Molecular recognition XIII. The binding of the H-type 2 human blood group determinant by a winged bean (Psophocarpus tetragonolobus) acidic lectin

1994 ◽  
Vol 72 (1) ◽  
pp. 158-163 ◽  
Author(s):  
Raymond U. Lemieux ◽  
Ming-Hui Du ◽  
Ulrike Spohr ◽  
Shreeta Acharya ◽  
Avadhesha Surolia
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Acetyl Derivative ◽  
Bulk Water ◽  
Winged Bean ◽  
Hydroxyl Groups ◽  
Human Blood Group ◽  
Methyl Derivatives

The winged bean acidic lectin (WBA II) binds the H-type 2 human blood group related trisaccharide (α-L-Fuc-(1c → 2b)-β-D-Gal-(1b → 4a)-β-D-GlcNAc-OMe, 1). Interactions that importantly contribute to the specificity of the complex formation are provided by CH2-6b, OH-4b, OH-3b, and OH-2c of 1. On the basis of the relative activities of the monodeoxy and mono-O-methyl derivatives of 1, the hydroxyl groups at the 3a, 6a, and 4c positions become located at the periphery of the combining site, whereas the CH3O-1a, NHAc-2a, and CH3-5c groups are more remote from the protein surface and fully exposed to bulk water. Whereas the WBA II lectin marginally recognizes the H-type 1 related trisaccharide (α-L-Fuc-(1c → 2b)-β-D-Gal-(1b → 3a)-β-D-GlcNAc-OMe, 23), the de-N-acetyl derivative (24) is bound 3.4 times more strongly than 1. This and other results, which are related to changes in interaction between the ligand and the apron of the combining site, are attributed to changes in hydration that lead to enthalpy–entropy compensation. In certain cases, the interactions are found to stabilize the complex.

Molecular recognition XII. The binding of the H human blood group determinants and congeners by a lectin of Galactiatenuiflora

1992 ◽  
Vol 70 (5) ◽  
pp. 1511-1530 ◽  
Author(s):  
Rémy Cromer ◽  
Ulrike Spohr ◽  
Deveshwari P. Khare ◽  
Jacques LePendu ◽  
Raymond U. Lemieux
Keyword(s):  
Molecular Recognition ◽  
Complex Formation ◽  
Blood Group ◽  
Aqueous Phase ◽  
Human Blood ◽  
Hydroxyl Groups ◽  
Human Blood Group ◽  
Hydrogen Bonded

The H-type 2 human blood group-related trisaccharide (α-L-Fuc-(1c → 2b)-β-D-Gal-(1b → 4a)-β-D-GlcNAc-OMe (52)) is bound by the anti-H lectin of Galactiatenuiflora very differently than by the lectin I of Ulexeuropaeus. The reason why the Galactia lectin binds the H-type 1 related trisaccharide (α-L-Fuc-(1c → 2b)-β-D-Gal-(1b → 3a)-β-D-GlcNAc-OMe (5)) more strongly and methyl α-L-fucopyranoside much more weakly than does the Ulex lectin is that, for the Galactia lectin, the hydroxyl groups at positions 3a, 3b, 4b, and 4c are indispensable to complex formation whereas it is the hydroxyl groups at positions 3b, 2c, 3c, and 4c which provide the key polar intractions in the case of the Ulex lectin. The H-type 2 (52)•Galactia lectin complex appears to have the hydroxyl groups at positions 6b, 2c, and 3c at or near the periphery of the combining site and the three key hydroxyl groups hydrogen bonded to the protein deep within the combining site and sheltered from water. The CH3O-1a, NHAc-2a, and CH2OH-6a groups likely remain in the aqueous phase remote from the surface of the protein.

Molecular recognition XI. The synthesis of extensively deoxygenated derivatives of the H-type 2 human blood group determinant and their binding by an anti-H-type 2 monoclonal antibody and the lectin 1 of Ulexeuropaeus

1992 ◽  
Vol 70 (1) ◽  
pp. 254-271 ◽  
Author(s):  
Ulrike Spohr ◽  
Eugenia Paszkiewicz-Hnatiw ◽  
Naohiko Morishima ◽  
Raymond U. Lemieux
Keyword(s):  
Monoclonal Antibody ◽  
Molecular Recognition ◽  
Blood Group ◽  
Human Blood ◽  
Water Molecules ◽  
Hydroxyl Groups ◽  
Human Blood Group ◽  
Derivatives Of ◽  
Hydrogen Bonded

