Order from disordered: Potential role of intrinsically disordered regions in phytopathogenic oomycete intracellular effector proteins

There is a continuous arms race between pathogens and their host plants. However, successful pathogens, such as phyto-pathogenic oomycetes, secrete effector proteins to manipulate host defense responses for disease development. Structural analyses of these effector proteins reveal the existence of re-gions that fail to fold into three-dimensional structures, intrin-sically disordered regions (IDRs). Because of their flexibility, these regions are involved in important biological functions of effector proteins, such as effector-host protein interactions that perturb host immune responses. Despite their signifi-cance, the role of IDRs in phytopathogenic oomycete effector-host protein interactions is not clear. This review, therefore, searched the literature for functionally characterized oomycete intracellular effectors with known host interactors. We further classify regions that mediate effector-host protein interactions into globular or disordered binding sites in these proteins. To fully appreciate the potential role of IDRs, five effector proteins encoding potential disordered binding sites were used as case studies. We also propose a pipeline that can be used to identify, classify as well as characterize po-tential binding regions in effector proteins. Understanding the role of IDRs in these effector proteins can aid in the develop-ment of new disease-control strategies.

Automated summary

This article investigates the role of intrinsically disordered regions (IDRs) in effector proteins secreted by phytopathogenic oomycetes. By analyzing functionally characterized effector proteins and their host interactors, the study classifies the regions involved in effector-host protein interactions as either globular or disordered binding sites. Five case studies are presented to demonstrate the potential role of IDRs, and a pipeline is proposed for identifying and characterizing potential binding regions in effector proteins. Understanding the function of IDRs in these effector proteins can contribute to the development of new disease-control strategies.