Structural Insights into Glycan Interactions of Human Pathogens

Abstract

Glycans are major components of every cell surface. In addition to their importance in many physiological processes, glycans play a key role during infection of many pathogens. The identification and characterisation of glycan-pathogen interactions at a molecular and atomic level is therefore a crucial step towards the design of novel antimicrobial drugs and vaccines. Protein functions related to glycan interactions include glycan biosynthesis (glycosyltransferases), glycan recognition (lectins) and glycan degradation (glycosylhydrolases). This thesis investigates structure-function relationships of four glycan binding proteins that are important for the infectivity of three major human pathogens: the polysialyltransferase (polyST) of Neisseria meningitidis serogroup B (NmB), the viral protein 8* (VP8*) of rotavirus, and the hemagglutinin (HA) and the neuraminidase (NA) of influenza A virus (IAV).