Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins
Antifreeze proteins (AFPs) can inhibit the freezing of body fluid at subzero temperatures to promote the survival of various organisms living in polar regions. Type III AFPs are categorized into three subgroups, QAE1, QAE2, and SP isoforms, based on differences in their isoelectric points. We determ...
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doaj-a408cfc7bd8e42eab345f9e1c932eeb42021-02-01T04:12:40ZengElsevierComputational and Structural Biotechnology Journal2001-03702021-01-0119897909Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteinsSeo-Ree Choi0Jaewang Lee1Yeo-Jin Seo2Hyun Sun Kong3Minjae Kim4EonSeon Jin5Jung Ryeol Lee6Joon-Hwa Lee7Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of KoreaDepartment of Obstetrics and Gynecology, Seoul National University Bundang Hospital, Gyeonggi 13620, Republic of Korea; Department of Biomedical Laboratory Science, Eulji University, Gyeonggi 13135, Republic of KoreaDepartment of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of KoreaDepartment of Obstetrics and Gynecology, Seoul National University Bundang Hospital, Gyeonggi 13620, Republic of KoreaDepartment of Life Science, Hanyang University, Seoul 04763, Republic of KoreaDepartment of Life Science, Hanyang University, Seoul 04763, Republic of KoreaDepartment of Obstetrics and Gynecology, Seoul National University Bundang Hospital, Gyeonggi 13620, Republic of Korea; Department of Obstetrics and Gynecology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea; Corresponding authors at: Department of Obstetrics and Gynecology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea (J.R. Lee), Department of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Republic of Korea (J.-H. Lee).Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Gyeongnam 52828, Republic of Korea; Corresponding authors at: Department of Obstetrics and Gynecology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea (J.R. Lee), Department of Chemistry and RINS, Gyeongsang National University, Gyeongnam 52828, Republic of Korea (J.-H. Lee).Antifreeze proteins (AFPs) can inhibit the freezing of body fluid at subzero temperatures to promote the survival of various organisms living in polar regions. Type III AFPs are categorized into three subgroups, QAE1, QAE2, and SP isoforms, based on differences in their isoelectric points. We determined the thermal hysteresis (TH), ice recrystallization inhibition (IRI), and cryopreservation activity of three isoforms of the notched-fin eelpout AFP and their mutant constructs and characterized their structural and dynamic features using NMR. The QAE1 isoform is the most active among the three classes of III AFP isoforms, and the mutants of inactive QAE2 and SP isoforms, QAE2ACT and SPACT, displayed the full TH and IRI activities with resepect to QAE1 isoform. Cryopreservation studies using mouse ovarian tissue revealed that the QAE1 isoform and the active mutants, QAE2ACT and SPACT, more effectively preserved intact follicle morphology and prevented DNA double-strand break damage more efficiently than the inactive isoforms. It was also found that all active AFPs, QAE1, QAE2ACT, and SPACT, formed unique H-bonds with the first 310 helix, an interaction that plays an important role in the formation of anchored clathrate water networks for efficient binding to the primary prism and pyramidal planes of ice crystals, which was disrupted in the inactive isoforms. Our studies provide valuable insights into the molecular mechanism of the TH and IRI activity, as well as the cryopreservation efficiency, of type III AFPs.http://www.sciencedirect.com/science/article/pii/S2001037021000209Antifreeze proteinCryopreservationIce crystallization inhibitionNMRThermal hysteresis |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Seo-Ree Choi Jaewang Lee Yeo-Jin Seo Hyun Sun Kong Minjae Kim EonSeon Jin Jung Ryeol Lee Joon-Hwa Lee |
spellingShingle |
Seo-Ree Choi Jaewang Lee Yeo-Jin Seo Hyun Sun Kong Minjae Kim EonSeon Jin Jung Ryeol Lee Joon-Hwa Lee Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins Computational and Structural Biotechnology Journal Antifreeze protein Cryopreservation Ice crystallization inhibition NMR Thermal hysteresis |
author_facet |
Seo-Ree Choi Jaewang Lee Yeo-Jin Seo Hyun Sun Kong Minjae Kim EonSeon Jin Jung Ryeol Lee Joon-Hwa Lee |
author_sort |
Seo-Ree Choi |
title |
Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins |
title_short |
Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins |
title_full |
Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins |
title_fullStr |
Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins |
title_full_unstemmed |
Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins |
title_sort |
molecular basis of ice-binding and cryopreservation activities of type iii antifreeze proteins |
publisher |
Elsevier |
series |
Computational and Structural Biotechnology Journal |
issn |
2001-0370 |
publishDate |
2021-01-01 |
description |
Antifreeze proteins (AFPs) can inhibit the freezing of body fluid at subzero temperatures to promote the survival of various organisms living in polar regions. Type III AFPs are categorized into three subgroups, QAE1, QAE2, and SP isoforms, based on differences in their isoelectric points. We determined the thermal hysteresis (TH), ice recrystallization inhibition (IRI), and cryopreservation activity of three isoforms of the notched-fin eelpout AFP and their mutant constructs and characterized their structural and dynamic features using NMR. The QAE1 isoform is the most active among the three classes of III AFP isoforms, and the mutants of inactive QAE2 and SP isoforms, QAE2ACT and SPACT, displayed the full TH and IRI activities with resepect to QAE1 isoform. Cryopreservation studies using mouse ovarian tissue revealed that the QAE1 isoform and the active mutants, QAE2ACT and SPACT, more effectively preserved intact follicle morphology and prevented DNA double-strand break damage more efficiently than the inactive isoforms. It was also found that all active AFPs, QAE1, QAE2ACT, and SPACT, formed unique H-bonds with the first 310 helix, an interaction that plays an important role in the formation of anchored clathrate water networks for efficient binding to the primary prism and pyramidal planes of ice crystals, which was disrupted in the inactive isoforms. Our studies provide valuable insights into the molecular mechanism of the TH and IRI activity, as well as the cryopreservation efficiency, of type III AFPs. |
topic |
Antifreeze protein Cryopreservation Ice crystallization inhibition NMR Thermal hysteresis |
url |
http://www.sciencedirect.com/science/article/pii/S2001037021000209 |
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