Aceylated Cyclophilin D Regulates Mitochondrial Function in the Developing Mouse Heart

Beutner, Gisela; Burris, Jonathan; Porter, George A.

doi:10.1016/j.bpj.2020.11.2175

Cited by 1 publication

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“…Western blot analysis confirmed that CypD expression and acetylation were upregulated in these apoptotic cells (* p < 0.05; ** p < 0.01; Figure 2 C–E). As an integrator of mitochondrial function, CypD acetylation may cause the irreversible opening of mPTP and culminate in the loss of mitochondrial ∆Ψm [ 16 , 39 ]. We used a JC-1 fluorescent probe to examine the mitochondrial ∆Ψm and found that the MbBV-infection significantly decreased ∆Ψm in MbBV-infected Spli221cells compared with the uninfected cells ( Figure 2 F,G, * p < 0.05).…”

Section: Resultsmentioning

confidence: 99%

“…Sustained opening of the mPTP results in loss of membrane potential, uncoupling of oxidative phosphorylation, ATP depletion, and increased production of reactive oxygen species. These effects will ultimately lead to cell death [ 16 , 39 , 41 ]. We also used a JC-1 fluorescent probe to examine ∆Ψm of mitochondria and found that MbBV infection significantly decreased ∆Ψm of infected insect cells compared with the uninfected cells ( Figure 2 F,G).…”

Section: Discussionmentioning

confidence: 99%

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Microplitis bicoloratus Bracovirus Promotes Cyclophilin D-Acetylation at Lysine 125 That Correlates with Apoptosis during Insect Immunosuppression

Zhang

et al. 2023

Viruses

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Cyclophilin D (CypD) is regulated during the innate immune response of insects. However, the mechanism by which CypD is activated under innate immunosuppression is not understood. Microplitis bicoloratus bracovirus (MbBV), a symbiotic virus in the parasitoid wasp, Microplitis bicoloratus, suppresses innate immunity in parasitized Spodoptera litura. Here, we demonstrate that MbBV promotes the CypD acetylation of S. litura, resulting in an immunosuppressive phenotype characterized by increased apoptosis of hemocytes and MbBV-infected cells. Under MbBV infection, the inhibition of CypD acetylation significantly rescued the apoptotic cells induced by MbBV, and the point-mutant fusion proteins of CypDK125R-V5 were deacetylated. The CypD-V5 fusion proteins were acetylated in MbBV-infected cells. Deacetylation of CypDK125R-V5 can also suppress the MbBV-induced increase in apoptosis. These results indicate that CypD is involved in the MbBV-suppressed innate immune response via the CypD-acetylation pathway and S. litura CypD is acetylated on K125.

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Section: Resultsmentioning

confidence: 99%