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Is the Galα(1,3)Gal epitope a major target for human xenoantibodies on pig fetal islet cells?
Author(s) -
Rydberg Lennart,
Groth CarlGustav,
Möller Erna,
Tibell Annika,
Samuelsson Bo E.
Publication year - 1995
Publication title -
xenotransplantation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.052
H-Index - 61
eISSN - 1399-3089
pISSN - 0908-665X
DOI - 10.1111/j.1399-3089.1995.tb00083.x
Subject(s) - epitope , islet , antibody , chemistry , radioimmunoassay , galactose , immune system , antigen , microbiology and biotechnology , fetus , glycolipid , biology , biochemistry , immunology , endocrinology , pregnancy , genetics , insulin
Abstract: The immune antibodies produced in diabetic patients by the challenge of the immune system with pig fetal islet‐like cell clusters were analyzed in regard to carbohydrate specificity. Binding of antibodies to total non‐acid glycosphingolipid fractions from pig aorta and pig erythrocytes was tested in a radioimmunoassay using native serum, serum adsorbed on solid phase columns with either Galα(1,3)Gal specificity or Galα(1,4)Gal specificity. The eluates from the columns were also tested. Adsorption on the Galα(1,3)Gal column completely eliminated binding both to aortic and erythrocytic fractions, while adsorption on the Galα(1,4)Gal column reduced the binding but did not eliminate it. This can be explained by the presence of at least two kinds of antibodies, one recognizing terminal α‐linked galactose and the other recognizing the Galα(1,3)Gal epitope, thus requiring a disaccharide for binding. A total non‐acid glycolipid fraction was prepared from porcine fetal islet‐like cell clusters and tested against immune serum from a patient transplanted with such cells. Binding was only found to the pentaglycosylceramide region with an identical retention time as the “linear B” antigen for pig aorta. This indicates the presence of that structure also in porcine fetal islet‐like cell clusters.