Carbonic anhydrases contribute to mitochondrial function, conidial development, and pathogenicity of Magnaporthe oryzae

作者：Qingqing Cui, T. Wang, Yujia Li, Xiaojing Liang, Xiaotong Song, Xinyue Ji, Linyi Wang, Xinquan Wang, Zhentao Chu, Yuejia Dang, Shi-hong Zhang · 发表于：Applied and Environmental Microbiology · 年份：2026 · DOI：10.1128/aem.02488-25 · 被引用次数：2 · 研究领域：Fungal and yeast genetics research、Enzyme function and inhibition、Metal-Catalyzed Oxygenation Mechanisms

ABSTRACT Carbonic anhydrases (CAs) are metalloenzymes widely present in biological systems, capable of catalyzing the reversible hydration of carbon dioxide (CO₂) to form bicarbonate (HCO 3 ⁻) and protons (H + ). This biochemical reaction plays a crucial role in various physiological processes. Previous studies have shown that MoCA1, a carbonic anhydrase in Magnaporthe oryzae , is localized in the mitochondria and is involved in conidial development and pathogenicity. However, the functions of other carbonic anhydrases in M. oryzae , such as MoCA2, MoCA4, and MoCA6, remain largely unexplored. Through subcellular localization analysis using DsRED-tagged fusion proteins, it was found that MoCAs are also localized in the mitochondria, and they exhibit interactions within this organelle. When the genes encoding MoCAs were deleted, the resulting mutants Δ MoCA2 , Δ MoCA4 , and Δ MoCA6 exhibited significant defects in conidial development and pathogenicity. Additionally, these mutants showed a marked decrease in mitochondrial membrane potential, indicating an apoptotic state, along with reduced intracellular ATP levels and downregulated expression of genes related to ATP synthesis. In nitrogen metabolism studies, the mutants displayed corresponding phenotypic changes, with significant downregulation of nitrogen metabolism-related gene expression. Taken together, the results of this study demonstrate that mitochondrial MoCAs play a critical role in conidiation and pathogenic mechani...