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The Serine/Threonine Protein Phosphatase 6 Is Required for Efficient Gametogenesis in Sexual-Stage Plasmodium berghei

ABSTRACT: The Serine/Threonine Protein Phosphatase 6 Is Required for Efficient Gametogenesis in Sexual-Stage Plasmodium berghei

PROVIDER: PRJNA1129863 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29653378_1.fastq.gz	Fastqsanger.gz
	SRR29653378_2.fastq.gz	Fastqsanger.gz
	SRR29653379_1.fastq.gz	Fastqsanger.gz
	SRR29653379_2.fastq.gz	Fastqsanger.gz
	SRR29653380_1.fastq.gz	Fastqsanger.gz

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The Serine/Threonine Protein Phosphatase 6 Is Required for Efficient Gametogenesis in Sexual-Stage Plasmodium berghei

Project description:Protein phosphorylation plays a critical role during the development of malaria parasites. Here, we performed a functional analysis of the Plasmodium berghei Ser/Thr protein phosphatase 6 (PbPP6), which is associated with the plasma membrane of macrogametes and ookinetes. Compared to wild-type P. berghei, the genetic disruption of pbpp6 (∆pbpp6) resulted in reduced asexual growth of the parasites and prolonged survival of infected mice. The ∆pbpp6 parasites showed impaired gametogenesis, particularly affecting male gametogenesis, which substantially decreased both ookinete formation and mosquito transmission. Transcriptomic analysis revealed an over 11-fold downregulation of nek3, a regulator of MAPK2 within the PKG-Ca²⁺ signaling cascade, foreshadowing pathway dysregulation that was further evidenced by significantly diminished intracellular cGMP levels, decreased cytosolic Ca²⁺ mobilization, and reduced DNA replication in activated Δpbpp6 gametocytes. Phosphoproteomic analysis detected increased phosphorylation at the Ser508 site of guanylyl cyclase alpha (GCα), indicating that PbPP6 regulates cGMP-PKG-Ca2+ signaling through modulation of GCα activity during gametogenesis. Additionally, we observed altered expression of messenger ribonucleoproteins in the Δpbpp6 parasites, which may affect the translational repression of stored mRNAs in female gametocytes and impact post-fertilization development in mosquitoes. Collectively, this study highlights the potential of targeting PP6 to disrupt malaria transmission.

2025-06-02 | GSE271105 | GEO

Serine/Threonine phosphatase PP2A is essential for optimal B cell function

Project description:Serine/Threonine phosphatase PP2A is essential for optimal B cell function

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Loss of Serine/Threonine Protein Phosphatase 6 Severely Impairs Sexual Stage Development in Malaria Parasite Plasmodium berghei

Project description:Protein phosphorylation plays a critical role during the development of malaria parasites. Here, we performed a functional analysis of the Plasmodium berghei Ser/Thr protein phosphatase 6 (PbPP6), which was associated with the plasma membrane of macrogametes and ookinetes. Compared to wild-type P. berghei, genetic disruption/deletion of the pbpp6 gene (∆pbpp6) reduced the asexual growth of the parasites and prolonged the survival of ∆pbpp6-infected mice. The ∆pbpp6 parasites showed impaired gametogenesis, particularly affecting male gametogenesis, which substantially decreased ookinete formation and transmission to mosquitoes. RNA-seq assays revealed that pbpp6 disruption led to over 11-fold down-regulation of the nek3 gene, a regulator of MAPK2 in the PKG-Ca2+ signaling cascade during male gametogenesis. Several PDEs (α, γ, δ) were also affected, indicating that PbPP6 plays a role in the cGMP-PKG-Ca2+ signaling pathway. Additionally, we observed altered expression of messenger ribonucleoproteins in the Δpbpp6 parasites, which may affect translational repression of stored mRNAs in female gametocytes and post-fertilization development in mosquitoes. Consistent with the dysregulated GO terms related to the cGMP-PKG-Ca2+ signaling cascade observed in RNA-seq analysis, the activated gametocytes of ∆pbpp6 exhibited significantly reduced levels of intracellular cGMP, cytosolic Ca2+ mobilization, and DNA replication. Phosphoproteomic analysis detected increased phosphorylation at the Ser508 site of guanylyl cyclase alpha (GCα), suggesting that PbPP6 regulates cGMP-PKG-Ca2+ signaling cascades by modulating the activity of GCα during gametogenesis. This study highlights the potential of targeting PP6 to disrupt malaria transmission.

