Recombinant glycoprotein therapeutics, which include antibody-based interventions, have emerged as one of the fastest growing classes of pharmacologically active molecules. Till date, over 67% of biologics and 80% of biosimilars approved by the FDA, feature some form of glycosylation. In fact, the pipeline of such interventions is also growing at a commendable pace (CAGR of over 20%). It is important to highlight that for higher eukaryotes, such as humans, glycosylation of certain biomolecules is not only important from the functional perspective, but it also imparts beneficial pharmacological properties, which influence efficacy, solubility, stability, and antigen binding. Further, glycans represent a promising class of biomarkers that are useful for disease prognosis, diagnosis, and assist in the prediction of treatment efficacy. In this context, several tumor-associated (aberrant) glycan molecules (such as Tn, sialyl-T and sialyl-Tn), as well as virulent glycoproteins on pathogenic viral envelopes (such as the glycan shield associated with the SARS-CoV-2 spike glycoprotein), are presently being investigated as viable therapeutic targets.

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