| Autor: |
Kumpel, Belinda M, Saldova, Radka, Koeleman, Carolien AM, Abrahams, Jodie L, Ederveen, Agnes Hipgrave, Armour, Kathryn L, Olovnikova, Natalia I, Vidarsson, Gestur, Kapur, Rick, Rudd, Pauline M, Wuhrer, Manfred |
| Předmět: |
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| Popis: |
Anti-D immunoglobulin (Anti-D Ig) prophylaxis prevents haemolytic disease of the fetus and newborn. Monoclonal IgG anti-Ds (mAb-Ds) would enable unlimited supplies but have differed in efficacy in FcγRIIIa-mediated ADCC assays and clinical trials. Structural variations of the oligosaccharide chains of mAb-Ds are hypothesised to be responsible. Quantitative data on 12 Fc-glycosylation features of 23 mAb-Ds (12 clones, 5 produced from multiple cell lines) and one blood donor-derived anti-D Ig were obtained by HPLC and mass spectrometry using 3 methods. Glycosylation of mAb-Ds from human B-lymphoblastoid cell lines (B) was similar to anti-D Ig although fucosylation varied, affecting ADCC activity. In vivo, two B mAb-Ds with 77-81% fucosylation cleared red cells and prevented D-immunisation but less effectively than anti-D Ig. High fucosylation (>89%) of mouse-human heterohybridoma (HH) and Chinese hamster ovary (CHO) mAb-Ds blocked ADCC and clearance. Rat YB2/0 mAb-Ds with 60%) together with lower fucosylation ( |
| Databáze: |
OpenAIRE |
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