H. Rosina Plomp
A5041478436- Monoclonal and Polyclonal Antibodies Research
- Glycosylation and Glycoproteins Research
- Blood groups and transfusion
- Galectins and Cancer Biology
- SARS-CoV-2 and COVID-19 Research
- Immunodeficiency and Autoimmune Disorders
Netherlands Metabolomics Centre
2018-2020
Leiden University Medical Center
2018-2020
Immunoglobulin G (IgG) antibodies are crucial for protection against invading pathogens. A highly conserved N-linked glycan within the IgG-Fc tail, which is essential IgG function, shows variable composition in humans. Afucosylated variants already used anticancer therapeutic their increased activity through Fc receptors (FcγRIIIa). Here, we report that afucosylated (approximately 6% of total humans) specifically formed enveloped viruses but generally not other antigens. This mediates...
Abstract The precise mechanisms underlying anti-inflammatory effects of intravenous immunoglobulin (IVIg) therapies remain elusive. sialylated IgG fraction within IVIg has been shown to be therapeutically more active in mouse models. Functionally, it suggested that undergoes conformational changes upon Fc-sialylation which sterically impede binding conventional FcγRs, but simultaneously allow human DC-SIGN (SIGN-R1 mice) and also CD23. These latter C-type lectins have proposed responsible...
After albumin, immunoglobulin G (IgG) are the most abundant proteins in human serum, with IgG1 and IgG3 being subclasses directed against protein antigens. The quality of IgG-Fc-glycosylation has important functional consequences, which have been found to be skewed towards low fucosylation some antigen-specific immune responses. This increases affinity IgG1-Fc-receptor (FcγR)IIIa/b thereby directly affects downstream effector functions disease severity. To date, IgG-glycosylation not...
Abstract IgG antibodies are crucial for protection against invading pathogens. A highly conserved N-linked glycan within the IgG-Fc-tail, essential function, shows variable composition in humans. Afucosylated variants already used anti-cancer therapeutic their elevated binding and killing activity through Fc receptors (FcγRIIIa). Here, we report that afucosylated which of minor abundance humans (∼6% total IgG) specifically formed surface epitopes enveloped viruses after natural infections or...