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Inhibition of Bacterial Ice Nucleators Is Not an Intrinsic Property of Antifreeze Proteins.
Schwidetzky, Ralph; Kunert, Anna T; Bonn, Mischa; Pöschl, Ulrich; Ramløv, Hans; DeVries, Arthur L; Fröhlich-Nowoisky, Janine; Meister, Konrad.
Affiliation
  • Schwidetzky R; Max Planck Institute for Polymer Research, 55128 Mainz, Germany.
  • Kunert AT; Max Planck Institute for Chemistry, 55128 Mainz, Germany.
  • Bonn M; Max Planck Institute for Polymer Research, 55128 Mainz, Germany.
  • Pöschl U; Max Planck Institute for Chemistry, 55128 Mainz, Germany.
  • Ramløv H; Roskilde University, 4000 Roskilde, Denmark.
  • DeVries AL; University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
  • Fröhlich-Nowoisky J; Max Planck Institute for Chemistry, 55128 Mainz, Germany.
  • Meister K; Max Planck Institute for Polymer Research, 55128 Mainz, Germany.
J Phys Chem B ; 124(24): 4889-4895, 2020 06 18.
Article in En | MEDLINE | ID: mdl-32437152
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Antifreeze Proteins / Ice Language: En Journal: J Phys Chem B Journal subject: QUIMICA Year: 2020 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Antifreeze Proteins / Ice Language: En Journal: J Phys Chem B Journal subject: QUIMICA Year: 2020 Document type: Article Affiliation country: