The Fab region of IgG impairs the internalization pathway of FcRn upon Fc engagement

Autor: Maximilian Brinkhaus, Erwin Pannecoucke, Elvera J. van der Kooi, Arthur E. H. Bentlage, Ninotska I. L. Derksen, Julie Andries, Bianca Balbino, Magdalena Sips, Peter Ulrichts, Peter Verheesen, Hans de Haard, Theo Rispens, Savvas N. Savvides, Gestur Vidarsson

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)

Disrupting the association between the Immunoglobulin G constant fragment (Fc) and the neonatal Fc receptor (FcRn) by engineered antibodies is a promising strategy to reduce autoantibody levels in autoimmune diseases. Here authors show that the varia

Externí odkaz: https://doaj.org/article/6899a98a2d164434bf23cc999f69e473

Oxygen level is a critical regulator of human B cell differentiation and IgG class switch recombination

Autor: Jana Koers, Casper Marsman, Juulke Steuten, Simon Tol, Ninotska I. L. Derksen, Anja ten Brinke, S. Marieke van Ham, Theo Rispens

Publikováno v: Frontiers in Immunology, Vol 13 (2022)

The generation of high-affinity antibodies requires an efficient germinal center (GC) response. As differentiating B cells cycle between GC dark and light zones they encounter different oxygen pressures (pO2). However, it is essentially unknown if an

Externí odkaz: https://doaj.org/article/5c4701492b4443feb08d74297f0074cc

Variable Domain N-Linked Glycans Acquired During Antigen-Specific Immune Responses Can Contribute to Immunoglobulin G Antibody Stability

Autor: Fleur S. van de Bovenkamp, Ninotska I. L. Derksen, Mariëlle J. van Breemen, Steven W. de Taeye, Pleuni Ooijevaar-de Heer, Rogier W. Sanders, Theo Rispens

Publikováno v: Frontiers in Immunology, Vol 9 (2018)

Immunoglobulin G (IgG) can contain N-linked glycans in the variable domains, the so-called Fab glycans, in addition to the Fc glycans in the CH2 domains. These Fab glycans are acquired following introduction of N-glycosylation sites during somatic hy

Externí odkaz: https://doaj.org/article/0055da8dc52145e294c840fdd3f67479

Elevated Fab glycosylation of anti-hinge antibodies

Autor: Jana Koers, Theo Rispens, G.J. Wolbink, Michael T. Nurmohamed, Willem J.J. Falkenburg, Ninotska I. L. Derksen, P. Ooijevaar-de Heer

Publikováno v: Koers, J, Derksen, N I L, Falkenburg, W J J, Ooijevaar-de Heer, P, Nurmohamed, M T, Wolbink, G J & Rispens, T 2021, ' Elevated Fab glycosylation of anti-hinge antibodies ', Scandinavian Journal of Rheumatology . https://doi.org/10.1080/03009742.2021.1986959
Scandinavian Journal of Rheumatology. Informa Healthcare

Objective: Rheumatoid arthritis (RA) is characterized by systemic inflammation and the presence of anti-citrullinated protein antibodies (ACPAs), which contain remarkably high levels of Fab glycosylation. Anti-hinge antibodies (AHAs) recognize immuno

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5408218c6f0c7a391c2c97f9c099364
https://doi.org/10.1080/03009742.2021.1986959

Fc Galactosylation Promotes Hexamerization of Human IgG1, Leading to Enhanced Classical Complement Activation

Autor: Ninotska I. L. Derksen, Theo Rispens, C. Ellen van der Schoot, Gerard van Mierlo, Thijs L. J. van Osch, Manfred Wuhrer, Gestur Vidarsson, Jan Nouta

Publikováno v: J Immunol
Journal of Immunology, 207(6), 1545-1554. AMER ASSOC IMMUNOLOGISTS

Human IgG contains one evolutionarily conserved N-linked glycan in its Fc region at position 297. This glycan is crucial for Fc-mediated functions, including its induction of the classical complement cascade. This is induced after target recognition

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e4cc2afd8534a4fbfe4aa0fbe1eb804
https://europepmc.org/articles/PMC8428746/