Intravenous immunoglobulin (IVIg) products from different pharmaceutical companies vary in composition, in part because of the selected blood donors and production process. N-glycosylation of the Fc-portion of IgG varies between blood donors and may influence both the side-effects and therapeutic effectiveness of IVIg. At present, the variation in Fc N-glycosylation between IVIg products has not been defined. Utilizing mass spectrometry, we performed relative quantitation of the Fc N-glycosylation of IgG, assessing a total of 154 unique lot numbers of IVIg. Seven products showed comparable Fc N-glycosylation, with only one product differing from the others in all glycosylation features (galactosylation, sialylation, fucosylation and bisecting N-acetylglucosamine). However, the mean difference did not exceed 3%. Within product variation was present to a minor degree, but largely indistinguishable from analytical variation. In conclusion, we expect that the minor variation in Fc N-glycosylation between IVIg products has a small effect, if any, on the biological activity.

dx.doi.org/10.1371/journal.pone.0139828, hdl.handle.net/1765/89207
PLoS ONE
Department of Immunology

Fokkink, W.-J.R, Falck, D, Santbergen, T.C.M, Huizinga, R, Wuhrer, M, & Jacobs, B.C. (2015). Comparison of Fc N-Glycosylation of pharmaceutical products of intravenous immunoglobulin G. PLoS ONE, 10(10). doi:10.1371/journal.pone.0139828