NLR immune receptor–nanobody fusions confer plant disease resistance
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S. Kamoun | Jiorgos Kourelis | Clémence Marchal | A. Harant | Andres Posbeyikian | Andrés Posbeyikian
[1] R. Terauchi,et al. Effector target-guided engineering of an integrated domain expands the disease resistance profile of a rice NLR immune receptor , 2023, eLife.
[2] C. Stevenson,et al. Allelic compatibility in plant immune receptors facilitates engineering of new effector recognition specificities , 2022, bioRxiv.
[3] T. Kroj,et al. New recognition specificity in a plant immune receptor by molecular engineering of its integrated domain , 2022, Nature Communications.
[4] Shanshan Wang,et al. Novel effector recognition capacity engineered into a paired NLR complex , 2021, bioRxiv.
[5] R. Terauchi,et al. Functional diversification gave rise to allelic specialization in a rice NLR immune receptor pair , 2021, bioRxiv.
[6] R. Liu,et al. Structural insights into the binding of nanobodies LaM2 and LaM4 to the red fluorescent protein mCherry , 2021, Protein science : a publication of the Protein Society.
[7] C. Cepko,et al. A general approach for stabilizing nanobodies for intracellular expression , 2021, bioRxiv.
[8] R. Terauchi,et al. Two NLR immune receptors acquired high-affinity binding to a fungal effector through convergent evolution of their integrated domain , 2021, bioRxiv.
[9] B. Steuernagel,et al. A five-transgene cassette confers broad-spectrum resistance to a fungal rust pathogen in wheat , 2021, Nature Biotechnology.
[10] M. Banfield,et al. The allelic rice immune receptor Pikh confers extended resistance to strains of the blast fungus through a single polymorphism in the effector binding interface , 2020, bioRxiv.
[11] R. Terauchi,et al. The rice NLR pair Pikp-1/Pikp-2 initiates cell death through receptor cooperation rather than negative regulation , 2020, bioRxiv.
[12] M. Hattori,et al. Structure-based engineering of anti-GFP nanobody tandems as ultra-high-affinity reagents for purification , 2020, Scientific Reports.
[13] A. Bak,et al. Optimizing the PBS1 Decoy System to Confer Resistance to Potyvirus Infection in Arabidopsis and Soybean , 2020, bioRxiv.
[14] S. Kamoun,et al. An N-terminal motif in NLR immune receptors is functionally conserved across distantly related plant species , 2019, bioRxiv.
[15] R. Terauchi,et al. Protein engineering expands the effector recognition profile of a rice NLR immune receptor , 2019, bioRxiv.
[16] Y. Qi,et al. Ligand-triggered allosteric ADP release primes a plant NLR complex , 2019, Science.
[17] Jose C. Tovar,et al. Stacking three late blight resistance genes from wild species directly into African highland potato varieties confers complete field resistance to local blight races , 2018, Plant biotechnology journal.
[18] You-Liang Peng,et al. Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces , 2018, Proceedings of the National Academy of Sciences.
[19] R. Terauchi,et al. Polymorphic residues in rice NLRs expand binding and response to effectors of the blast pathogen , 2018, Nature Plants.
[20] Harald Kolmar,et al. Camelid and shark single domain antibodies: structural features and therapeutic potential. , 2017, Current opinion in structural biology.
[21] D. Weigel,et al. Activation of a Plant NLR Complex through Heteromeric Association with an Autoimmune Risk Variant of Another NLR , 2017, Current Biology.
[22] Hadley Wickham,et al. ggplot2 - Elegant Graphics for Data Analysis (2nd Edition) , 2017 .
[23] Jonathan D. G. Jones,et al. Comparative analysis of plant immune receptor architectures uncovers host proteins likely targeted by pathogens , 2016, BMC Biology.
[24] S. H. Kim,et al. Using decoys to expand the recognition specificity of a plant disease resistance protein , 2016, Science.
[25] T. Kroj,et al. Integration of decoy domains derived from protein targets of pathogen effectors into plant immune receptors is widespread , 2016, The New phytologist.
[26] R. Terauchi,et al. Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor , 2015, eLife.
[27] S. Robatzek,et al. Tomato I2 immune receptor can be engineered to confer partial resistance to the oomycete Phytophthora infestans in addition to the fungus Fusarium oxysporum , 2015, bioRxiv.
[28] Jonathan D. G. Jones,et al. A Plant Immune Receptor Detects Pathogen Effectors that Target WRKY Transcription Factors , 2015, Cell.
[29] H. Yoshioka,et al. A Receptor Pair with an Integrated Decoy Converts Pathogen Disabling of Transcription Factors to Immunity , 2015, Cell.
[30] R. Terauchi,et al. The “sensor domains” of plant NLR proteins: more than decoys? , 2015, Front. Plant Sci..
