The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site

Mark James Agostino, Tony Velkov, Tamir Dingjan, Spencer John Williams, Elizabeth Yuriev, Paul Allen Ramsland

Research output: Contribution to journalArticleResearchpeer-review

7 Citations (Scopus)

Abstract

Euonymus europaeus lectin (EEL) is a carbohydrate-binding protein derived from the fruit of the European spindle tree. EEL was first identified for its erythrocyte agglutinating properties and specificity for B and H blood groups. However, a detailed molecular picture of the structural basis of carbohydrate recognition by EEL remains to be developed. In this study, we performed fluorescence titrations of a range of carbohydrates against EEL. Binding of EEL to a wide range of carbohydrates was observed, including a series of blood group-related carbohydrates, mannosides, chitotriose and sialic acid. Affinity was strongest for carbohydrates with H-related structures and the B trisaccharide. A homology model of EEL was produced from templates identified using the HHPred server, which employs hidden Markov models (HMMs) to identify templates. The HMM approach identified that the best templates for EEL were proteins featuring a ricin B-like (R-type) fold. Separate templates were used to model the core and binding site regions of the lectin. Through the use of constrained docking and spatial comparison with a template ligand, binding modes for the carbohydrate ligands were predicted. A relationship between the experimental binding energies and the computed binding energies of the selected docked poses was determined and optimized. Collectively, our results suggest that EEL utilizes a single site for recognition of carbohydrates terminating in a variety of monosaccharides.
Original languageEnglish
Pages (from-to)101 - 114
Number of pages14
JournalGlycobiology
Volume25
Issue number1
DOIs
Publication statusPublished - 2015

Cite this

Agostino, Mark James ; Velkov, Tony ; Dingjan, Tamir ; Williams, Spencer John ; Yuriev, Elizabeth ; Ramsland, Paul Allen. / The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site. In: Glycobiology. 2015 ; Vol. 25, No. 1. pp. 101 - 114.
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abstract = "Euonymus europaeus lectin (EEL) is a carbohydrate-binding protein derived from the fruit of the European spindle tree. EEL was first identified for its erythrocyte agglutinating properties and specificity for B and H blood groups. However, a detailed molecular picture of the structural basis of carbohydrate recognition by EEL remains to be developed. In this study, we performed fluorescence titrations of a range of carbohydrates against EEL. Binding of EEL to a wide range of carbohydrates was observed, including a series of blood group-related carbohydrates, mannosides, chitotriose and sialic acid. Affinity was strongest for carbohydrates with H-related structures and the B trisaccharide. A homology model of EEL was produced from templates identified using the HHPred server, which employs hidden Markov models (HMMs) to identify templates. The HMM approach identified that the best templates for EEL were proteins featuring a ricin B-like (R-type) fold. Separate templates were used to model the core and binding site regions of the lectin. Through the use of constrained docking and spatial comparison with a template ligand, binding modes for the carbohydrate ligands were predicted. A relationship between the experimental binding energies and the computed binding energies of the selected docked poses was determined and optimized. Collectively, our results suggest that EEL utilizes a single site for recognition of carbohydrates terminating in a variety of monosaccharides.",
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The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site. / Agostino, Mark James; Velkov, Tony; Dingjan, Tamir; Williams, Spencer John; Yuriev, Elizabeth; Ramsland, Paul Allen.

In: Glycobiology, Vol. 25, No. 1, 2015, p. 101 - 114.

Research output: Contribution to journalArticleResearchpeer-review

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