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Abstract <p>Heat stress (HS) is a critical bottleneck restricting the commercial cultivation of <i>Pleurotus ostreatus</i>, severely compromising its yield and quality. Glutathione peroxidase (GPX) is a conserved antioxidant enzyme essential for stress adaptation, yet its regulatory mechanism in the fungal heat stress response (HSR) remains unclear. This study characterized a GPX homolog <i>PoGPX</i> in <i>P. ostreatus</i> and elucidated its functions in fungal growth, abiotic stress resistance, and HSR. <i>PoGPX</i> was downregulated during fruiting body development and upregulated under multiple abiotic stresses (especially HS). Silencing <i>PoGPX</i> promoted mycelial growth, biomass accumulation, and hyphal hyperbranching, accompanied by elevated intracellular reactive oxygen species (ROS) levels and compensatory changes in antioxidant enzyme activities. Notably, silencing <i>PoGPX</i> increased cytosolic trehalose content by 0.45–0.62-fold compared with the wild type (WT) strain, and this elevation was reversed by treatment with the ROS scavenger <i>N</i>-acetylcysteine, implying <i>PoGPX</i> modulates trehalose biosynthesis through ROS signaling. Functionally, silencing <i>PoGPX</i> alleviated HS-induced oxidative damage (reduced malondialdehyde content) and suppressed the upregulation of heat shock protein (HSP) genes expression (<i>HSP60</i>, <i>HSP90</i>, <i>HSP104</i>). Critically, inhibiting trehalose biosynthesis restored the HSR phenotypes in <i>PoGPX</i>-silenced strains, indicating trehalose as the key downstream mediator of <i>PoGPX</i>-regulated HSR. These findings uncover that <i>PoGPX</i> regulates HSR in <i>P. ostreatus</i> through trehalose biosynthesis induced by intracellular ROS levels. This study provides novel insights into fungal HSR mechanisms and identifies <i>PoGPX</i> as a promising target for genetic engineering to improve the thermotolerance of <i>P. ostreatus</i> in commercial cultivation.</p> Key points <p><i>• PoGPX acts as a key negative regulator on mycelial growth and hyphal branching in P. ostreatus.</i></p> <p><i>• The PoGPX silencing alleviates the heat stress response of P. ostreatus.</i></p> <p><i>• PoGPX regulates the heat stress response in P. ostreatus by modulating cytosolic trehalose biosynthesis.</i></p>

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Glutathione peroxidase gene regulates heat stress response via trehalose synthesis in Pleurotus ostreatus

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月24日

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  • Guang Zhang,
  • Jiajia Wang,
  • Li Shang,
  • Mengmeng Ding,
  • Zhongwei Wu,
  • Qian An,
  • Yanjie Wang,
  • Chaohui Zhang,
  • Bin Chen

摘要

Abstract

Heat stress (HS) is a critical bottleneck restricting the commercial cultivation of Pleurotus ostreatus, severely compromising its yield and quality. Glutathione peroxidase (GPX) is a conserved antioxidant enzyme essential for stress adaptation, yet its regulatory mechanism in the fungal heat stress response (HSR) remains unclear. This study characterized a GPX homolog PoGPX in P. ostreatus and elucidated its functions in fungal growth, abiotic stress resistance, and HSR. PoGPX was downregulated during fruiting body development and upregulated under multiple abiotic stresses (especially HS). Silencing PoGPX promoted mycelial growth, biomass accumulation, and hyphal hyperbranching, accompanied by elevated intracellular reactive oxygen species (ROS) levels and compensatory changes in antioxidant enzyme activities. Notably, silencing PoGPX increased cytosolic trehalose content by 0.45–0.62-fold compared with the wild type (WT) strain, and this elevation was reversed by treatment with the ROS scavenger N-acetylcysteine, implying PoGPX modulates trehalose biosynthesis through ROS signaling. Functionally, silencing PoGPX alleviated HS-induced oxidative damage (reduced malondialdehyde content) and suppressed the upregulation of heat shock protein (HSP) genes expression (HSP60, HSP90, HSP104). Critically, inhibiting trehalose biosynthesis restored the HSR phenotypes in PoGPX-silenced strains, indicating trehalose as the key downstream mediator of PoGPX-regulated HSR. These findings uncover that PoGPX regulates HSR in P. ostreatus through trehalose biosynthesis induced by intracellular ROS levels. This study provides novel insights into fungal HSR mechanisms and identifies PoGPX as a promising target for genetic engineering to improve the thermotolerance of P. ostreatus in commercial cultivation.

Key points

• PoGPX acts as a key negative regulator on mycelial growth and hyphal branching in P. ostreatus.

• The PoGPX silencing alleviates the heat stress response of P. ostreatus.

• PoGPX regulates the heat stress response in P. ostreatus by modulating cytosolic trehalose biosynthesis.