Synthesis of βDGlcNAc(1 →6) and βDGal(1 → 4)βDGlcNAc(1 → 6) derivatives of the TN (αDGalNAc) human blood group determinant

1982 ◽  
Vol 60 (1) ◽  
pp. 76-80 ◽  
Author(s):  
Raymond U. Lemieux ◽  
Maria Halina Burzynska
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Antigenic Determinants ◽  
Immunological Properties ◽  
Human Blood Group ◽  
Chloride Method ◽  
Derivatives Of

In order to investigate the immunological properties of certain I blood group specific glycoproteins, the potential antigenic determinants βDGlcNAc(1 → 6)αDGalNAc and βDGal(1 → 4)βDGlcNAc(1 → 6)αDGalNAc attached as glycosides to 8-methoxy-carbonyloctanol were synthesized by way of the phthalimido-chloride method.

Syntheses of core chain trisaccharides related to human blood group antigenic determinants

1982 ◽  
Vol 60 (1) ◽  
pp. 68-75 ◽  
Author(s):  
R. U. Lemieux ◽  
S. Z. Abbas ◽  
B. Y. Chung
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Antigenic Determinants ◽  
Human Blood Group ◽  
The Core ◽  
Chloride Method

Trisaccharides related to the core chain of human blood group determinants were synthesized by way of the phthalimido-chloride method; namely, β-D-Galp-(1 → 3)-β-D-GlcNAcp-(1 → 6)-D-Galp (3), β-D-Galp-(1 → 3)-β-D-GlcNAcp-(1 → 3)-D-Galp (5), β-D-Galp-(1 → 4)-β-D-GlcNAcp-(1 → 6)-D-Galp (4), and β-D-Galp-(1 → 4)-β-D-GlcNAcp-(1 → 3)-D-Galp (6). The syntheses of the 8-methoxy-carbonyloctyl β-glycosides of these trisaccharides are also reported.

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.

Molecular recognition. VIII. The binding of the β-D-galactopyranosyl residue of the Lewis b human blood group determinant by the lectin IV of Griffonia simplicifolia and by a monoclonal anti-Lewis b antibody. Evidence for intramolecular hydrogen bonding

1988 ◽  
Vol 66 (12) ◽  
pp. 3083-3098 ◽  
Author(s):  
Raymond U. Lemieux ◽  
Rémy Cromer ◽  
Ulrike Spohr
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Parent Compound ◽  
Intramolecular Hydrogen Bonding ◽  
The Other ◽  
Griffonia Simplicifolia ◽  
Human Blood Group ◽  
Weak Binding ◽  
Intramolecular Hydrogen ◽  
Derivatives Of

The 3b-deoxy, 4b-deoxy, 6b-deoxy, 6b-deoxy-6b-fluoro, 6b-chloro-6b-deoxy, and the 5b-des-hydroxymethyl derivatives of the Lewis b (αLFucd(1 → 2)βDGalb(1 → 3)[αLFucc(1 → 4)]βDGlcNAca-OMe) human blood group determinant were synthesized in order to examine the involvement of the βDGal b unit in the binding of the Leb-OMe tetrasaccharide both by the lectin IV of Griffonia simplicifolia and a hybridoma monoclonal anti-Leb antibody. The replacement of the CH2OH-5b group by hydrogen resulted in very weak binding by both the proteins, but the 6b-deoxy derivative was bound nearly as strongly as the parent compound in the case of the lectin but nine times more strongly in the case of the antibody. The 6b-fluoride was slightly more strongly bound than the 6b-deoxy derivative by both the proteins. On the other hand, the 6b-chloride was bound three times more strongly by the lectin but three times more weakly by the antibody than the 6b-deoxy derivative. The thermodynamic parameters for the binding of the 6b-deoxy derivative by the lectin as compared to those for Leb-OMe confirmed that OH-6b interacts within the combining site of the complex. The results appear to require that for both proteins the CH2OH-5b group becomes involved in nonpolar interactions within the combining site. It seems probable that OH-6b is accepted intramolecularly hydrogen bonded to O-5b in the case of the lectin but to OH-4b in the case of the antibody. The involvement of OH-3b, OH-4b, and OH-4c as the key polar grouping for the binding of Leb-OMe by the lectin and of OH-3b and OH-2d in the case of the antibody was reported previously.

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.

