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Kissel, Theresa; Ge, Changrong; Hafkenscheid, Lise; Kwekkeboom, Joanneke C; Slot, Linda M; Cavallari, Marco; He, Yibo; van Schie, Karin A; Vergroesen, Rochelle D; Kampstra, Arieke S B; Reijm, Sanne; Stoeken-Rijsbergen, Gerrie; Koeleman, Carolien; Voortman, Lennard M; Heitman, Laura H; Xu, Bingze; Pruijn, Ger J M; Wuhrer, Manfred; Rispens, Theo; Huizinga, Tom W J; Scherer, Hans Ulrich; Reth, Michael; Holmdahl, Rikard; Toes, Rene E M
Science advances, 2022-Feb-11, Letnik: 8, Številka: 6Journal Article
The hallmark autoantibodies in rheumatoid arthritis are characterized by variable domain glycans (VDGs). Their abundant occurrence results from the selective introduction of N-linked glycosylation sites during somatic hypermutation, and their presence is predictive for disease development. However, the functional consequences of VDGs on autoreactive B cells remain elusive. Combining crystallography, glycobiology, and functional B cell assays allowed us to dissect key characteristics of VDGs on human B cell biology. Crystal structures showed that VDGs are positioned in the vicinity of the antigen-binding pocket, and dynamic modeling combined with binding assays elucidated their impact on binding. We found that VDG-expressing B cell receptors stay longer on the B cell surface and that VDGs enhance B cell activation. These results provide a rationale on how the acquisition of VDGs might contribute to the breach of tolerance of autoreactive B cells in a major human autoimmune disease.
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in: SICRIS
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