Thermodynamic analysis of ligand binding to winged bean (Psophocarpus tetragonolobus) acidic agglutinin reveals its specificity for terminally monofucosylated H-reactive sugars.

Acharya, Shreeta; Patanjali, Sankhavaram R.; Sajjan, S. Umadevi; Bulusu, Gopalakrishnan; Surolia, Avadhesha

doi:10.1016/s0021-9258(19)38438-8

Cited by 28 publications

(5 citation statements)

References 49 publications

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“…PTL-II is reported to recognize blood group H . In keeping with this, machine learning shows that PTL-II binds type 2 blood group H epitopes (Fuc α1,2Galβ1,4GlcNAc, Figure ).…”

Section: Resultsmentioning

confidence: 83%

A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities

et al. 2022

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Glycans are critical to every facet of biology and medicine, from viral infections to embryogenesis. Tools to study glycans are rapidly evolving, however the majority of our knowledge is deeply dependent on binding by glycan binding proteins (e.g., lectins). The specificities of lectins, which are often naturally isolated proteins, have not been welldefined, making it difficult to leverage their full potential for glycan analysis. Herein, we use glycan microarray analysis of 116 commercially available lectins, including different preparations of the same lectin, to extract the specific glycan features required for lectin binding. Data was obtained using the Consortium for Functional Glycomics microarray (CFG v5.0) containing 611 glycans. We use a combination of machine learning algorithms to define lectin specificity, mapping inputs (glycan sequences) to outputs (lectin-glycan binding) for a large-scale evaluation of lectin-glycan binding behaviours. Our motif analysis was performed by integrating 68 manually defined glycan features with systematic probing of computational rules for significant binding motifs using mono-and disaccharides-and linkages. Using a combination of machine learning and manual annotation of the data, we created a detailed interpretation of glycan-binding specificity for 57 unique lectins, categorized by their major binding motifs: mannose, complex-type N-glycan, O-glycan, fucose, sialic acid and sulfate, GlcNAc and chitin, Gal and LacNAc, and GalNAc. Our work provides fresh insights into the complex binding features of commercially available lectins in current use, providing a critical guide to these important reagents.

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“…PTL-II is reported to recognize blood group H . In keeping with this, machine learning shows that PTL-II binds type 2 blood group H epitopes (Fuc α1,2Galβ1,4GlcNAc, Figure ).…”

Section: Resultsmentioning

confidence: 83%

A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities

et al. 2022

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“…Protein Purification . Con A and WBA II were purified by affinity chromatography from jack bean and winged bean seeds, respectively ( , ). Their purity was checked by sodium dodecyl sulfate−polyacrylamide gel electrophoresis.…”

Section: Methodsmentioning

confidence: 99%

Conformational Stability of Legume Lectins Reflect Their Different Modes of Quaternary Association: Solvent Denaturation Studies on Concanavalin A and Winged Bean Acidic Agglutinin

et al. 2002

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Thermodynamic parameters associated with the unfolding of the legume lectin, WBA II, were determined by isothermal denaturation. The analysis of isothermal denaturation data provided values for conformational stability and heat capacity for WBA II unfolding. To explore the role of intersubunit contact in stability, we carried out similar studies under identical conditions on Concanavalin A, a legume lectin of nearly similar size, buried hydrophobic surface area and tertiary structure to that of WBA II but with a different oligomerization pattern. Both proteins showed a reversible two-state unfolding with guanidine hydrochloride. As expected, the change in heat capacity upon unfolding was similar for both proteins at 3.5 and 3.7 kcal mol(-1) K(-1) for Concanavalin A and WBA II, respectively. Although the deltaG(H20) at the maximum stability of both proteins is around 16 kcal/mol, Concanavalin A exhibits greater stability at higher temperatures. The T(g) obtained for Concanavalin A and WBA II were 21 degrees C apart at 87.2 and 66.6 degrees C, respectively. The higher conformational stability at higher temperatures and the T(g) of Concanavalin A as compared to that of WBA II are largely due to substantial differences in the degree of subunit contact in these dimeric proteins. Ionic interactions and hydrogen bonding between the monomers of the two proteins also seem to play a significant role in the observed stability differences between these two proteins.

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“…The 29 kDa subunit contains a single binding site. WBA II is a homodimeric glycoprotein (pI 5.5) of 54 kDa which binds to the terminal fucosylated H-antigenic determinant either on human erythrocytes or in solution. , …”

Section: Winged Bean Agglutininsmentioning

confidence: 99%

“…WBA II is a homodimeric glycoprotein (pI 5.5) of 54 kDa which binds to the terminal fucosylated H-antigenic determinant either on human erythrocytes or in solution. 149,150 1. WBA I Schwarz and co-workers 151 reported an ITC binding study of WBA I with Gal, GalNAc, MeRGal, and MeβGal.…”

Section: Winged Bean Agglutininsmentioning

confidence: 99%

Thermodynamic Studies of Lectin−Carbohydrate Interactions by Isothermal Titration Calorimetry

2002

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Thermodynamic analysis of ligand binding to winged bean (Psophocarpus tetragonolobus) acidic agglutinin reveals its specificity for terminally monofucosylated H-reactive sugars.

Cited by 28 publications

References 49 publications

A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities

A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities

Conformational Stability of Legume Lectins Reflect Their Different Modes of Quaternary Association: Solvent Denaturation Studies on Concanavalin A and Winged Bean Acidic Agglutinin

Thermodynamic Studies of Lectin−Carbohydrate Interactions by Isothermal Titration Calorimetry

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