The Ice-Binding Site of Atlantic Herring Antifreeze Protein Corresponds to the Carbohydrate-Binding Site of C-Type Lectins

Ewart, K. Vanya; Li, Zhengjun; Yang, Dan; Fletcher, George P.; Hew, Choy L.

doi:10.1021/bi972503w

Cited by 70 publications

(48 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Apart from calcium-dependent carbohydrate binding, CRDs of other C-type lectins have been reported to bind noncarbohydrate ligands, including proteins, lipids (21), and ice (22). Examples of protein ligands include the coagulation factors IX/Xbinding protein (23), the low-affinity IgE-Fc⑀ receptor (CD23; Ref.…”

Section: Tetranectin (Tn)mentioning

confidence: 99%

The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine

Graversen¹,

Lorentsen²,

Jacobsen³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

Tetranectin, a homotrimeric protein belonging to the family of C-type lectins and structurally highly related to corresponding regions of the mannose-binding proteins, is known specifically to bind the plasminogen kringle 4 protein domain, an interaction sensitive to lysine. Surface plasmon resonance and isothermal calorimetry binding analyses using single-residue and deletion mutant tetranectin derivatives produced in Escherichia coli showed that the kringle 4 binding site resides in the carbohydrate recognition domain and includes residues of the putative carbohydrate binding site. Furthermore, the binding analysis revealed that the interaction is sensitive to calcium in addition to lysine.

show abstract

Section: Tetranectin (Tn)mentioning

confidence: 99%

The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine

Graversen¹,

Lorentsen²,

Jacobsen³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…, a type II AFP adopts a new conformation that creates the icebinding domain (Ewart et al, 1996(Ewart et al, , 1998(Ewart et al, , 1999(Ewart et al, , 2000Achenbach and Ewart, 2002). However, Ca 21 had no effect on antifreeze activity in unfrozen winter rye extracts (Fig.…”

mentioning

confidence: 98%

Calcium Interacts with Antifreeze Proteins and Chitinase from Cold-Acclimated Winter Rye

et al. 2004

View full text Add to dashboard Cite

During cold acclimation, winter rye (Secale cereale) plants accumulate pathogenesis-related proteins that are also antifreeze proteins (AFPs) because they adsorb onto ice and inhibit its growth. Although they promote winter survival in planta, these dual-function AFPs proteins lose activity when stored at subzero temperatures in vitro, so we examined their stability in solutions containing CaCl2, MgCl2, or NaCl. Antifreeze activity was unaffected by salts before freezing, but decreased after freezing and thawing in CaCl2 and was recovered by adding a chelator. Ca2+ enhanced chitinase activity 3- to 5-fold in unfrozen samples, although hydrolytic activity also decreased after freezing and thawing in CaCl2. Native PAGE, circular dichroism, and Trp fluorescence experiments showed that the AFPs partially unfold after freezing and thawing, but they fold more compactly or aggregate in CaCl2. Ruthenium red, which binds to Ca2+-binding sites, readily stained AFPs in the absence of Ca2+, but less stain was visible after freezing and thawing AFPs in CaCl2. We conclude that the structure of AFPs changes during freezing and thawing, creating new Ca2+-binding sites. Once Ca2+ binds to those sites, antifreeze activity, chitinase activity and ruthenium red binding are all inhibited. Because free Ca2+ concentrations are typically low in the apoplast, antifreeze activity is probably stable to freezing and thawing in planta. Ca2+ may regulate chitinase activity if concentrations are increased locally by release from pectin or interaction with Ca2+-binding proteins. Furthermore, antifreeze activity can be easily maintained in vitro by including a chelator during frozen storage.

show abstract

“…Type-I AFPs are found in other flounder and certain cottids (sculpins), indicating they have also evolved independently on multiple occasions (Graham et al, 2013). In contrast, type-II AFPs present in smelt, herring and some cottids (sea raven, Hemitripterus americanus) are globular, cysteine-rich and have apparently evolved from C-type lectins (Slaughter et al, 1981;Ng and Hew, 1992;Ewart et al, 1998). While some type-II AFPs require Ca 2+ for TH activity, others do not, once again suggesting evolution from different sources.…”

Section: Structures and Evolution Of Fish Antifreeze Proteinsmentioning

confidence: 99%

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

Duman¹

2015

Journal of Experimental Biology

136

View full text Add to dashboard Cite

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.

show abstract

The Ice-Binding Site of Atlantic Herring Antifreeze Protein Corresponds to the Carbohydrate-Binding Site of C-Type Lectins

Cited by 70 publications

References 28 publications

The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine

The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine

Calcium Interacts with Antifreeze Proteins and Chitinase from Cold-Acclimated Winter Rye

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

Contact Info

Product

Resources

About