Glycosylation is the most abundant and diverse form of post-translational modification of
proteins that is common to all eukaryotic cells. Enzymatic glycosylation of proteins involves a …

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

Glycans, carbohydrate molecules in the realm of biology, are present as biomedically
important glycoconjugates and a characteristic aspect is that their structures in many …

Simple and complex carbohydrates (glycans) have long been known to play major
metabolic, structural and physical roles in biological systems. Targeted microbial binding to …

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 …

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 …

Complement is an ancient danger-sensing system that contributes to host defense, immune
surveillance and homeostasis. C5a and its G protein–coupled receptor mediate many of the …

IgG molecules exert both pro-and antiinflammatory effector functions based on the
composition of the fragment crystallizable (Fc) domain glycan. Sialylated IgG Fc domains …

Glycosylation is crucial in cellular metabolism and survival. Of interest is the role of N-linked
and O-linked glycans in disease states. Robust analytical methods must be defined to …

The fine structures of Fc N-glycans can modulate the effector functions of IgG antibodies. It
has been demonstrated that lack of the core fucose on the Fc N-glycans leads to drastic …