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  • 1
    Electronic Resource
    Electronic Resource
    The reducing end of αGal oligosaccharides contributes to their efficiency in blocking natural antibodies of human and baboon sera (1996)
    Springer
    Transplant international 9 (1996), S. 98-101 
    Details
    ISSN: 1432-2277
    Keywords: Xenotransplantation, natural antibodies, oligosaccharides ; Oligosaccharides, xenotransplantation ; Natural antibodies, xenotransplantation ; Baboon, xenotransplantation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Synthetic galactosyl oligosaccharides were tested for their ability to inhibit the cytotoxic reaction of human and baboon natural antibodies on PK15 cells in culture. Methyl-α-Gal gave weak inhibition, Galα1-3Gal substantially inhibited the reaction (400 μM), and Galα1-3Galβ2-4GlcNAc was ten times more efficient (30 μM). The modification from α to β anomeric configuration of the nonreducing end resulted in a complete loss of activity, while substitutions at the reducing end induced only a partial loss of activity. These observations suggest that natural anti-αGal antibodies recognize the epitope from its nonreducing end, but that substitutions at the reducing terminus can modify the antibody-binding capacity. Modified tri- and tetrasaccharides are better inhibitors than the disaccharide but not as good as Galα1-3Galβ1-4GlcNAc. The reducing terminus therefore contributes some energy to the reaction, indicating that certain oligosaccharides will be of more potential clinical use than others.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00336385
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular basis for erythrocyte Le(a+b+) and salivary ABH partial-secretor phenotypes: expression of a FUT2 secretor allele with an A→T mutation at nucleotide 385 correlates with reducedα(1,2) fucosyltransferase activity (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 985-993 
    Details
    ISSN: 1573-4986
    Keywords: secretor ; fucosyltransferase ; Lewis a ; Lewis b ; saliva ABH ; blood group ; FUT2 ; ABO ; Polynesia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract TheSe wA385T mutation of the FUT2 gene was found to correlate with both the erthrocyte Le(a+b+) and/or salivary ABH partial-secretor phenotypes of Polynesians. Constructs with FUT1 and FUT2 wild type genes, and the FUT2Se wA385T,se G428A andse C571T mutated alleles, were cloned into pcDNAI, and expressed in COS-7 cells. COS-7 cells transfected with theSe wA385T allele had weak, but detectable, α(1,2)fucosyltransferase activity, with an acceptor substrate pattern similar to the wild type FUT2 gene. Comparative kinetic studies from cell extracts with mutatedSe wA385T and wild type FUT2 alleles gave similarK m values, but less enzyme activity was present in cells transfected withSe wA385T (V max 230 pmol h−1 mg−1), as compared to those transfected with FUT2 (V max 1030 pmol h−1 mg−1), suggesting that the mutated enzyme is more unstable. These results confirm that the molecular basis for the erythrocyte Le(a+b+) and the associated ABH salivary partial-secretor phenotype, is an amino acid change of Ile 129→Phe in the secretor α(1,2)fucosyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01053194
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  • 3
    Electronic Resource
    Electronic Resource
    Recognition of the blood group H type 2 trisaccharide epitope by 28 monoclonal antibodies and three lectins (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 263-271 
    Details
    ISSN: 1573-4986
    Keywords: ELISA ; synthetic oligosaccharides ; monoclonal antibodies ; blood group H ; lectins ; ABO
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The patterns of cross-reaction of 30 monoclonal antibodies and three lectins were determined by ELISA with 21 ABH, Ii or Lewis related synthetic oligosaccharides coupled to bovine serum albumin. At least seven main groups of cross-reactive patterns were identified among the antibodies, plus several intermediate patterns between two of the main antibody groups. The three lectins had different cross-reaction patterns,Galactia tenuiflora was different from all the antibodies,Ulex europaeus lectin 1 andLotus tetragonolobus were similar, but not identical to groups III and V of antibodies respectively. The anti-H antibodies cross-reacting with A type 2 gave similar agglutination scores with all the normal ABO erythrocytes, while the anti-H antibodies not cross-reacting with A type 2 reacted with different scores: O〉A2〉A2B〉B〉A1〉A1B〉Oh, suggesting that these antibodies react better with the free H epitopes and do not recognize the H in A or B epitopes. Based on the ELISA and agglutination results and the lowest energy conformations of each oligosaccharide obtained by computer modelling, the most probable oligosaccharide surface areas recognized by each antibody main group are illustrated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731501
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  • 4
    Electronic Resource
    Electronic Resource
    Computer simulation of histo-blood group oligosaccharides: energy maps of all constituting disaccharides and potential energy surfaces of 14 ABH and Lewis carbohydrate antigens (1995)
    Springer
    Glycoconjugate journal 12 (1995), S. 331-349 
    Details
    ISSN: 1573-4986
    Keywords: Blood group ; molecular modelling ; oligosaccharide conformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The three-dimensional structures of fourteen histo-blood groups carbohydrate antigens have been established through a combination of molecular mechanics and conformational searching methods. The conformational space available for each disaccharide, constituents of these determinants, has been throroughly characterized. The results have been organized in a data bank fashion. Larger relatives, i.e. 14 tri- and tetrasaccharides of histo-blood group antigens, have been modelled using a different method for exploring the complex potential energy surface. This approach is aimed at establishing all the possible families of conformations, along with the conformational pathways. Different conformational behaviours are exhibited by these oligosaccharides. Some of them, i.e. LeX and LeY tri and tetrasaccharides, are very rigid; 99% of their populations belong to the same conformational family. Others, like H type 1, H type 2 or H type 6 oligosaccharides, are essentially rigid, but a secondary conformational family, corresponding to 3–4% of the total population, can arise. Finally, the H types 3 and 4 trisaccharides, and the A type 1 and A type 2 tetrasaccharides are predicted to behave rather flexibly. The information gathered in the present investigation has been used to analyse the body of experimental evidence, either physical or biological, available for this series of carbohydrate antigens. Of special interest are the several different alignments that can be proposed for these molecules. They yield a realistic definition of the three-dimensional features of the epitopes thereby providing essential information about how carbohydrate antigens are recognized by proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731336
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    Paper (German National Licenses)
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