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IgG-Fc glycosylation before and after rituximab treatment in immune thrombocytopenia. / Schmidt, David E; de Haan, Noortje; Sonneveld, Myrthe E et al.

In: Scientific reports, Vol. 10, No. 1, 3051, 01.12.2020.

Research output: Contribution to journalArticleAcademicpeer-review

Harvard

Schmidt, DE, de Haan, N, Sonneveld, ME, Porcelijn, L, van der Schoot, CE, de Haas, M, Zwaginga, J-J, Wuhrer, M & Vidarsson, G 2020, 'IgG-Fc glycosylation before and after rituximab treatment in immune thrombocytopenia', Scientific reports, vol. 10, no. 1, 3051. https://doi.org/10.1038/s41598-020-59651-7

APA

Schmidt, D. E., de Haan, N., Sonneveld, M. E., Porcelijn, L., van der Schoot, C. E., de Haas, M., Zwaginga, J-J., Wuhrer, M., & Vidarsson, G. (2020). IgG-Fc glycosylation before and after rituximab treatment in immune thrombocytopenia. Scientific reports, 10(1), [3051]. https://doi.org/10.1038/s41598-020-59651-7

Vancouver

Schmidt DE, de Haan N, Sonneveld ME, Porcelijn L, van der Schoot CE, de Haas M et al. IgG-Fc glycosylation before and after rituximab treatment in immune thrombocytopenia. Scientific reports. 2020 Dec 1;10(1):3051. doi: 10.1038/s41598-020-59651-7

Author

Schmidt, David E ; de Haan, Noortje ; Sonneveld, Myrthe E et al. / IgG-Fc glycosylation before and after rituximab treatment in immune thrombocytopenia. In: Scientific reports. 2020 ; Vol. 10, No. 1.

BibTeX

@article{e63e6b9561974d5986313e555ade2e0c,
title = "IgG-Fc glycosylation before and after rituximab treatment in immune thrombocytopenia",
abstract = "The interactions of antibodies with myeloid Fcγ receptors and the complement system are regulated by an Asn297-linked glycan in the Fc portion of IgG. Alterations of serum IgG-Fc glycosylation have been reported in various autoimmune diseases, and correlate with treatment response and disease activity. We hypothesized that IgG-Fc glycosylation is altered in immune thrombocytopenia (ITP) and associates with response to anti-CD20 monoclonal antibody treatment (rituximab). IgG-Fc glycosylation was analyzed by liquid chromatography-mass spectrometry. We found that IgG-Fc glycosylation was identical between refractory ITP patients (HOVON64 trial; N = 108) and healthy controls (N = 120). Two months after rituximab treatment, we observed a shift in Fc glycosylation, with a mean 1.7% reduction in galactosylation for IgG1 and IgG4 and a mean 1.5% increase for bisection in IgG1, IgG2/3 and IgG4 (adjusted p < 1.7 × 10 −3 and p < 2 × 10 −4, respectively). Neither baseline nor longitudinal changes in IgG-Fc glycosylation after rituximab were associated with clinical treatment response. We conclude that IgG-Fc glycosylation in refractory ITP is similar to healthy controls and does not predict treatment responses to rituximab. The observed changes two months after treatment suggest that rituximab may influence total serum IgG-Fc glycosylation. Overall, our study suggests that the pathophysiology of refractory ITP may differ from other autoimmune diseases. ",
author = "Schmidt, {David E} and {de Haan}, Noortje and Sonneveld, {Myrthe E} and Leendert Porcelijn and {van der Schoot}, {C Ellen} and {de Haas}, Masja and Jaap-Jan Zwaginga and Manfred Wuhrer and Gestur Vidarsson",
note = "Funding Information: This work was supported by a research grant from the Landsteiner Foundation for Blood Transfusion Research (LSBR) and a doctoral stipend to D.E.S. by the Studienstiftung des Deutschen Volkes. Publisher Copyright: {\textcopyright} 2020, The Author(s). Copyright: Copyright 2020 Elsevier B.V., All rights reserved.",
year = "2020",
month = dec,
day = "1",
doi = "10.1038/s41598-020-59651-7",
language = "English",
volume = "10",
journal = "Scientific reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - IgG-Fc glycosylation before and after rituximab treatment in immune thrombocytopenia

