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Glycobiology, 2002, Vol. 12, No. 3 173-182
© 2002 Oxford University Press

Absorption of anti–blood group A antibodies on P-selectin glycoprotein ligand-1/immunoglobulin chimeras carrying blood group A determinants: core saccharide chain specificity of the Se and H gene encoded {alpha}1,2 fucosyltransferases in different host cells

Jonas C. Löfling1, Elenor Hauzenberger and Jan Holgersson

Division of Clinical Immunology, F79, IMP1, Karolinska Institutet, Huddinge University Hospital AB, S-141 86 Stockholm, Sweden

To specifically eliminate recipient anti-blood group ABO antibodies prior to ABO-incompatible organ or bone marrow transplantation, an efficient absorber of ABO antibodies has been developed in which blood group determinants may be carried at high density and by different core saccharide chains on a mucin-type protein backbone. The absorber was made by transfecting different host cells with cDNAs encoding a P-selectin glycoprotein ligand-1/mouse immunoglobulin G2b chimera (PSGL-1/mIgG2b), the H- or Se-gene encoded {alpha}1,2-fucosyltransferases (FUT1 or FUT2) and the blood group A gene encoded {alpha}1,3 N-acetylgalactosaminyltransferase ({alpha}1,3 GalNAcT). Western blot analysis of affinity-purified recombinant PSGL-1/mIgG2b revealed that different precursor chains were produced in 293T, COS-7m6, and Chinese hamster ovary (CHO)-K1 host cells coexpressing FUT1 or FUT2. FUT1 directed expression of H type 2 structures mainly, whereas FUT2 preferentially made H type 3 structures. None of the host cells expressing either FUT1 or FUT2 supported expression of H type 1 structures. Furthermore, the highest A epitope density was on PSGL-1/mIgG22b made in CHO-K1 cells coexpressing FUT2 and the {alpha}1,3 GalNAcT. This PSGL-1/mIgG2b was used for absorption of anti–blood group A antibodies in human blood group O serum. At least 80 times less A trisaccharides on PSGL-1/mIgG2b in comparison to A trisaccharides covalently linked to macroporous glass beads were needed for the same level of antibody absorption. In conclusion, PSGL-1/mIgG2b, if substituted with A epitopes, was shown to be an efficient absorber of anti–blood group A antibodies and a suitable model protein for studies on protein glycosylation.

1 To whom correspondence should be addressed


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