Other Protective Measures of Antifreeze Proteins

The primary function of antifreeze proteins is without doubt the inhibition of ice crystal growth in the body fluids and the inhibition of ice recrystallization in various organisms. Modification of the structure of the frozen environment by ice algae has also been reported but also this is a mechan...

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Main Authors: Ramløv, Hans, Friis, Dennis Steven
Format: Book Part
Language:English
Published: Springer 2020
Subjects:
Online Access:https://forskning.ruc.dk/da/publications/b748f4e3-0bc5-4b0a-8b6f-9fca78f609d1
https://doi.org/10.1007/978-3-030-41948-6_8
https://hdl.handle.net/1800/b748f4e3-0bc5-4b0a-8b6f-9fca78f609d1
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spelling fturoskildefispu:oai:pure.atira.dk:publications/b748f4e3-0bc5-4b0a-8b6f-9fca78f609d1 2023-12-03T10:23:59+01:00 Other Protective Measures of Antifreeze Proteins Ramløv, Hans Friis, Dennis Steven Ramløv, Hans Friis, Dennis Steven 2020 https://forskning.ruc.dk/da/publications/b748f4e3-0bc5-4b0a-8b6f-9fca78f609d1 https://doi.org/10.1007/978-3-030-41948-6_8 https://hdl.handle.net/1800/b748f4e3-0bc5-4b0a-8b6f-9fca78f609d1 eng eng Springer info:eu-repo/semantics/closedAccess Ramløv , H & Friis , D S 2020 , Other Protective Measures of Antifreeze Proteins . in H Ramløv & D S Friis (eds) , Antifreeze Proteins : Biochemistry, Molecular Biology and Applications . vol. 2 , Springer , Switzerland , pp. 185-203 . https://doi.org/10.1007/978-3-030-41948-6_8 Antifreeze protein Bacteria Biofilm Membrane bookPart 2020 fturoskildefispu https://doi.org/10.1007/978-3-030-41948-6_8 2023-11-08T23:55:51Z The primary function of antifreeze proteins is without doubt the inhibition of ice crystal growth in the body fluids and the inhibition of ice recrystallization in various organisms. Modification of the structure of the frozen environment by ice algae has also been reported but also this is a mechanism related to ice. However, other properties, not related to ice but still related to cold, of antifreeze proteins have been observed. These properties include interaction with cell membranes and anti-virulence properties in both animals and plants. In this chapter we present evidence that AFPs interact with both biological and model membrane systems and that these interactions rely both on the type of antifreeze protein as well as the saturation/unsaturation of the membrane lipids in question. Anti-virulence of an antifreeze glycoprotein has been shown in the context of a single species of insect and for a large number of plants. In the first case it is an AFGP and a derivative of this, from the tick Ixodes scapularis (IAFGP), which is shown to influence the formation of bacterial biofilm conferring increased resistance to various pathogens in both transgenic invertebrates and transgenic vertebrates. In the second case, plant antifreeze proteins are similar to pathogenesis-related proteins in plants and confer antifungal properties to the plants whereby increased survival of plants subjected to psychrophilic pathogens is achieved. The adaptational and evolutionary aspects of the above properties are also discussed in this chapter. Book Part ice algae Roskilde University Research Portal (RUC) 185 203 Cham
institution Open Polar
collection Roskilde University Research Portal (RUC)
op_collection_id fturoskildefispu
language English
topic Antifreeze protein
Bacteria
Biofilm
Membrane
spellingShingle Antifreeze protein
Bacteria
Biofilm
Membrane
Ramløv, Hans
Friis, Dennis Steven
Other Protective Measures of Antifreeze Proteins
topic_facet Antifreeze protein
Bacteria
Biofilm
Membrane
description The primary function of antifreeze proteins is without doubt the inhibition of ice crystal growth in the body fluids and the inhibition of ice recrystallization in various organisms. Modification of the structure of the frozen environment by ice algae has also been reported but also this is a mechanism related to ice. However, other properties, not related to ice but still related to cold, of antifreeze proteins have been observed. These properties include interaction with cell membranes and anti-virulence properties in both animals and plants. In this chapter we present evidence that AFPs interact with both biological and model membrane systems and that these interactions rely both on the type of antifreeze protein as well as the saturation/unsaturation of the membrane lipids in question. Anti-virulence of an antifreeze glycoprotein has been shown in the context of a single species of insect and for a large number of plants. In the first case it is an AFGP and a derivative of this, from the tick Ixodes scapularis (IAFGP), which is shown to influence the formation of bacterial biofilm conferring increased resistance to various pathogens in both transgenic invertebrates and transgenic vertebrates. In the second case, plant antifreeze proteins are similar to pathogenesis-related proteins in plants and confer antifungal properties to the plants whereby increased survival of plants subjected to psychrophilic pathogens is achieved. The adaptational and evolutionary aspects of the above properties are also discussed in this chapter.
author2 Ramløv, Hans
Friis, Dennis Steven
format Book Part
author Ramløv, Hans
Friis, Dennis Steven
author_facet Ramløv, Hans
Friis, Dennis Steven
author_sort Ramløv, Hans
title Other Protective Measures of Antifreeze Proteins
title_short Other Protective Measures of Antifreeze Proteins
title_full Other Protective Measures of Antifreeze Proteins
title_fullStr Other Protective Measures of Antifreeze Proteins
title_full_unstemmed Other Protective Measures of Antifreeze Proteins
title_sort other protective measures of antifreeze proteins
publisher Springer
publishDate 2020
url https://forskning.ruc.dk/da/publications/b748f4e3-0bc5-4b0a-8b6f-9fca78f609d1
https://doi.org/10.1007/978-3-030-41948-6_8
https://hdl.handle.net/1800/b748f4e3-0bc5-4b0a-8b6f-9fca78f609d1
genre ice algae
genre_facet ice algae
op_source Ramløv , H & Friis , D S 2020 , Other Protective Measures of Antifreeze Proteins . in H Ramløv & D S Friis (eds) , Antifreeze Proteins : Biochemistry, Molecular Biology and Applications . vol. 2 , Springer , Switzerland , pp. 185-203 . https://doi.org/10.1007/978-3-030-41948-6_8
op_rights info:eu-repo/semantics/closedAccess
op_doi https://doi.org/10.1007/978-3-030-41948-6_8
container_start_page 185
op_container_end_page 203
op_publisher_place Cham
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