Unveiling the structural dynamics of virus fusion glycoproteins by hydrogen-deuterium mass spectrometry

DRA lecture held by Lecturer Valeria Calvaresi, University of Oxford, UK

Hydrogen-deuterium exchange mass spectrometry unveils the structural dynamics of virus fusion glycoproteins underlying entry mechanisms and evolution of SARS-CoV-2 and Ebola virus.  

Enveloped viruses present on their surface specific protein machineries, aka fusion glycoproteins, which mediates virus entry into host cells and are the main target of the immune system. During the virus life cycle, fusion glycoproteins can adopt different conformations that underpin virus-host interactions at the different stages of entry and can as well facilitate immune escape. Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is particularly suitable to map protein structural and conformational changes at high resolution along protein sequences, therefore represents a powerful technique to uncover the mechanisms of virus-host interactions. The speaker will present how she utilized HDX-MS combined to a novel orthogonal technique -mass photometry- to understand the molecular mechanisms of SARS-CoV-2 and Ebola virus entry, from enzymatic processing, receptor binding to fusion priming, as well how those two viruses have evolved the conformational features of their fusion glycoproteins giving rise to the emergence of new more infectious variants, over the course of pandemic/epidemics.

The lecture is organized on behalf of the graduate programme in pharmaceutical sciences, Drug Research Academy, by Professor Kasper D. Rand, Department of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen.

The DRA lecture is free of charge and open for attendance by all interested parties. It is not necessary to pre-register.