Abstract:
:Various biological activities of immunoglobulin G (IgG) including antibody-dependent cellular cytotoxicity (ADCC) are modulated by the structural features of the N-glycans in the Fc part. In this study, we describe a population of IgG1 alloantibodies which are formed during pregnancy against human platelet antigens (HPA) of the fetus, causing fetoneonatal alloimmune thrombocytopenia. By analyzing the Fc-glycosylation of the pathogenic, affinity-purified IgG1 alloantibodies at the glycopeptide level using mass spectrometry, we found markedly decreased levels of core-fucosylation as well as increased levels of galactosylation and sialylation as compared to glycosylation patterns of total serum IgG1 of the same patients. Because IgG1 Fc-core-fucosylation is known to influence ADCC activity, modulation of core-fucosylation may have a profound effect on disease severity and prognosis. Studies in large patient cohorts will have to be performed to establish such correlations. Moreover, experiments in animal models as well as in vitro immunological tests will be needed to unravel the mechanisms regulating IgG Fc glycosylation.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Wuhrer M,Porcelijn L,Kapur R,Koeleman CA,Deelder A,de Haas M,Vidarsson Gdoi
10.1021/pr800651jsubject
Has Abstractpub_date
2009-02-01 00:00:00pages
450-6issue
2eissn
1535-3893issn
1535-3907journal_volume
8pub_type
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