The structural basis of specific protease-inhibitor interactions at the plant-pathogen interface

Curr Opin Struct Biol. 2013 Dec;23(6):842-50. doi: 10.1016/ Epub 2013 Aug 9.


Antagonistic host-pathogen interactions offer intriguing insights into coevolutionary processes at the molecular level. Studies on secreted immune proteases from the model plant tomato and their interactions with different unrelated pathogen-derived inhibitors revealed that the inhibitors exhibit a remarkable selectivity towards different host proteases, and that the host proteases accumulate variant residues at the interaction surfaces that interfere with inhibitor binding. Here, we summarize and discuss the recent findings and use structural models to identify the molecular features underpinning protease selectivity. The observed basic principles translate to other examples of secreted immune hydrolases and their putative inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Genetic Variation
  • Host-Pathogen Interactions*
  • Molecular Sequence Data
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / genetics
  • Peptide Hydrolases / metabolism*
  • Plants / drug effects
  • Plants / enzymology*
  • Plants / immunology
  • Plants / microbiology*
  • Protease Inhibitors / metabolism*
  • Protease Inhibitors / pharmacology
  • Protein Binding


  • Protease Inhibitors
  • Peptide Hydrolases