Glycosylation is the only post-translational modification that can produce significant structural changes to proteins. While genes unequivocally encode the sequence of amino acids, there is no genetic template for the glycan part. Instead of being defined by a single gene, glycans are encoded in a complex dynamic network of hundreds of genes which code for enzymes involved in the synthesis of glycans. Glycosylation of IgG has important regulatory functions. New high-throughput technologies, allow us to quantitate N-linked glycans from individual human plasma proteins.
We recently started a small pilot study to analyse the composition of the IgG glycome to examine the effects of age (and the prolonged influence of environmental factors) on IgG glycosylation.