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Updated: Oct 30, 2025

Unravelling the Function of a Bacterial Effector from a Non-cultivable Plant Pathogen Using a Yeast Two-hybrid Screen
Published on: January 20, 2017
Xanthomonas effector XopR hijacks host actin cytoskeleton via complex coacervation
He Sun1, Xinlu Zhu1, Chuanxi Li2
1School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Phytobacterial type III effectors (T3Es) use intrinsically disordered regions (IDRs) to hijack plant cell's actin cytoskeleton. The T3E XopR forms coacervates, manipulating actin assembly for bacterial infection.
Area of Science:
- Plant pathology
- Molecular biology
- Biochemistry
Background:
- Intrinsically disordered regions (IDRs) are key features of phytobacterial type III effectors (T3Es).
- IDRs are believed to facilitate effector translocation and immune evasion through sequence variation.
- The precise mechanisms by which T3Es manipulate host cells remain an active area of research.
Purpose of the Study:
- To elucidate the mechanism by which the Xanthomonas campestris T3E XopR subverts the host actin cytoskeleton.
- To investigate the role of the T3E IDR in host-pathogen interactions.
Main Methods:
- Studied liquid-liquid phase separation (LLPS) of XopR mediated by its IDR.
- Investigated the interaction of XopR with the Arabidopsis actin cytoskeleton and actin-binding proteins.
- Analyzed the manipulation of actin assembly dynamics, including nucleation, crosslinking, and depolymerization.
Main Results:
- XopR undergoes LLPS via multivalent IDR interactions, forming coacervates.
- XopR hijacks the Arabidopsis actin cytoskeleton by forming macromolecular complexes at the cell cortex.
- XopR progressively manipulates actin nucleation, F-actin crosslinking, and actin depolymerization through stoichiometric control of coacervates.
Conclusions:
- Bacterial T3Es employ sophisticated strategies, such as protein complex coacervation, to subvert host cellular processes.
- The IDR of XopR is crucial for hijacking the host actin cytoskeleton, enabling bacterial virulence.
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