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 …

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 …

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 …

While a third of the world carries the burden of tuberculosis, disease control has been
hindered by a lack of tools, including a rapid, point-of-care diagnostic and a protective …

Antiviral activities of antibodies may either be dependent only on interactions between the
antibody and cognate antigen, as in binding and neutralization of an infectious virion, or …

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 …

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 …

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 …

Monoclonal antibodies are being developed as therapeutics to complement drugs and
vaccines or to fill the gap where no drugs or vaccines exist. These therapeutic antibodies …

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 …