Abstract:
There is a continuous arms race between pathogens and their
host plants. However, successful pathogens, such as phytopathogenic
oomycetes, secrete effector proteins to manipulate
host defense responses for disease development. Structural
analyses of these effector proteins reveal the existence of regions
that fail to fold into three-dimensional structures, intrinsically
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 significance, 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 aswell as
characterize potential binding regions in effector proteins. Understanding
the role of IDRs in these effector proteins can aid in
the development of new disease-control strategies.
