Viral surface glycoproteins in carbohydrate recognition: Structure and modelling

A large number of clinically important viruses utilize carbohydrate viral surface protein interactions to propagate infection and disease. The identification and structural characterization of the proteins and glycans essential in these recognition phenomena opens up new avenues for both drug discovery and vaccine development. This chapter describes some of the most significant developments in the field of structure-based investigations of viral surface-resident carbohydrate-recognizing proteins. Specifically, an overview of these carbohydrate-recognizing proteins from four important human viruses, including influenza, dengue, rotavirus, parainfluenza, and associated structural investigations will be presented. The surface of flavivirus is predominantly covered by E-glycoprotein (EGP) that forms dimers tethered to the surface by a stalk region. The EGP-associated glycan of the virus has been shown to be important for Dengue virus infection. Both human parainfluenza viruses and Newcastle disease virus have a surface-resident carbohydrate recognizing protein known as hemagglutinin-neuramindase (HN), which is involved in both cellular recognition and as a receptor-destroying enzyme. Influenza virus neuraminidase (NA) is a glycosylated homo-tetramer that is tethered to the virus surface by a long protein stalk at its C terminal.