scholarly journals Host Protein BSL1 Associates with Phytophthora infestans RXLR Effector AVR2 and the Solanum demissum Immune Receptor R2 to Mediate Disease Resistance

2012 ◽  
Vol 24 (8) ◽  
pp. 3420-3434 ◽  
Author(s):  
Diane G.O. Saunders ◽  
Susan Breen ◽  
Joe Win ◽  
Sebastian Schornack ◽  
Ingo Hein ◽  
...  
PLoS ONE ◽  
2008 ◽  
Vol 3 (8) ◽  
pp. e2875 ◽  
Author(s):  
Vivianne G. A. A. Vleeshouwers ◽  
Hendrik Rietman ◽  
Pavel Krenek ◽  
Nicolas Champouret ◽  
Carolyn Young ◽  
...  

2019 ◽  
Vol 154 (1) ◽  
pp. 17-29 ◽  
Author(s):  
Charikleia Schoina ◽  
Natalie Verbeek-de Kruif ◽  
Francine Govers ◽  
Klaas Bouwmeester

1944 ◽  
Vol 61 (1) ◽  
pp. 137-147 ◽  
Author(s):  
William Black

The existence in Mexico of blight-resistant species of potato has been known for many years, but they occur in the wild and are quite unsuitable for agricultural purposes. In order to utilise their resistance to disease it is necessary to combine disease resistance with the cropping qualities of cultivated forms while eliminating the undesirable characters which are prominent in the wild forms. Breeding work with this object in view has been in progress at the Scottish Plant Breeding Station for several years, and results obtained in the course of testing progenies for reaction to blight infection are discussed in the following pages.


2015 ◽  
Vol 28 (10) ◽  
pp. 1063-1072 ◽  
Author(s):  
Ryan G. Anderson ◽  
Devdutta Deb ◽  
Kevin Fedkenheuer ◽  
John M. McDowell

Some of the most devastating oomycete pathogens deploy effector proteins, with the signature amino acid motif RXLR, that enter plant cells to promote virulence. Research on the function and evolution of RXLR effectors has been very active over the decade that has transpired since their discovery. Comparative genomics indicate that RXLR genes play a major role in virulence for Phytophthora and downy mildew species. Importantly, gene-for-gene resistance against these oomycete lineages is based on recognition of RXLR proteins. Comparative genomics have revealed several mechanisms through which this resistance can be broken, most notably involving epigenetic control of RXLR gene expression. Structural studies have revealed a core fold that is present in the majority of RXLR proteins, providing a foundation for detailed mechanistic understanding of virulence and avirulence functions. Finally, functional studies have demonstrated that suppression of host immunity is a major function for RXLR proteins. Host protein targets are being identified in a variety of plant cell compartments. Some targets comprise hubs that are also manipulated by bacteria and fungi, thereby revealing key points of vulnerability in the plant immune network.


2016 ◽  
Vol 171 (1) ◽  
pp. 645-657 ◽  
Author(s):  
Lina Yang ◽  
Hazel McLellan ◽  
Shaista Naqvi ◽  
Qin He ◽  
Petra C. Boevink ◽  
...  

2020 ◽  
Vol 229 (1) ◽  
pp. 501-515 ◽  
Author(s):  
Yu Du ◽  
Xiaokang Chen ◽  
Yalu Guo ◽  
Xiaojiang Zhang ◽  
Houxiao Zhang ◽  
...  

2011 ◽  
Vol 190 (3) ◽  
pp. 653-666 ◽  
Author(s):  
Eleanor M. Gilroy ◽  
Rosalind M. Taylor ◽  
Ingo Hein ◽  
Petra Boevink ◽  
Ari Sadanandom ◽  
...  

2015 ◽  
Vol 28 (12) ◽  
pp. 1316-1329 ◽  
Author(s):  
Artemis Giannakopoulou ◽  
John F. C. Steele ◽  
Maria Eugenia Segretin ◽  
Tolga O. Bozkurt ◽  
Ji Zhou ◽  
...  

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.


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