[31] G. Rätsch,et al. Species-wide Genetic Incompatibility Analysis Identifies Immune Genes as Hot Spots of Deleterious Epistasis , 2014, Cell.
[32] David Fenyö,et al. A robust pipeline for rapid production of versatile nanobody repertoires , 2014, Nature Methods.
[33] T. Kroj,et al. A novel conserved mechanism for plant NLR protein pairs: the “integrated decoy” hypothesis , 2014, Front. Plant Sci..
[34] B. Keller,et al. The powdery mildew resistance gene Pm8 derived from rye is suppressed by its wheat ortholog Pm3. , 2014, The Plant journal : for cell and molecular biology.
[35] M. Banfield,et al. Single amino acid mutations in the potato immune receptor R3a expand response to Phytophthora effectors. , 2014, Molecular plant-microbe interactions : MPMI.
[36] Nicola J. Patron,et al. A golden gate modular cloning toolbox for plants. , 2014, ACS synthetic biology.
[37] Juan Du,et al. Agroinfiltration and PVX Agroinfection in Potato and Nicotiana benthamiana , 2014, Journal of visualized experiments : JoVE.
[38] J. Dangl,et al. Pivoting the Plant Immune System from Dissection to Deployment , 2013, Science.
[39] Serge Muyldermans,et al. Nanobodies: natural single-domain antibodies. , 2013, Annual review of biochemistry.
[40] R. Terauchi,et al. The Rice Resistance Protein Pair RGA4/RGA5 Recognizes the Magnaporthe oryzae Effectors AVR-Pia and AVR1-CO39 by Direct Binding[W][OA] , 2013, Plant Cell.
[41] R. Terauchi,et al. Arms race co-evolution of Magnaporthe oryzae AVR-Pik and rice Pik genes driven by their physical interactions. , 2012, The Plant journal : for cell and molecular biology.
[42] R. Visser,et al. Functional stacking of three resistance genes against Phytophthora infestans in potato , 2011, Transgenic Research.
[43] Ernst Weber,et al. A Modular Cloning System for Standardized Assembly of Multigene Constructs , 2011, PloS one.
[44] J. Dangl,et al. NB-LRR proteins: pairs, pieces, perception, partners, and pathways. , 2010, Current opinion in plant biology.
[45] F. Takken,et al. To Nibble at Plant Resistance Proteins , 2009, Science.
[46] H. Matsumura,et al. Association Genetics Reveals Three Novel Avirulence Genes from the Rice Blast Fungal Pathogen Magnaporthe oryzae[W][OA] , 2009, The Plant Cell Online.
[47] M. Yano,et al. Two Adjacent Nucleotide-Binding Site–Leucine-Rich Repeat Class Genes Are Required to Confer Pikm-Specific Rice Blast Resistance , 2008, Genetics.
[48] Heinrich Leonhardt,et al. Targeting and tracing antigens in live cells with fluorescent nanobodies , 2006, Nature Methods.
[49] L. Wyns,et al. Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies. , 2005, Journal of molecular biology.
[50] Jonathan D. G. Jones,et al. Structure–Function Analysis of Cf-9, a Receptor-Like Protein with Extracytoplasmic Leucine-Rich Repeatsw⃞ , 2005, The Plant Cell Online.
[51] D. Baulcombe,et al. High throughput virus‐induced gene silencing implicates heat shock protein 90 in plant disease resistance , 2003, The EMBO journal.
[52] S. Dinesh-Kumar,et al. Structure-function analysis of the tobacco mosaic virus resistance gene N. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[53] P. D. de Wit,et al. Agroinfiltration is a versatile tool that facilitates comparative analyses of Avr9/Cf-9-induced and Avr4/Cf-4-induced necrosis. , 2000, Molecular plant-microbe interactions : MPMI.
[54] D. Baulcombe,et al. The Rx Gene from Potato Controls Separate Virus Resistance and Cell Death Responses , 1999, Plant Cell.
[55] A. Roberts,et al. Assembly and movement of a plant virus carrying a green fluorescent protein overcoat. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[56] Austin Hughes,et al. A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks , 1995, Nature.
[57] D. Baulcombe,et al. A feature of the coat protein of potato virus X affects both induced virus resistance in potato and viral fitness. , 1993, Virology.
[58] S. Muyldermans,et al. Naturally occurring antibodies devoid of light chains , 1993, Nature.
[59] R. Terauchi,et al. Lessons in Effector and NLR Biology of Plant-Microbe Systems. , 2018, Molecular plant-microbe interactions : MPMI.
[60] Corella S. Casas-Delucchi,et al. Modulation of protein properties in living cells using nanobodies , 2010, Nature Structural &Molecular Biology.
[61] S. Dinesh-Kumar,et al. Structure – function analysis of the tobacco mosaic virus resistance gene , 2000 .