Universität zu Köln

Jijie Chai

Institute for Biochemistry, University of Cologne
Contact: jchai(at)uni-koeln.de
For more information visit: Chai lab

Jane Parker

Max Planck Institute for Plant Breeding Research
Contact: parker(at)mpipz.mpg.de
For more information visit: Parker lab

Paul Schulze-Lefert

Max Planck Institute for Plant Breeding Research
Contact: schlef(at)mpipz.mpg.de
For more information visit: Schulze-Lefert lab

Abstract

Nucleotide-binding domain/leucine-rich repeat (NLR) receptors provide a crucial barrier to pathogen infection in mammals and plants. In both systems, NLRs sense microbe-mediated perturbations inside host cells and, via conformational switches, induce cell death and anti-microbial pathways leading to disease resistance. This project integrates protein structure-function studies with in vivo molecular and pathology phenotyping, genetics and cell biology to answer fundamental questions about how plant sensor NLRs activate cell death pathways and whether different NLR types converge on the same or distinct cell death machineries in immunity.

Johanndrees, O., Baggs, E.L., Uhlmann, C., Locci, F., Läßle, H.L., Melkonian, K., Käufer, K., Dongus, J.A., Nakagami, H., Krasileva, K.V., Parker, J.E, Lapin, D. (2023) Variation in plant Toll/Interleukin-1 receptor domain protein dependence on ENHANCED DISEASE SUSCEPTIBILITY 1  Plant Physiology, Volume 191, Issue 1, January 2023, Pages 626–642, https://doi.org/10.1093/plphys/kiac480

Wang,J., Song, W., Chai, J. (2022) Structure, biochemical function and signaling mechanism of plant NLRs. Molecular Plant https://doi.org/10.1016/j.molp.2022.11.011 (review)

Sun, Y., Wang, Y., Zhang, X., Chen, Z., Xia, Y., Wang, L., Sun, Y., Zhang, M., Xiao, Y., Han, Z., Wang, Y., & Chai, J. Plant receptor-like protein activation by a microbial glycoside hydrolase. Nature (2022). https://doi.org/10.1038/s41586-022-05214-x

Förderer, A., Li, E., Lawson, A.W., Deng, Y., Sun, Y., Logemann, E., Zhang, X., Wen, J., Han, Z., Chang, J., Chen, Y., Schulze-Lefert, P., & Chai, J. A wheat resistosome defines common principles of immune receptor channels. Nature (2022) https://doi.org/10.1038/s41586-022-05231-w

Huang S., Jia, A., Song, W., Hessler, G., Meng, Y., Sun, Y., Xu, L., Laessle, H., Jirschitzka, J., Ma, S., Xiao, Y., Yu, D., Hou, J., Liu, R., Sun, H., Liu, X., Han, Z., Chang, J., Parker, J.E., Chai, J. (2022) Identification and receptor mechanism of TIR-catalyzed small molecules in plant immunity. Science DOI: 10.1126/science.abq3297

Jia, A., Huang, S,. Song, W., Wang, J., Meng, Y,. Sun, Y., Xu, L., Laessle, H., Jirschitzka, J., Hou, J., Zhang, T., Yu, W., Hessler, G., Li, E., Ma, S., Yu, D., Gebauer, J., Baumann, U., Liu, X., Han, Z., Chang, J., Parker, J.E., Chai, J. (2022) TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity. Science 10.1126/science.abq8180

Lapin, D., Johanndrees, O., Wu, Z., Parker, J.E. (2022) Molecular innovations in plant TIR-based immunity signaling. The Plant Cell 2022: 00: 1-18 https://doi.org/10.1093/plcell/koac035

Parker, J.E., Hessler, G., Cui, H. (2021) A new biochemistry connecting pathogen detection to induced defense in plants. New Phytologist https://doi.org/10.1111/nph.17924

Pruitt, R.N., Locci, F., Wanke, F., Zhang, L., Saile, S.C., Joe, A., Karelina, D., Hua, C., Fröhlich, K., Wan, W.-L., Hu, M., Rao, S., Stolze, S.C., Harzen, A., Gust, A.A., Harter, K., Joosten, M.H.A.J., Thomma, B.P.H.J., Zhou, J.-M., Dangl, J.L., Weigel, D., Nakagami, H., Oecking, C., El Kasmi, F., Parker, J.E., & Nürnberger, T. (2021) EDS1–PAD4–ADR1 node mediates Arabidopsis pattern-triggered immunity. Nature. https://doi.org/10.1038/s41586-021-03829-0

Bauer, S., Yu, D., Lawson, A.W., Saur, I.M.L., Frantzeskakis, L., Kracher, B., Logemann, E., Chai, J., Maekawa, T., Schulze-Lefert, P. (2021) The leucine-rich repeats in allelic barley MLA immune receptors define specificity towards sequence-unrelated powdery mildew avirulence effectors with a predicted common RNase-like fold. PLoS Pathog 17(2): e1009223. doi:10.1371/journal.ppat.1009223

Mahdi, L.K., Huang, M., Zhang, X., Nakano, R.T., Kopp, L.B., Saur, I.M.L., Jacob, F., Kovacova, V., Lapin, D., Parker, J.E., Murphy, J.M., Hofmann, K., Schulze-Lefert, P., Chai, J., Maekawa, T. (2020) Discovery of a Family of Mixed Lineage Kinase Domain-like Proteins in Plants and Their Role in Innate Immune Signaling. Cell Host & Microbe https://doi.org/10.1016/j.chom.2020.08.012

Sun, X., Lapin, D., Feehan, J.M., Stolze, S.C., Kramer, K., Dongus, J.A., Rzemieniewski, J., Blanvillain-Baufumé, S., Harzen, A., Bautor, J., Derbyshire, P., Menke, F.L.H., Finkemeier, I., Nakagami, H., Jones, J.D.G., & Parker, J.E.(2021) Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity. Nature Communications 12, Article number: 3335 https://doi.org/10.1038/s41467-021-23614-x

Xing, Y., Xu, N., Bhandari, D.,D., Lapin, D., Sun, X., Luo, X., Wang, Y., Cao, J., Wang, H., Coaker, G., Parker, J.,E., Liu, J. Bacterial effector targeting of a plant iron sensor facilitates iron acquisition and pathogen colonization. The Plant Cell Koab075 https://doi.org/10.1093/plcell/koab075

Zhao, C., Tang, Y., Wang. J., Zeng, Y., Sun, H., Zheng, Z., Su, R., Schneeberger, K., Parker, J.E., Cui, H. (2021) A mis‐regulated cyclic nucleotide‐gated channel mediates cytosolic calcium elevation and activates immunity in Arabidopsis. New Phytologist doi:10.1111/nph.17218

Bauer, S., Yu, D., Lawson, A.W., Saur, I.M.L., Frantzeskakis, L., Kracher, B., Logemann, E., Chai, J., Maekawa, T., Schulze-Lefert, P. (2021) The leucine-rich repeats in allelic barley MLA immune receptors define specificity towards sequence-unrelated powdery mildew avirulence effectors with a predicted common RNase-like fold. PLoS Pathog 17(2): e1009223. doi:10.1371/journal.ppat.1009223

Ma, S., Lapin, D., Liu, L., Sun, Y., Song, W., Zhang, X., Logemann, E., Yu, D., Wang, J., Jirschitzka, J., Han, Z., Schulze-Lefert, P., Parker, J.E., Chai, J. (2020) Direct pathogen-induced assembly of an NLR immune receptor complex to form a holoenzyme. Science Vol. 370, Issue 6521, eabe3069; https://doi.org/10.1126/science.abe3069