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Curr Opin Plant Biol. 2008 Aug;11(4):380-8. doi: 10.1016/j.pbi.2008.04.007. Epub 2008 Jun 10.

Enzyme-inhibitor interactions at the plant-pathogen interface.

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Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, 50829 Cologne, Germany.


The plant apoplast during plant-pathogen interactions is an ancient battleground that holds an intriguing range of attacking enzymes and counteracting inhibitors. Examples are pathogen xylanases and polygalacturonases that are inhibited by plant proteins like TAXI, XIP, and PGIP; and plant glucanases and proteases, which are targeted by pathogen proteins such as GIP1, EPI1, EPIC2B, and AVR2. These seven well-characterized inhibitors have different modes of action and many probably evolved from inactive enzymes themselves. Detailed studies of the structures, sequence variation, and mutated proteins uncovered molecular struggles between these enzymes and their inhibitors, resulting in positive selection for variant residues at the contact surface, where single residues determine the outcome of the interaction.

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