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<p>Biological ice nucleation plays a pivotal role in atmospheric processes, yet the molecular basis of fungal ice nucleation remains poorly understood. We report the biochemical characterization of an ice nucleation protein (<i>Pc</i>INP) from the soil-dwelling fungus <i>Podila clonocystis</i>, an organism that has been implicated in ice nuclei production; however, its ice nucleation activity has not been demonstrated. Using sequence similarity networks, we identified <i>Pc</i>INP as a putative fungal homolog of bacterial INPs and confirmed its function through recombinant expression in <i>Escherichia coli.</i> We probed the function of <i>Pc</i>INP structure through domain truncations and demonstrated that the N-terminal region is not necessary for ice nucleation activity and can be replaced with an expression-enhancing tag that significantly increases the number of active ice nuclei. Finally, we observed that a solution that contains monomeric <i>Pc</i>INP has identical activity to solutions containing oligomerized INP, suggesting <i>Pc</i>INP utilizes an in vitro aggregation mechanism to generate active oligomers. Our findings establish <i>Pc</i>INP as a member of the emerging class of fungal INPs, expanding the known diversity of biological ice nucleators and highlighting their potential for environmental and biotechnological applications.</p>

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Biochemical characterization of a fungal ice nucleation protein from Podila clonocystis

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年5月13日

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  • Brenna J. C. Walsh,
  • Sarah L. Brewer,
  • Andrea J. Shepard,
  • Noor Mahmoud,
  • Elizabeth A. Robinson,
  • Brooke M. Luisi,
  • Joel M. Sarapas,
  • William D. Stone

摘要

Biological ice nucleation plays a pivotal role in atmospheric processes, yet the molecular basis of fungal ice nucleation remains poorly understood. We report the biochemical characterization of an ice nucleation protein (PcINP) from the soil-dwelling fungus Podila clonocystis, an organism that has been implicated in ice nuclei production; however, its ice nucleation activity has not been demonstrated. Using sequence similarity networks, we identified PcINP as a putative fungal homolog of bacterial INPs and confirmed its function through recombinant expression in Escherichia coli. We probed the function of PcINP structure through domain truncations and demonstrated that the N-terminal region is not necessary for ice nucleation activity and can be replaced with an expression-enhancing tag that significantly increases the number of active ice nuclei. Finally, we observed that a solution that contains monomeric PcINP has identical activity to solutions containing oligomerized INP, suggesting PcINP utilizes an in vitro aggregation mechanism to generate active oligomers. Our findings establish PcINP as a member of the emerging class of fungal INPs, expanding the known diversity of biological ice nucleators and highlighting their potential for environmental and biotechnological applications.