2 to assess the degree to which the resulting I2 mutants have an altered response. We discovered that wild-Type I2 protein responds weakly to AVR3a. One mutant in the N-Terminal coiled-coil domain, I2I141N, appeared sensitized and displayed markedly increased response to AVR3a. Remarkably, I2I141N conferred partial resistance to P. infestans. Further, I2I141N has an expanded response spectrum to F. oxysporum f. sp. lycopersici effectors compared with the wild-Type I2 protein. Our results suggest that synthetic immune receptors can be engineered to confer resistance to phylogenetically divergent pathogens and indicate that knowledge gathered for one NLR could be exploited to improve NLR from other plant species.
AB - Plants and animals rely on immune receptors, known as nucleotide-binding domain and leucine-rich repeat (NLR)-containing proteins, to defend against invading pathogens and activate immune responses. How NLR receptors respond to pathogens is inadequately understood. We previously reported single-residue mutations that expand the response of the potato immune receptor R3a to AVR3aEM, a stealthy effector from the late blight oomycete pathogen Phytophthora infestans. I2, another NLR that mediates resistance to the wilt-causing fungus Fusarium oxysporum f. sp. lycopersici, is the tomato ortholog of R3a. We transferred previously identified R3a mutations to I2 to assess the degree to which the resulting I2 mutants have an altered response. We discovered that wild-Type I2 protein responds weakly to AVR3a. One mutant in the N-Terminal coiled-coil domain, I2I141N, appeared sensitized and displayed markedly increased response to AVR3a. Remarkably, I2I141N conferred partial resistance to P. infestans. Further, I2I141N has an expanded response spectrum to F. oxysporum f. sp. lycopersici effectors compared with the wild-Type I2 protein. Our results suggest that synthetic immune receptors can be engineered to confer resistance to phylogenetically divergent pathogens and indicate that knowledge gathered for one NLR could be exploited to improve NLR from other plant species.
UR - http://www.scopus.com/inward/record.url?scp=84951844034&partnerID=8YFLogxK
U2 - 10.1094/MPMI-07-15-0147-R
DO - 10.1094/MPMI-07-15-0147-R
M3 - Article
C2 - 26367241
AN - SCOPUS:84951844034
SN - 0894-0282
VL - 28
SP - 1316
EP - 1329
JO - Molecular Plant-Microbe Interactions
JF - Molecular Plant-Microbe Interactions
IS - 12
ER -