The protein phosphatase 2A holoenzyme is a key regulator of starch metabolism and bradyzoite differentiation in Toxoplasma gondii

Jin-Lei Wang (), Ting-Ting Li, Hany M. Elsheikha, Qin-Li Liang, Zhi-Wei Zhang, Meng Wang, L. David Sibley and Xing-Quan Zhu ()
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Jin-Lei Wang: Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Ting-Ting Li: Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Hany M. Elsheikha: University of Nottingham, Sutton Bonington Campus
Qin-Li Liang: Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Zhi-Wei Zhang: Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Meng Wang: Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences
L. David Sibley: Washington University School of Medicine in St. Louis
Xing-Quan Zhu: Shanxi Agricultural University

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: Abstract Phenotypic switching between tachyzoite and bradyzoite is the fundamental mechanism underpinning the pathogenicity and adaptability of the protozoan parasite Toxoplasma gondii. Although accumulation of cytoplasmic starch granules is a hallmark of the quiescent bradyzoite stage, the regulatory factors and mechanisms contributing to amylopectin storage in bradyzoites are incompletely known. Here, we show that T. gondii protein phosphatase 2A (PP2A) holoenzyme is composed of a catalytic subunit PP2A-C, a scaffold subunit PP2A-A and a regulatory subunit PP2A-B. Disruption of any of these subunits increased starch accumulation and blocked the tachyzoite-to-bradyzoite differentiation. PP2A contributes to the regulation of amylopectin metabolism via dephosphorylation of calcium-dependent protein kinase 2 at S679. Phosphoproteomics identified several putative PP2A holoenzyme substrates that are involved in bradyzoite differentiation. Our findings provide novel insight into the role of PP2A as a key regulator of starch metabolism and bradyzoite differentiation in T. gondii.

Date: 2022
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DOI: 10.1038/s41467-022-35267-5

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