The Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linné Weg 10, 50829 Cologne, Germany.
Curr Opin Struct Biol. 2013 Dec;23(6):842-50. doi: 10.1016/j.sbi.2013.07.013. 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.
拮抗的宿主-病原体相互作用为分子水平上的协同进化过程提供了有趣的见解。对模式植物番茄的分泌型免疫蛋白酶及其与不同非相关病原体衍生抑制剂的相互作用的研究表明，抑制剂对不同的宿主蛋白酶表现出显著的选择性，而宿主蛋白酶在相互作用表面积累变异残基，干扰抑制剂结合。在这里，我们总结和讨论了最近的发现，并使用结构模型来确定支持蛋白酶选择性的分子特征。所观察到的基本原则适用于其他分泌型免疫水解酶及其假定抑制剂的例子。
