Probing Viral Receptor-Glycan Interactions using Polyvalent Multifunctional Glycan-Nanoparticle

Multivalent viral receptor-glycan interactions are central to viral infection and immune response regulation. However, the underpinning structural mechanisms are often poorly understood, due to a lack of effective probes for such complex, multimeric and flexible proteins. Herein we will develop polyvalent glycan-nanoparticles (NPs) with tuneable glycan valency and flexibility as novel structural probes for two closely related, almost identical tetrameric receptors, DC-SIGN/R, which bind to the HIV/Ebola virus surface sugars to enhance viral infection.[1]

However, how their four carbohydrate-recognition-domains (CRDs) are spatially arranged remain unclear. This information is key to their specific binding to viral surface glycans and viral trans-infection. We hypothesis that a perfect spatial match between the NP surface multiple glycans and protein binding sites will result in high affinity multivalent binding, allowing us to derive the CRD arrangement.[2]

Further information about this project and how to apply can be found on our website.