AU - Schmidt, David E

AU - de Haan, Noortje

AU - Sonneveld, Myrthe E

AU - Porcelijn, Leendert

AU - van der Schoot, C Ellen

AU - de Haas, Masja

AU - Zwaginga, Jaap-Jan

AU - Wuhrer, Manfred

AU - Vidarsson, Gestur

N1 - Funding Information: This work was supported by a research grant from the Landsteiner Foundation for Blood Transfusion Research (LSBR) and a doctoral stipend to D.E.S. by the Studienstiftung des Deutschen Volkes. Publisher Copyright: © 2020, The Author(s). Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

PY - 2020/12/1

Y1 - 2020/12/1

N2 - The interactions of antibodies with myeloid Fcγ receptors and the complement system are regulated by an Asn297-linked glycan in the Fc portion of IgG. Alterations of serum IgG-Fc glycosylation have been reported in various autoimmune diseases, and correlate with treatment response and disease activity. We hypothesized that IgG-Fc glycosylation is altered in immune thrombocytopenia (ITP) and associates with response to anti-CD20 monoclonal antibody treatment (rituximab). IgG-Fc glycosylation was analyzed by liquid chromatography-mass spectrometry. We found that IgG-Fc glycosylation was identical between refractory ITP patients (HOVON64 trial; N = 108) and healthy controls (N = 120). Two months after rituximab treatment, we observed a shift in Fc glycosylation, with a mean 1.7% reduction in galactosylation for IgG1 and IgG4 and a mean 1.5% increase for bisection in IgG1, IgG2/3 and IgG4 (adjusted p < 1.7 × 10 −3 and p < 2 × 10 −4, respectively). Neither baseline nor longitudinal changes in IgG-Fc glycosylation after rituximab were associated with clinical treatment response. We conclude that IgG-Fc glycosylation in refractory ITP is similar to healthy controls and does not predict treatment responses to rituximab. The observed changes two months after treatment suggest that rituximab may influence total serum IgG-Fc glycosylation. Overall, our study suggests that the pathophysiology of refractory ITP may differ from other autoimmune diseases.

AB - The interactions of antibodies with myeloid Fcγ receptors and the complement system are regulated by an Asn297-linked glycan in the Fc portion of IgG. Alterations of serum IgG-Fc glycosylation have been reported in various autoimmune diseases, and correlate with treatment response and disease activity. We hypothesized that IgG-Fc glycosylation is altered in immune thrombocytopenia (ITP) and associates with response to anti-CD20 monoclonal antibody treatment (rituximab). IgG-Fc glycosylation was analyzed by liquid chromatography-mass spectrometry. We found that IgG-Fc glycosylation was identical between refractory ITP patients (HOVON64 trial; N = 108) and healthy controls (N = 120). Two months after rituximab treatment, we observed a shift in Fc glycosylation, with a mean 1.7% reduction in galactosylation for IgG1 and IgG4 and a mean 1.5% increase for bisection in IgG1, IgG2/3 and IgG4 (adjusted p < 1.7 × 10 −3 and p < 2 × 10 −4, respectively). Neither baseline nor longitudinal changes in IgG-Fc glycosylation after rituximab were associated with clinical treatment response. We conclude that IgG-Fc glycosylation in refractory ITP is similar to healthy controls and does not predict treatment responses to rituximab. The observed changes two months after treatment suggest that rituximab may influence total serum IgG-Fc glycosylation. Overall, our study suggests that the pathophysiology of refractory ITP may differ from other autoimmune diseases.

UR - http://www.scopus.com/inward/record.url?scp=85079770156&partnerID=8YFLogxK

U2 - 10.1038/s41598-020-59651-7

DO - 10.1038/s41598-020-59651-7

M3 - Article

C2 - 32080262

VL - 10

JO - Scientific reports

JF - Scientific reports

SN - 2045-2322

IS - 1

M1 - 3051

ER -

ID: 15809185