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 and Fc-fusion antibody-like proteins have become successful biologics
developed for cancer treatment, passive immunity against infection, addiction, and …

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 …

The majority of monoclonal antibody (mAb) therapeutics possess the ability to engage
innate immune effectors through interactions mediated by their fragment crystallizable (Fc) …

Herein we will review the role of glycans in the immune system. Specific topics covered
include: the glycosylation sites of IgE, IgM, IgD, IgE, IgA, and IgG; how glycans can encode …

Monoclonal antibody and Fc fusion protein drugs are complex heterogeneous mixtures of
numerous different protein variants and modifications. N-glycosylation as one of the most …

The antibody Fc region regulates antibody cytotoxic activities and serum half-life. In a
therapeutic context, however, the cytotoxic effector function of an antibody is often not …

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 …

Despite the worldwide success of vaccination, newborns remain vulnerable to infections.
While neonatal vaccination has been hampered by maternal antibody-mediated dampening …

IgG antibodies are secreted from B cells and bind to a variety of pathogens to control
infections as well as contribute to inflammatory diseases. Many of the functions of IgGs are …