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@ARTICLE{MisasVillamil:862155,
      author       = {Misas Villamil, Johana C. and Mueller, André N. and Demir,
                      Fatih and Meyer, Ute and Ökmen, Bilal and Schulze Hüynck,
                      Jan and Breuer, Marlen and Dauben, Helen and Win, Joe and
                      Huesgen, Pitter F. and Doehlemann, Gunther},
      title        = {{A} fungal substrate mimicking molecule suppresses plant
                      immunity via an inter-kingdom conserved motif},
      journal      = {Nature Communications},
      volume       = {10},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2019-02509},
      pages        = {1576},
      year         = {2019},
      abstract     = {Ustilago maydis is a biotrophic fungus causing corn smut
                      disease in maize. The secreted effector protein Pit2 is an
                      inhibitor of papain-like cysteine proteases (PLCPs)
                      essential for virulence. Pit2 inhibitory function relies on
                      a conserved 14 amino acids motif (PID14). Here we show that
                      synthetic PID14 peptides act more efficiently as PLCP
                      inhibitors than the full-length Pit2 effector. Mass
                      spectrometry shows processing of Pit2 by maize PLCPs, which
                      releases an inhibitory core motif from the PID14 sequence.
                      Mutational analysis demonstrates that two conserved residues
                      are essential for Pit2 function. We propose that the Pit2
                      effector functions as a substrate mimicking molecule: Pit2
                      is a suitable substrate for apoplastic PLCPs and its
                      processing releases the embedded inhibitor peptide, which in
                      turn blocks PLCPs to modulate host immunity. Remarkably, the
                      PID14 core motif is present in several plant associated
                      fungi and bacteria, indicating the existence of a conserved
                      microbial inhibitor of proteases (cMIP).},
      cin          = {ZEA-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ZEA-3-20090406},
      pnm          = {582 - Plant Science (POF3-582) / ProPlantStress -
                      Proteolytic processing in plant stress signal transduction
                      and responses to abiotic stress and pathogen attack
                      (639905)},
      pid          = {G:(DE-HGF)POF3-582 / G:(EU-Grant)639905},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30952847},
      UT           = {WOS:000463472200021},
      doi          = {10.1038/s41467-019-09472-8},
      url          = {https://juser.fz-juelich.de/record/862155},
}