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

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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)

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.

Suggested Citation

  • Jin-Lei Wang & Ting-Ting Li & Hany M. Elsheikha & Qin-Li Liang & Zhi-Wei Zhang & Meng Wang & L. David Sibley & Xing-Quan Zhu, 2022. "The protein phosphatase 2A holoenzyme is a key regulator of starch metabolism and bradyzoite differentiation in Toxoplasma gondii," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-35267-5
    DOI: 10.1038/s41467-022-35267-5
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    References listed on IDEAS

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    1. Uhn Soo Cho & Wenqing Xu, 2007. "Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme," Nature, Nature, vol. 445(7123), pages 53-57, January.
    2. Shaojun Long & Bryan Anthony & Lisa L. Drewry & L. David Sibley, 2017. "A conserved ankyrin repeat-containing protein regulates conoid stability, motility and cell invasion in Toxoplasma gondii," Nature Communications, Nature, vol. 8(1), pages 1-14, December.
    3. Céline Christiansen & Deborah Maus & Ellen Hoppenz & Mateo Murillo-León & Tobias Hoffmann & Jana Scholz & Florian Melerowicz & Tobias Steinfeldt & Frank Seeber & Martin Blume, 2022. "In vitro maturation of Toxoplasma gondii bradyzoites in human myotubes and their metabolomic characterization," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
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    1. Jin-Lei Wang & Ting-Ting Li & Nian-Zhang Zhang & Meng Wang & Li-Xiu Sun & Zhi-Wei Zhang & Bao-Quan Fu & Hany M. Elsheikha & Xing-Quan Zhu, 2024. "The transcription factor AP2XI-2 is a key negative regulator of Toxoplasma gondii merogony," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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