Barghahn, S., Saridis, G., Mantz, M., Meyer, U., Mellüh, J.C., Misas Villamil, J.C., Huesgen, P.F. and Doehlemann, G. (2023) Combination of transcriptomic, proteomic and degradomic profiling reveals common and distinct patterns of pathogen-induced cell death in maize. Plant J. doi: 10.1111/tpj.16356.

Koenig, M., Moser, D., Leusner, J., Depotter, J., Doehlemann, G. and Misas Villamil, J.C. (2023) Maize phytocytokines modulate pro-survival host responses and pathogen resistance. Mol Plant Microbe Interact. doi: 10.1094/MPMI-01-23-0005-R.

Demir, F., Perrar, A., Mantz , M., Huesgen, P.F. (2022) Sensitive Plant N-Terminome Profiling with HUNTER. Methods Mol Biol 2022;2447:139-158. doi: 10.1007/978-1-0716-2079-3_12

Mooney, B. C., Mantz, M., Graciet, E, Huesgen, P. F. (2021) Cutting the line: manipulation of plant immunity by bacterial type III effector proteases.J Exp Botdoi:10.1093/jxb/erab095

Former participating project leader

Pitter Huesgen

CECAD, University of Cologne
Contact: p.huesgen(at)fz-juelich.de
For more information visit: Huesgen lab

Regulated cell death (RCD) plays a major role in determining the outcome of plant-microbe interactions. Initiation and execution of RCD often involves proteolytic activity, however little is known about the signals that activate cell death proteases, their substrates that are cleaved or degraded during RCD, the immune signals that are released by dying cells, the response by surrounding cells, and how proteases contribute to specificity and execution of different plant cell death pathways. This project aims to characterise protease-substrate relationships underlying RCD and their consequences for plant-pathogen interactions.

Misas VillamilJ, Mueller A, Demir F, Meyer U, Ökmen B, Schulze Hüynck J, Breuer M, Dauben H, Win J, Huesgen PF, and Doehlemann G. (2019). A fungal substrate mimicking molecule suppresses plant immunity via an inter-kingdom conserved motif.Nat Commun 10, 1576.

Perrar A, Dissmeyer N, and Huesgen PF (2019). New beginnings and new ends – Methods for large-scale characterization of protein termini and their use in plant biology. J Exp Bot 70, 2021-2038.

Ziemann S, van der Linde K, Lahrmann U, Acar B, Kaschani F, Colby T, Kaiser M, Ding Y, Schmelz EA, Huffaker A, Holton N, Zipfel C, and Doehlemann G. (2018). An apoplastic peptide activates salicylic acid signalling in maize. Nat Plants 4, 172-180.

Ökmen, B., Kemmerich, B., Hilbig, D., Wemhöner, R., Aschenbroich, J., Perrar, A., Huesgen, P.F., Schipper, K., and Doehlemann, G. (2018). Dual function of a secreted fungalysin metalloprotease in Ustilago maydis. New Phytol 220, 249-261.

Rinschen MM, Hoppe AK, Grahammer F, Kann M, Völker LA, Schurek EM, Binz J, Höhne M, Malisic M, Demir F, Malisic M, Huber TB, Kurschat C, Kizhakkedathu JN, Schermer B, Huesgen PF*, and Benzing T* (2017). N-Degradomic analysis reveals a proteolytic network processing the podocyte cytoskeleton. J Am Soc Nephrol, 28, 2867-2878.

Christensen SA, Huffaker A, Kaplan F, Sims J, Ziemann S, Doehlemann G, Ji L, Schmitz RJ, Kolomiets MV, Alborn HT, Mori N, Ni X, Byers S, Abdo Z, and Schmelz EA. (2015). Maize death acids, 9-lipoxygenase derived cyclopente(a)nones and derivatives, display activity as cytotoxic phytoalexins and transcriptional mediators. Proc Natl Acad Sci USA 112, 11407-11412.

Hof, A., Zechmann, B., Schwammbach, D., Hückelhoven, R., and Doehlemann, G. (2014). Alternative cell death mechanisms determine epidermal resistance in incompatible barley-Ustilago interactions. Mol Plant Microbe Interact 27, 403-414.

Mueller AN, Ziemann S, Treitschke S, Aßmann D, and Doehlemann G. (2013). Compatibility in the Ustilago maydis – maize interaction requires inhibition of host cysteine proteases by the fungal effector Pit2. PloS Pathogens 9, e1003177.

van der Linde K, Hemetsberger C, Kastner C, Kaschani F, van der Hoorn RAL, Kumlehn J, and Doehlemann G. (2012). A maize cystatin suppresses host immunity by inhibition of apoplastic cysteine proteases. Plant Cell 24, 1285-1300.

Weng SSH^#, Demir F^#, Ergin EK, Dirnberger S, Uzozie A, Tuscher D, Nierves L, Tsui J, Huesgen PF*, and Lange PF* (2019) Sensitive determination of proteolytic proteoforms in limited microscale proteome samples, bioRxiv, 566109. ^#equal contribution, *shared corresponding authorsPassarge A, Demir F, Green J, Depotter JRL, Scott B, Huesgen PF, Doehlemann G, Misas Villamil J. (2021) Host apoplastic cysteine protease activity is suppressed during the mutualistic association of Lolium perenne and Epichloë festucae. Journal of Experimental Botany. 13;72(9):3410-3426.

Schulze Hüynck, J., Kaschani, F., van der Linde, K., Ziemann, S., Müller, A. N., Colby, T., Kaiser, M., Misas Villamil, J. C., Doehlemann, G. (2019). Proteases underground: Analysis of the maize root apoplast identifies organ-specific papain-like cysteine protease activity. Frontiers in Plant Science, 10 :473

Misas Villamil JC., van der Hoorn RAL, Doehlemann G. (2016) Papain-like cysteine proteases as hubs in plant immunity. New Phytologist, 212(4), 902–907.

Misas-Villamil JC, Kolodziejek I, Crabill E, Kaschani F, Niessen S, Shindo T, Kaiser M, Alfano JR, van der Hoorn RA. (2013) Pseudomonas syringae pv. syringae uses proteasome inhibitor syringolin A to colonize from wound infection sites. PLoS Pathog. 9(3).

Shindo T., Misas Villamil, JC, Hörger, AC, SongJ, van der Hoorn RAL (2012) A role in immunity for Arabidopsis cysteine protease RD21, the ortholog of the tomato immune protease C14. PLoS ONE, 7(1).

van der Linde K, Kastner C, Kumlehn J, Kahmann R, Doehlemann G. (2011) Systemic virus-induced gene silencing allows functional characterization of maize genes during biotrophic interaction with Ustilago maydis. New Phytologist 189(2):471-83.