Why are antibodies glycosylated?
Antibody glycosylation defines the functional potential of the antibody by delineating the structure of the antibody Fc region and determining which Fc receptors it can bind to in order to recruit effector cells.
Table of Contents
Why are antibodies glycosylated?
Antibody glycosylation defines the functional potential of the antibody by delineating the structure of the antibody Fc region and determining which Fc receptors it can bind to in order to recruit effector cells.
Are immunoglobulins glycosylated?
The best studied glycoproteins in terms of the structure and function of their glycosylation are immunoglobulins (Figure 1), in particular human immunoglobulin G (IgG; Arnold et al.
What is glycosylation of IgG?
Differential IgG glycosylation is known to modulate IgG effector functions and is involved in disease development and progression, representing both a predisposition and a functional mechanism involved in disease pathology. This makes IgG glycosylation analysis a promising add-on to improve existing disease biomarkers.
Where is IgG glycosylated?
All four subclasses of human serum IgG contain a single N-glycosylation site in the constant region of their heavy chain, which is occupied by biantennary, largely core-fucosylated and partially truncated oligosaccharides, that may carry a bisecting N-acetylglucosamine and sialic acid residues.
What does N-glycosylation do?
Protein N-glycosylation is a metabolic process that has been highly conserved in evolution. In all eukaryotes, N-glycosylation is obligatory for viability. It functions by modifying appropriate asparagine residues of proteins with oligosaccharide structures, thus influencing their properties and bioactivities.
What is glycosylation where and why does it happen in eukaryotic cells?
The glycocalyx is a major characteristic of Eukaryote cells (see section “Glycosylation in cells”). It is this surface location where major interactions between cells takes place and enables communication and recognition processes to take place.
What is glycosylation of IgG antibodies?
Glycosylation is a common post-translational modification for IgG antibodies produced by mammalian cells such as Chinese hamster ovary (CHO) cells, which are frequently used for production. IgG1 molecules contain a single N-linked glycan at Asn297 in each of the two heavy chains.
How can I observe light chain glycosylation?
Light chain glycosylation can also be observed using the proprietary protocols. Due to the presence of a ‘shoulder’ on the light chain peak of some antibody samples, an alternative CGE method was utilised in an attempt to further resolve any potential glycoforms present in these samples.
Is there a shoulder on the light chain peak of antibodies?
Due to the presence of a ‘shoulder’ on the light chain peak of some antibody samples, an alternative CGE method was utilised in an attempt to further resolve any potential glycoforms present in these samples.
Does light chain glycosylation increase the risk of amyloidosis?
Together our results suggest that light chain glycosylation may be one of several modifications which may render the protein more prone to amyloid formation. Amino Acid Sequence
