Hyperactive antifreeze proteins from longhorn beetles: Some structural insights

Kristiansen, Erlend; Wilkens, Casper; Vincents, Bjarne; Friis, Dennis Steven; Lorentzen, Anders; Jenssen, Håvard; Løbner-Olesen, Anders; Ramløv, Hans

doi:10.1016/j.jinsphys.2012.09.004

Cited by 36 publications

(41 citation statements)

References 71 publications

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“…Notably, Rhagium mordax, a longhorn beetle from northern Europe and a close relative of R. inquisitor, produces several isoforms of a hyperactive AFP (RmAFP1-8), each with significant sequence identity (75-82%) to RiAFP (49). A molecular dynamics model of RmAFP1 reveals a ␤-solenoid prediction that is similar to the architecture RiAFP.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of an Insect Antifreeze Protein and Its Implications for Ice Binding

Hakim

Nguyen

Basu

et al. 2013

Journal of Biological Chemistry

103

121

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Background: Antifreeze proteins bind to ice crystals and inhibit their growth. Results: The crystal structure of a potent beetle antifreeze protein was determined by direct methods. Conclusion: Ordered crystallographic waters on the protein surface match several planes of hexagonal ice. Significance: The structure is the largest determined ab initio without heavy atoms, and its ordered waters suggest a molecular basis for ice binding.

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Section: Resultsmentioning

confidence: 99%

Crystal Structure of an Insect Antifreeze Protein and Its Implications for Ice Binding

Hakim

Nguyen

Basu

et al. 2013

Journal of Biological Chemistry

103

121

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“…Similar AFPs are present in other beetles (Qiu et al, 2010;Mao et al, 2011). The inquisitor beetle Rhagium inquisitor (Kristiansen et al, 2011) and related Rhagium mordax (Kristiansen et al, 2012) have evolved AFPs different from the other beetles, some with greater specific activity. The increased activity may result from the expansion of the ice-binding motif beyond the T-C-T to include additional threonines (T-X-T-X-T-X-T) in repeats separated by residues that lack obvious repeats.…”

Section: Coleoptera (Beetle) Antifreeze Proteinsmentioning

confidence: 71%

Animal ice-binding (antifreeze) proteins and glycolipids: an overview with emphasis on physiological function

Duman¹

2015

Journal of Experimental Biology

136

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Ice-binding proteins (IBPs) assist in subzero tolerance of multiple cold-tolerant organisms: animals, plants, fungi, bacteria etc. IBPs include: (1) antifreeze proteins (AFPs) with high thermal hysteresis antifreeze activity; (2) low thermal hysteresis IBPs; and (3) icenucleating proteins (INPs). Several structurally different IBPs have evolved, even within related taxa. Proteins that produce thermal hysteresis inhibit freezing by a non-colligative mechanism, whereby they adsorb onto ice crystals or ice-nucleating surfaces and prevent further growth. This lowers the so-called hysteretic freezing point below the normal equilibrium freezing/melting point, producing a difference between the two, termed thermal hysteresis. True AFPs with high thermal hysteresis are found in freeze-avoiding animals (those that must prevent freezing, as they die if frozen) especially marine fish, insects and other terrestrial arthropods where they function to prevent freezing at temperatures below those commonly experienced by the organism. Low thermal hysteresis IBPs are found in freeze-tolerant organisms (those able to survive extracellular freezing), and function to inhibit recrystallization -a potentially damaging process whereby larger ice crystals grow at the expense of smaller ones -and in some cases, prevent lethal propagation of extracellular ice into the cytoplasm. Ice-nucleator proteins inhibit supercooling and induce freezing in the extracellular fluid at high subzero temperatures in many freeze-tolerant species, thereby allowing them to control the location and temperature of ice nucleation, and the rate of ice growth. Numerous nuances to these functions have evolved. Antifreeze glycolipids with significant thermal hysteresis activity were recently identified in insects, frogs and plants.

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“…However, as we shall see in the following discussion, in some organisms, certain sequences or motifs and structures seem to be favored, whether they evolved by convergent evolution or from a common ancestral protein (Cheng and DeVries, 2002;Kristiansen et al, 2012;Hakim et al, 2013).…”

Section: Types Of Afpmentioning

confidence: 93%

“…In polar fish, antifreeze activity (i.e., separation of the melting point and HFP) is at maximum about 1.2 C (Cheng and DeVries, 1991). In insects, which have the highest antifreeze activity, it is up to about 8 C Wilkens and Ramløv, 2009;Kristiansen et al, 2012), but activities of 13 C under certain circumstances were mentioned by Bennett et al (2005). However, in plants, fungi, and so forth, antifreeze activity is significantly lower, often no more than a few tenths of a degree centigrade (Griffith et al, 1992).…”

Section: Afps In Various Organismsmentioning

confidence: 99%

“…However, the structures of only a few are known. These include the beetles (Coleoptera) T. molitor (Liou et al, 1999(Liou et al, , 2000a, D. canadensis (Andorfer and Duman, 2000), Microdera punctipennis (Zhao et al, 2005;Qiu et al, 2010), Anatolica polita (Mao et al, 2011), R. inquisitor, and R. mordax (Kristiansen et al, 2011(Kristiansen et al, , 2012. Within the order Lepidoptera, the structures of AFPs from moth species of the genus Choristoneura (Tyshenko et al, 2005) and the inchworm Campaea perlata (Lin et al, 2011) have been characterized.…”

Section: Insect Afpsmentioning

confidence: 99%

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