IgG subclasses and allotypes: from structure to effector functions
Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human
serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ …
serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ …
Intravenous immunoglobulin therapy: how does IgG modulate the immune system?
I Schwab, F Nimmerjahn - Nature Reviews Immunology, 2013 - nature.com
Intravenous immunoglobulin (IVIG) preparations comprise pooled IgG antibodies from the
serum of thousands of donors and were initially used as an IgG replacement therapy in …
serum of thousands of donors and were initially used as an IgG replacement therapy in …
The emerging importance of IgG Fab glycosylation in immunity
FS van de Bovenkamp, L Hafkenscheid… - The Journal of …, 2016 - journals.aai.org
Human IgG is the most abundant glycoprotein in serum and is crucial for protective
immunity. In addition to conserved IgG Fc glycans,∼ 15–25% of serum IgG contains glycans …
immunity. In addition to conserved IgG Fc glycans,∼ 15–25% of serum IgG contains glycans …
The history of IgG glycosylation and where we are now
BA Cobb - Glycobiology, 2020 - academic.oup.com
IgG glycosylation is currently at the forefront of both immunology and glycobiology, likely due
in part to the widespread and growing use of antibodies as drugs. For over four decades, it …
in part to the widespread and growing use of antibodies as drugs. For over four decades, it …
[HTML][HTML] Engineered sialylation of pathogenic antibodies in vivo attenuates autoimmune disease
JD Pagan, M Kitaoka, RM Anthony - Cell, 2018 - cell.com
Self-reactive IgGs contribute to the pathology of autoimmune diseases, including systemic
lupus erythematosus and rheumatoid arthritis. Paradoxically, IgGs are used to treat …
lupus erythematosus and rheumatoid arthritis. Paradoxically, IgGs are used to treat …
[HTML][HTML] Challenges of glycosylation analysis and control: an integrated approach to producing optimal and consistent therapeutic drugs
P Zhang, S Woen, T Wang, B Liau, S Zhao, C Chen… - Drug discovery today, 2016 - Elsevier
Highlights•Glycosylation of antibodies has a range of effects on their binding and effector
functions.•Regulatory agencies require stringent glycan analysis to ensure safety and …
functions.•Regulatory agencies require stringent glycan analysis to ensure safety and …
Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes
A Bondt, Y Rombouts, MHJ Selman… - Molecular & Cellular …, 2014 - ASBMB
The N-linked glycosylation of the constant fragment (Fc) of immunoglobulin G has been
shown to change during pathological and physiological events and to strongly influence …
shown to change during pathological and physiological events and to strongly influence …
Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity
N Washburn, I Schwab, D Ortiz… - Proceedings of the …, 2015 - National Acad Sciences
Despite the beneficial therapeutic effects of intravenous immunoglobulin (IVIg) in
inflammatory diseases, consistent therapeutic efficacy and potency remain major limitations …
inflammatory diseases, consistent therapeutic efficacy and potency remain major limitations …
Glycoengineering of antibodies for modulating functions
Antibodies are immunoglobulins that play essential roles in immune systems. All antibodies
are glycoproteins that carry at least one or more conserved N-linked oligosaccharides (N …
are glycoproteins that carry at least one or more conserved N-linked oligosaccharides (N …
Glycoproteomic analysis of antibodies
Antibody glycosylation has been shown to change with various processes. This review
presents mass spectrometric approaches for antibody glycosylation analysis at the level of …
presents mass spectrometric approaches for antibody glycosylation analysis at the level of …