Abstract The Immunoglobulin G (IgG) glycome is well known for its heterogeneity and shows
a significant degree of variation within populations. IgG glycome composition is influenced …

Antibodies produced in response to a foreign antigen are characterized by polyclonality, not
only in the diverse epitopes to which their variable domains bind but also in the various …

Although elevated levels of anti-citrullinated protein antibodies (ACPAs) are a hallmark of
rheumatoid arthritis (RA), the in vivo functions of these antibodies remain unclear. Here, we …

Immunoglobulins are heterodimeric proteins composed of 2 heavy and 2 light chains. They
can be separated functionally into variable domains that bind antigens and constant …

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 …

Fine structural details of glycans attached to the conserved N-glycosylation site significantly
not only affect function of individual immunoglobulin G (IgG) molecules but also mediate …

Glycosylation of immunoglobulin G (IgG) influences IgG effector function by modulating
binding to Fc receptors. To identify genetic loci associated with IgG glycosylation, we …

Self-reactive IgGs contribute to the pathology of autoimmune diseases, including systemic
lupus erythematosus and rheumatoid arthritis. Paradoxically, IgGs are used to treat …

Glycosylation of the Fc region of IgG has a profound impact on the safety and clinical efficacy
of therapeutic antibodies. While the biantennary complex-type oligosaccharide attached to …

Background The majority of human proteins are being modified by covalent attachment of
complex oligosaccharides—glycans. Both glycans and polypeptide parts of a protein …