Application Focus: Viral Glycobiology Research
Glycobiology is important in a number of ways for viral research. Viral surface proteins are often heavily glycosylated to both avoid recognition by the host cell and, in some cases, interact with host receptors. For example, the spike protein glycosylation of the SARS-CoV-2 virus is usually the extension of an N-linked core pentasaccharide compound, composed of a stem of chitobiose followed by mannoses to form two antennary complexes. Understanding glycosylation of viral spike proteins and their potential epitope masking is of fundamental importance for vaccine research.
Viral receptors recognized by many viruses are glycosylated proteins, as well. SARS-CoV-2 and others uses angiotensin-converting enzyme 2, (ACE2) as their receptor, while other ß-coronaviruses utilize sialic acid residues on cellular glycoproteins.
Glycans are currently being studied as vaccines against viruses (Dengue, Hepatitis C), parasites (Plasmodium) and fungi (Candida). Human milk oligosaccharides (HMOs) have been shown to reduce the possibility of infections through interference with adhesion of pathogenic bacteria and potentially viruses. Galectins have pro- or anti-viral properties and play an important role in innate immunity. Finally, some galectin inhibitors may block HIV infection of T cells.
Oligosaccharides are currently isolated from nature or synthesized at extremely low yield via a complex set of protection and deprotection steps. At the Midwest Bioprocessing Center we are developing new enzymatic technologies to build the key activated sugar building blocks needed to make important glycans, as well as custom oligosaccharides required to support and create additional research in this important field.