Molecular recognition. II. The binding of the Lewis b and Y human blood group determinants by the lectin IV of Griffoniasimplicifolia

1985 ◽  
Vol 63 (10) ◽  
pp. 2644-2652 ◽  
Author(s):  
Ulrike Spohr ◽  
Ole Hindsgaul ◽  
Raymond U. Lemieux
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Association Constants ◽  
Binding Reaction ◽  
Human Blood Group ◽  
Chemically Modified ◽  
Inhibition Data ◽  
Topographical Feature ◽  
Derivatives Of ◽  
Relative Potencies

Using a radioimmunoassay to measure the relative potencies as inhibitors of a wide number of chemically modified structures related to the Lewis b human blood group determinant, it was found that derivatives of the Lewis b (αLFuc(1→2)βDGal(1→3)[αLFuc(1→4)]βDGlcNAc) and the Y (αLFuc(1→2)PDGal(1→4)[αLFuc(1→3)]βDGlcNAc) determinants are complexed by the lectin IV of Griffoniasimplicifolia through the recognition of a topographical feature that is common to both the tetrasaccharides. This surface provides a nonpolar region formed by the two methyl groups of the fucose units and extends along the C-1—O-5—C-5 side of the αLFuc(1→2) unit and terminates at one end by a polar grouping which is formed by OH-3 and OH-4 of the βDGal unit and OH-4 of the αLFuc(1→4) unit. Association constants were determined from changes in ultraviolet absorption that occur as the result of complex formation. For the reaction of the Lewis b-OCH3 tetrasaccharide, the thermodynamic parameters were found to be ΔH = −13 kcal/mol and ΔS = −22 cal/mol/K. The inhibition data for the relevant monodeoxy derivatives indicated that OH-2 and OH-3 of both of the αLFuc units are not directly involved in the binding reaction. The basis for drawing these conclusions was strengthened by finding that the reaction of the simple Lewis b analog, methoxymethyl (1→2)βDGal(1→3)[αLFuc(1→4)]βDGlcNAcOCH3 displayed very similar thermodynamic values; namely, ΔH = −14 kcal/mol and ΔS = −26 cal/mol/K, to those mentioned above for the Leb-OCH3 tetrasaccharide. The OH-4 of the αLFuc(1→2) unit may be bound in an intramolecularly hydrogen bonded form.

scholarly journals Monoclonal antibodies specific for T cell-associated carbohydrate determinants react with human blood group antigens CAD and SDA.

1988 ◽  
Vol 167 (1) ◽  
pp. 119-131 ◽  
Author(s):  
A Conzelmann ◽  
L Lefrancois
Keyword(s):  
Sialic Acid ◽  
T Cell ◽  
Blood Group ◽  
Human Blood ◽  
Antigen Expression ◽  
Intraepithelial Lymphocytes ◽  
Cytotoxic T Cell ◽  
Antigenic Determinants ◽  
Blood Group Antigens ◽  
Human Blood Group

The CT antigenic determinants have previously been shown to be present on the T200 glycoproteins and other proteins of murine cytotoxic T cell clones but not of T helper clones or nonactivated lymphocytes (1, 2). Two determinants recognized by mAbs CT1 and CT2 are also expressed on thymocytes in a developmentally regulated fashion during fetal thymus ontogeny and are found in a subset of Lyt-2+ intraepithelial lymphocytes in the intestinal mucosa (3-5). Previous studies of the biosynthesis of CT+ proteins suggested that these determinants were composed of carbohydrate (8). We now demonstrate that the anti-CT mAbs react with a carbohydrate determinant at the nonreducing terminus of O-linked oligosaccharides that has the configuration GalNAc beta 1,4[SA alpha 2,3]-galactose. The CT antibodies detected this determinant not only on CTL clones but also in the human blood group antigens Cad and Sda+. Variant CTL lines, non-Cad erythrocytes, and Sda- glycoproteins that lacked the GalNAc residue did not bind the CT mAb. Sialic acid was essential for CT antigen expression since neuraminidase or mild periodate treatment abrogated CT antibody binding. In addition, other carbohydrate structures with terminal GalNAc residues such as the A or Tn blood group antigens were not recognized. The CT antibodies thus define GalNAc and sialic acid containing carbohydrate antigens that are expressed on discrete subsets of T lymphocytes and may also be useful reagents for the detection of Cad and Sda+ blood group antigens.

scholarly journals Human blood group glycosyltransferases. I. Purification of n-acetylgalactosaminyltransferase.

1978 ◽  
Vol 253 (2) ◽  
pp. 377-379 ◽  
Author(s):  
M. Nagai ◽  
V. Davè ◽  
B.E. Kaplan ◽  
A. Yoshida
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Human Blood Group
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