The relative potencies of a wide variety of deoxygenated derivatives of the methyl glycoside of α-L-Fuc-(1 → 2)-β-D-Gal-(1 → 4)- β-D-GlcNAc (the H-type 2 human blood group related trisaccharide) for the inhibition of the binding of an artificial H-type 2 antigen by the lectin I of Ulexeuropaeus confirmed the previous evidence that the key and productive interaction involves only the three hydroxyl groups of the α-L-fucose unit, the hydroxyl at the 3-position of the β-D-galactose residue, and the nonpolar groups in their immediate environment. Except for the acetamido group and the hydroxymethyl of the β-D-Gal unit, which stay in the aqueous phase, on complex formation the remaining three hydroxyl groups appear to come to reside at or near the periphery of the combining site since their replacement by hydrogen causes relatively small changes (< ± 1 kcal/mol) in the stability of the complex (ΔG0). Relatively much larger but compensating changes occur for the enthalpy and entropy terms, and these may arise primarily from the differences in the water structure about the periphery of the combining site and the oligosaccharide both prior to and after complexation. It is proposed that steric constraints lead to an ordered state of the water molecules hydrogen-bonded to the polar groups within the cleft formed by the key region of the amphiphilic combining site. Their release to form less ordered clusters of more strongly hydrogen-bonded water molecules in bulk solution would contribute importantly to the driving force for complexation. It is demonstrated that the surface used for the binding of H-type 2-OMe by a monoclonal anti-H antibody is virtually identical to that used by the Ulex lectin. Keywords: molecular recognition, H-type 2 blood group determinant and deoxygenated derivatives, lectin I of Ulexeuropaeus, anti-H-type 2 monoclonal antibody, enthalpy–entropy compensation.

The conformations of oligosaccharides related to the ABH and Lewis human blood group determinants

1980 ◽  
Vol 58 (6) ◽  
pp. 631-653 ◽  
Author(s):  
R. U. Lemieux ◽  
K. Bock ◽  
L. T. J. Delbaere ◽  
S. Koto ◽  
V. S. Rao
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Antigenic Determinants ◽  
Anomeric Effect ◽  
Human Blood Group ◽  
Good Accord ◽  
Resonance Properties ◽  
Synthetic Oligosaccharides

Nuclear magnetic resonance properties are shown to be in good accord with those that are expected for synthetic oligosaccharides in the conformations which are predicted by hard-sphere molecular modelling and taking into consideration the important contribution by the exo-anomeric effect. The studies involve first a comparison of the βDGal(1 → 3)βDGlcNAc (Type 1) and βDGal(1 → 4)βDGlcNAc (Type 2) disaccharide structures based mainly on 13Cmr and then an examination of the relationships between the calculated conformations and 1Hmr and 13Cmr parameters for human blood group determinants which are derived from the Type 1 core disaccharide. Among the structures examined are the di-, tri-, and tetrasaccharides for the ABH and Lewis antigenic determinants. Certain immunological–conformational relationships are noted.

A highly convergent synthesis of an N-linked glycopeptide presenting the H-type 2 human blood group determinant

Tetrahedron ◽  
2006 ◽  
Vol 62 (20) ◽  
pp. 4954-4978 ◽  
Author(s):  
Zhi-Guang Wang ◽  
J. David Warren ◽  
Vadim Y. Dudkin ◽  
Xufang Zhang ◽  
Ulrich Iserloh ◽  
...  
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Convergent Synthesis ◽  
Human Blood Group

ChemInform Abstract: Toward Fully Synthetic Homogeneous Glycoproteins: A High Mannose Core Containing Glycopeptide Carrying Full H-Type 2 Human Blood Group Specificity.

ChemInform ◽  
2010 ◽  
Vol 32 (34) ◽  
pp. no-no
Author(s):  
Zhi-Guang Wang ◽  
Xufang Zhang ◽  
Michael Visser ◽  
David Live ◽  
Andrzej Zatorski ◽  
...  
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Human Blood Group ◽  
Group Specificity ◽  
High Mannose

Molecular recognition of a human blood group determinant by a plant lectin

1990 ◽  
Vol 68 (7) ◽  
pp. 1116-1121 ◽  
Author(s):  
Louis T. J. Delbaere ◽  
Margaret Vandonselaar ◽  
Lata Prasad ◽  
J. Wilson Quail ◽  
Joyce R. Pearlstone ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Binding Site ◽  
Blood Group ◽  
Human Blood ◽  
Noncovalent Complex ◽  
Side Chain ◽  
Hydroxyl Groups ◽  
Binding Studies ◽  
Con A ◽  
Human Blood Group

The lectin IV of Griffoniasimplicifolia (GS4) specifically binds the terminal tetrasaccharide unit of the Lewis b human blood group determinant (Leb). The single crystal X-ray analysis of the complex with Leb-OMe has demonstrated that the binding site on the lectin is a shallow depression with a negatively charged aspartate side chain at the bottom of the cavity. In addition to this aspartate, a serine and an asparagine side chain provide the polar groups that hydrogen bond to the three hydroxyl groups of Leb, which has been termed the key polar grouping for complex formation. A notable characteristic of the binding site is that five aromatic amino acid side chains (one Phe, two Tyr, and two Trp residues) surround these polar interactions and make van der Waals contacts with the tetrasaccharide. Thus, as predicted from previous solution binding studies, extensive nonpolar interactions are involved, which contribute importantly both to the specificity of the reaction and the stability of the noncovalent complex that is formed. These results represent the first structural example of the molecular recognition of a human blood group determinant by the receptor site of a protein. Extensive sequence homology exists between GS4 and the concanavalin A (Con A), pea, and favin lectins. The main hydrophilic groups of the carbohydrate-binding site of GS4 and Con A are aspartate, asparagine, and serine residues; the homology suggests that the serine is replaced by asparagine in the case of the pea and favin lectins. It appears probable that these two latter lectins possess very similar, if not identical, specificities. Keywords: lectin, carbohydrate, molecular recognition, binding.

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