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Journal Article

Inhibition of Bacterial Ice Nucleators Is Not an Intrinsic Property of Antifreeze Proteins

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Kunert,  Anna T.
Multiphase Chemistry, Max Planck Institute for Chemistry, Max Planck Society;

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Pöschl,  Ulrich
Multiphase Chemistry, Max Planck Institute for Chemistry, Max Planck Society;

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Fröhlich-Nowoisky,  Janine
Multiphase Chemistry, Max Planck Institute for Chemistry, Max Planck Society;

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Citation

Schwidetzky, R., Kunert, A. T., Bonn, M., Pöschl, U., Ramlov, H., DeVries, A. L., et al. (2020). Inhibition of Bacterial Ice Nucleators Is Not an Intrinsic Property of Antifreeze Proteins. The Journal of Physical Chemistry B, 124(24), 4889-4895. doi:10.1021/acs.jpcb.0c03001.


Cite as: https://hdl.handle.net/21.11116/0000-0007-4ED4-3
Abstract
Cold-adapted organisms use antifreeze proteins (AFPs) or ice-nucleating proteins (INPs) for the survival in freezing habitats. AFPs have been reported to be able to inhibit the activity of INPs, a property that would be of great physiological relevance. The generality of this effect is not understood, and for the few known examples of INP inhibition by AFPs, the molecular mechanisms remain unclear. Here, we report a comprehensive evaluation of the effects of five different AFPs on the activity of bacterial ice nucleators using a high-throughput ice nucleation assay. We find that bacterial INPs are inhibited by certain AFPs, while others show no effect. Thus, the ability to inhibit the activity of INPs is not an intrinsic property of AFPs, and the interactions of INPs and different AFPs proceed through protein-specific rather than universal molecular mechanisms.