De Meyer Frédéric, Carlier Aurélien
Laboratory of Microbiology, Department of Biochemistry and Microbiology, Ghent University, Ghent, Belgium.
LIPME, Université de Toulouse, INRAE, CNRS, Castanet-Tolosan, France.
Front Microbiol. 2023 Jan 24;14:1114690. doi: 10.3389/fmicb.2023.1114690. eCollection 2023.
Serine protease inhibitors are a large family of proteins involved in important pathways and processes, such as inflammatory responses and blood clotting. Most are characterized by a precise mode of action, thereby targeting a narrow range of protease substrates. However, the serine-protease inhibitor ecotin is able to inhibit a broad range of serine proteases that display a wide range of specificities. This specificity is driven by special structural features which allow unique flexibility upon binding to targets. Although frequently observed in many human/animal-associated bacteria, ecotin homologs may also be found in plant-associated taxa and environmental species. The purpose of this review is to provide an update on the biological importance, role in host-microbe interactions, and evolutionary relationship between ecotin orthologs isolated from Eukaryotic and Prokaryotic species across the Tree of Life.
丝氨酸蛋白酶抑制剂是一大类参与重要途径和过程的蛋白质,如炎症反应和血液凝固。大多数丝氨酸蛋白酶抑制剂的特点是作用方式精确,因此靶向的蛋白酶底物范围较窄。然而,丝氨酸蛋白酶抑制剂依柯丁能够抑制多种具有广泛特异性的丝氨酸蛋白酶。这种特异性是由特殊的结构特征驱动的,这些特征使得依柯丁在与靶标结合时具有独特的灵活性。尽管依柯丁同源物在许多与人类/动物相关的细菌中经常被观察到,但在与植物相关的分类群和环境物种中也可能发现。本综述的目的是提供关于依柯丁直系同源物的生物学重要性、在宿主-微生物相互作用中的作用以及从生命之树中的真核生物和原核生物物种中分离出的依柯丁直系同源物之间进化关系的最新信息。