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<p>Deoxyguanosine triphosphatases (dGTPases) are nucleotide-depleting enzymes known to play a role in antiviral defense. While their enzymatic mechanism is established, the structural and functional diversity of dGTPases remains poorly understood. Here, we report a systematic analysis of dGTPase homologs across bacteria, archaea, and eukaryotes, revealing their widespread distribution and association with diverse immune-related domains. Through integrative bioinformatics and structural mining, we identify a class of bacterial dGTPases that assemble into stable octameric and higher-order oligomeric structures. Using cryo-electron microscopy, we resolve the octameric and 16-mer assemblies of a representative Vibrio dGTPase (Vdg) and further captured filamentous forms. Functional assays demonstrate that octamer formation is essential and sufficient for antiviral activity, while higher-order assemblies are dispensable. We also identify dAMP as an allosteric regulator, underscoring the functional versatility of dGTPases. Our findings provide insights into the modular architecture, oligomerization-driven activation, and immune function of bacterial dGTPases, and broaden our understanding of nucleotide depletion-based antiviral strategies.</p>

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Octameric dGTPase assemblies mediate broad anti-phage defense

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年7月25日

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  • Miao Shi,
  • Peipei Li,
  • Quanjin Li,
  • Chao Ning,
  • Sen Yin,
  • Yina Gao,
  • Yong Wang,
  • Jingyu Li,
  • Zhaolong Li,
  • Songqing Liu,
  • Dong Li,
  • Changwei Wei,
  • Ang Gao

摘要

Deoxyguanosine triphosphatases (dGTPases) are nucleotide-depleting enzymes known to play a role in antiviral defense. While their enzymatic mechanism is established, the structural and functional diversity of dGTPases remains poorly understood. Here, we report a systematic analysis of dGTPase homologs across bacteria, archaea, and eukaryotes, revealing their widespread distribution and association with diverse immune-related domains. Through integrative bioinformatics and structural mining, we identify a class of bacterial dGTPases that assemble into stable octameric and higher-order oligomeric structures. Using cryo-electron microscopy, we resolve the octameric and 16-mer assemblies of a representative Vibrio dGTPase (Vdg) and further captured filamentous forms. Functional assays demonstrate that octamer formation is essential and sufficient for antiviral activity, while higher-order assemblies are dispensable. We also identify dAMP as an allosteric regulator, underscoring the functional versatility of dGTPases. Our findings provide insights into the modular architecture, oligomerization-driven activation, and immune function of bacterial dGTPases, and broaden our understanding of nucleotide depletion-based antiviral strategies.