Humoral immune responses are characterized by complex mixtures of polyclonal antibody
species varying in their isotype, target epitope specificity and affinity. Posttranslational …

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 …

INTRODUCTION Antibody function is often considered static and mostly determined by
isotype and subclass. The conserved N-linked glycan at position 297 in the Fc domain of …

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 …

Glycosylation of the immunoglobulin G (IgG)-Fc tail is required for binding to Fc-gamma
receptors (FcγRs) and complement-component C1q. A variety of IgG1-glycoforms is …

Therapeutic monoclonal antibodies are the fastest growing class of biological therapeutics
for the treatment of various cancers and inflammatory disorders. In cancer immunotherapy …

Immunoglobulin (IgG) glycosylation is a complex enzymatically controlled process, essential
for the structure and function of IgG. IgG glycome is relatively stable in the state of …

Antibody-mediated cellular cytotoxicity (ADCC), a key immune effector mechanism, relies on
the binding of antigen–antibody complexes to Fcγ receptors expressed on immune cells …

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 …

Healthy immune responses require efficient protection without excessive inflammation.
Recent discoveries on the degree of fucosylation of a human N-linked glycan at a conserved …