Poster
Florian Kümmel
Max Planck Institute for Plant Breeding Research
Cologne
Yueqiang Leng
North Dakota State University, Department of Plant Pathology
Fargo, North Dakota, United States
Jan Jirschitzka
Institute of Biochemistry, University of Cologne, Cologne, Germany.
C, Nordrhein-Westfalen, Germany
Sara Stolze
Max Planck Institute for Plant Breeding Research, Proteomics Group
Koeln, Nordrhein-Westfalen, Germany
Laurens Wachsmuth
CECAD Research Center, Institute for Genetics, University of Cologne
Cologne, Nordrhein-Westfalen, Germany
Manolis Pasparakis
Professor
CECAD Research Center, Institute for Genetics, University of Cologne
Cologne, Nordrhein-Westfalen, Germany
Shaobin Zhong, n/a
Research Geneticist
United States Department of Agriculture
Fargo, North Dakota, United States
Paul Schulze-Lefert
Professor
Max Planck Institute for Plant Breeding Research
Köln, Nordrhein-Westfalen, Germany
Virulence mechanisms of host-selective necrotrophic pathogens are poorly understood. The necrotrophic fungus Bipolaris sorokiniana isolate ND90Pr requires barley Scs6 to cause spot blotch disease and associated host cell death. Scs6 is located at the Mla resistance locus and encodes an intracellular NOD-like receptor (NLR). Virulence of ND90Pr depends on an uncharacterized effector produced by at least two non-ribosomal peptide (NRP) synthetases (NRPSs) encoded at the VHv1 locus. Intercellular washing fluid (IWF) from ND90Pr-infected barley, but not from nrps virulence mutants, induces Scs6-dependent cell death in barley and heterologous N. benthamiana leaves. Expression of Scs6 in human HEK293 cells followed by application of IWF from wild-type ND90Pr is sufficient to reconstitute a host cell death response, suggesting direct activation of SCS6 by the NRP effector. Scs6-mediated cell death in HEK293 cells is Ca2+-dependent but independent of known vertebrate cell death pathways. In N. benthamiana, oligomerization of SCS6 is detectable within 30 minutes of IWF infiltration, suggesting rapid effector translocation inside plant cells and NLR activation. We identified the mass of the NRP effector using high-resolution mass spectrometry (MS) and analyzed its biochemical properties using peptidase digestion assays and MS/MS. Our findings indicate that a plant NLR can be directly targeted by an NRP effector of a necrotrophic fungus to induce cell death for disease susceptibility.