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Loss of Serine/Threonine Protein Phosphatase 6 Severely Impairs Sexual Stage Development in Malaria Parasite Plasmodium berghei

Project description:Protein phosphorylation plays a critical role during the development of malaria parasites. Here, we performed a functional analysis of the Plasmodium berghei Ser/Thr protein phosphatase 6 (PbPP6), which was associated with the plasma membrane of macrogametes and ookinetes. Compared to wild-type P. berghei, genetic disruption/deletion of the pbpp6 gene (∆pbpp6) reduced the asexual growth of the parasites and prolonged the survival of ∆pbpp6-infected mice. The ∆pbpp6 parasites showed impaired gametogenesis, particularly affecting male gametogenesis, which substantially decreased ookinete formation and transmission to mosquitoes. RNA-seq assays revealed that pbpp6 disruption led to over 11-fold down-regulation of the nek3 gene, a regulator of MAPK2 in the PKG-Ca2+ signaling cascade during male gametogenesis. Several PDEs (α, γ, δ) were also affected, indicating that PbPP6 plays a role in the cGMP-PKG-Ca2+ signaling pathway. Additionally, we observed altered expression of messenger ribonucleoproteins in the Δpbpp6 parasites, which may affect translational repression of stored mRNAs in female gametocytes and post-fertilization development in mosquitoes. Consistent with the dysregulated GO terms related to the cGMP-PKG-Ca2+ signaling cascade observed in RNA-seq analysis, the activated gametocytes of ∆pbpp6 exhibited significantly reduced levels of intracellular cGMP, cytosolic Ca2+ mobilization, and DNA replication. Phosphoproteomic analysis detected increased phosphorylation at the Ser508 site of guanylyl cyclase alpha (GCα), suggesting that PbPP6 regulates cGMP-PKG-Ca2+ signaling cascades by modulating the activity of GCα during gametogenesis. This study highlights the potential of targeting PP6 to disrupt malaria transmission.

2025-06-27 | PXD063164 | Pride

Loss of Serine/Threonine Protein Phosphatase 6 Severely Impairs Sexual Stage Development in Malaria Parasite Plasmodium berghei

Project description:Protein phosphorylation plays a critical role during the development of malaria parasites. Here, we performed a functional analysis of a Plasmodium berghei Ser/Thr protein phosphatase 6 (PbPP6), which was associated with the plasma membrane of macrogametes and ookinetes. Compared with the wild-type P. berghei, genetic disruption/deletion of the pbpp6 gene (∆pbpp6) reduced the asexual growth of the parasites and prolonged the survival of ∆pbpp6-infected mice. The ∆pbpp6 parasites displayed impaired gametogenesis, with a more significant effect on male gametogenesis, which substantially decreased ookinete formation and transmission to mosquitoes. RNA-seq assays revealed that pbpp6 deletion led to over 11-fold down-regulation of the nek3 gene, a regulator of MAPK2 downstream of protein kinase G (PKG)-dependent Ca2+ signaling cascade in male gametogenesis, suggesting that PbPP6 plays a role in the Ca2+ signaling pathway. Meanwhile, we observed altered expression of messenger ribonucleoproteins in the Δpbpp6 parasites, which may affect translational repression of stored mRNAs in female gametocytes and post-fertilization development in mosquitoes. A phospho-proteomic analysis detected increased phosphorylation at the Ser375 site of the phosphoinositide metabolism kinase PIP5K, a target of the PKG. In addition, the Thr699 site of PKG is also a putative target of PbPP6, suggesting that PbPP6 may be involved in a PKG-mediated transcending signaling network to control the sexual development of the malaria parasite. Our study highlighted the significance of protein phosphorylation in sexual development and Plasmodium phosphatases as potential targets for disrupting malaria transmission.

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Serine/Threonine phosphatase PP2A is essential for optimal B cell function

Project description:Protein phosphatase 2A (PP2A), a serine/threonine phosphatase, has been shown to control T cell function. We found that in vitro activated B cells and B cells from various lupus-prone mice and patients with systemic lupus erythematosus display increased PP2A activity. To understand the contribution of PP2A to B cell function, we generated a Cd19CrePpp2r1aflox/flox (flox/flox) mouse which lacks functional PP2A only in B cells. Flox/flox mice displayed reduced spontaneous germinal center formation and decreased responses to T-dependent and T-independent antigens while their B cells responded poorly in vitro to stimulation with an anti-CD40 antibody or CpG in the presence of IL-4. Transcriptome and metabolome studies revealed altered NAD and purine/pyrimidine metabolism and increased expression of purine nucleoside phosphorylase in PP2A-deficient B cells. Our results demonstrate that PP2A is required for optimal B cell function and may contribute to increased B cell activity in systemic autoimmunity.

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Dynamic molecular events associated to Plasmodium berghei gametogenesis through proteomic approach

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