Xanthomonas effector XopR hijacks host actin cytoskeleton via complex coacervation

He Sun, Xinlu Zhu, Chuanxi Li, Zhiming Ma, Xiao Han, Yuanyuan Luo, Liang Yang, Jing Yu and Yansong Miao ()
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He Sun: Nanyang Technological University
Xinlu Zhu: Nanyang Technological University
Chuanxi Li: Nanyang Technological University
Zhiming Ma: Nanyang Technological University
Xiao Han: Nanyang Technological University
Yuanyuan Luo: Nanyang Technological University
Liang Yang: Nanyang Technological University
Jing Yu: Nanyang Technological University
Yansong Miao: Nanyang Technological University

Nature Communications, 2021, vol. 12, issue 1, 1-17

Abstract: Abstract The intrinsically disordered region (IDR) is a preserved signature of phytobacterial type III effectors (T3Es). The T3E IDR is thought to mediate unfolding during translocation into the host cell and to avoid host defense by sequence diversification. Here, we demonstrate a mechanism of host subversion via the T3E IDR. We report that the Xanthomonas campestris T3E XopR undergoes liquid-liquid phase separation (LLPS) via multivalent IDR-mediated interactions that hijack the Arabidopsis actin cytoskeleton. XopR is gradually translocated into host cells during infection and forms a macromolecular complex with actin-binding proteins at the cell cortex. By tuning the physical-chemical properties of XopR-complex coacervates, XopR progressively manipulates multiple steps of actin assembly, including formin-mediated nucleation, crosslinking of F-actin, and actin depolymerization, which occurs through competition for actin-depolymerizing factor and depends on constituent stoichiometry. Our findings unravel a sophisticated strategy in which bacterial T3E subverts the host actin cytoskeleton via protein complex coacervation.

Date: 2021
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DOI: 10.1038/s41467-021-24375-3

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