Immunoglobulin G Fragment Crystallizable Glycosylation Hematopoietic Stem Cell Transplantation Is Dissimilar to Donor Profiles
Autor: | Noortje de Haan, Manfred Wuhrer, Gertjan J. Driessen, Maarten J. D. van Tol, Arjan C. Lankester |
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Přispěvatelé: | Pediatrics |
Rok vydání: | 2018 |
Předmět: |
lcsh:Immunologic diseases. Allergy
Male 0301 basic medicine Glycosylation Adolescent medicine.medical_treatment Immunology Graft vs Host Disease Hematopoietic stem cell transplantation Immunoglobulin G 03 medical and health sciences chemistry.chemical_compound immunoglobulin G 0302 clinical medicine Antibody Specificity medicine Humans Immunology and Allergy Child B cell biology Chemistry fragment crystallizable glycosylation Immunoglobulin Fc Fragments Infant immune reconstitution Hematopoietic Stem Cells medicine.disease Tissue Donors 3. Good health carbohydrates (lipids) Transplantation Leukemia surgical procedures operative 030104 developmental biology medicine.anatomical_structure Case-Control Studies Child Preschool 030220 oncology & carcinogenesis N-glycan hematopoietic stem cell transplantation biology.protein Female Antibody lcsh:RC581-607 |
Zdroj: | Frontiers in Immunology, 9:1238. Frontiers Media S.A. Frontiers in Immunology Frontiers in Immunology, 9 Frontiers in Immunology, Vol 9 (2018) |
ISSN: | 1664-3224 |
Popis: | Immunoglobulin G (IgG) fragment crystallizable (Fc) N-glycosylation has a large influence on the affinity of the antibody for binding to Fcγ-receptors (FcγRs) and C1q protein, thereby influencing immune effector functions. IgG Fc glycosylation is known to be partly regulated by genetics and partly by stimuli in the microenvironment of the B cell. Following allogeneic hematopoietic stem cell transplantation (HSCT), and in the presence of (almost) complete donor chimerism, IgG is expected to be produced by, and glycosylated in, B cells of donor origin. We investigated to what extent IgG glycosylation in patients after transplantation is determined by factors of the donor (genetics) or the recipient (environment). Using an IgG subclass-specific liquid chromatography–mass spectrometry method, we analyzed the plasma/serum IgG Fc glycosylation profiles of 34 pediatric patients pre-HSCT and at 6 and 12 months post-HSCT and compared these to the profiles of their donors and age-matched healthy controls. Patients treated for hematological malignancies as well as for non-malignant hematological diseases showed after transplantation a lower Fc galactosylation than their donors. Especially for the patients treated for leukemia, the post-HSCT Fc glycosylation profiles were more similar to the pre-HSCT recipient profiles than to profiles of the donors. Pre-HSCT, the leukemia patient group showed as distinctive feature a decrease in sialylation and in hybrid-type glycans as compared to healthy controls, which both normalized after transplantation. Our data suggest that IgG Fc glycosylation in children after HSCT does not directly mimic the donor profile, but is rather determined by persisting environmental factors of the host. |
Databáze: | OpenAIRE |
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