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A fungal substrate mimicking molecule suppresses plant immunity via an inter-kingdom conserved motif

Johana C Misas Villamil1, André N Mueller2, Fatih Demir3

  • 1Botanical Institute and Cluster of Excellence on Plant Sciences, University of Cologne, Cologne, D-50674, Germany.

Nature Communications
|April 7, 2019
PubMed

Insights

The corn smut fungus Ustilago maydis uses a protein called Pit2 to inhibit essential plant proteases. This research reveals a smaller, potent inhibitory motif within Pit2, crucial for fungal virulence.

Area of Science:

  • Plant Pathology
  • Molecular Biology
  • Biochemistry

Background:

  • Ustilago maydis causes corn smut disease in maize.
  • The fungal effector protein Pit2 inhibits papain-like cysteine proteases (PLCPs), which are vital for virulence.
  • Pit2's inhibitory activity depends on a conserved 14-amino acid motif (PID14).

Purpose of the Study:

  • To investigate the mechanism of Pit2's inhibition of PLCPs.
  • To determine the functional significance of the PID14 motif.
  • To explore the broader implications of the PID14 motif in plant-microbe interactions.

Main Methods:

  • Synthesis and testing of PID14 peptides as PLCP inhibitors.
  • Mass spectrometry to identify Pit2 processing products.
  • Mutational analysis of conserved residues in Pit2.

Main Results:

  • Synthetic PID14 peptides demonstrated enhanced PLCP inhibitory activity compared to full-length Pit2.
  • Mass spectrometry revealed Pit2 is processed by maize PLCPs, releasing an inhibitory core.
  • Mutational analysis identified two essential conserved residues for Pit2 function.
  • The PID14 motif was found in other plant-associated microbes, suggesting a conserved mechanism.

Conclusions:

  • Pit2 acts as a substrate-mimicking molecule, releasing an embedded inhibitor upon processing by host PLCPs.
  • This mechanism allows the fungus to modulate host immunity by blocking essential proteases.
  • The conserved microbial inhibitor of proteases (cMIP) represents a widespread strategy in plant-associated microbes.

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