When the COVID-19 pandemic hit, Valeria reoriented her whole research and HDX-MS expertise to the study of the SARS-CoV-2 spike glycoprotein, based on the intuition that cryo-EM structure alone could not fully explain the mechanisms of emergence of new variants and decipher the many conformational states sampled by the viral glycoproteins in solution. In other words, what makes a variant more infectious than another one? How do glycoproteins bind to host receptors and trigger membrane fusion? Which strategies the viral glycoproteins adopt to escape antibodies? This is where Valeria’s research interests lie within Struwe group. By using the dynamics information provided by HDX-MS, we can learn a great deal on viral structures and on the functional roles of their glycans, speeding up the research of vaccines and therapeutics.
Valeria earned a Master degree in Pharmaceutical Chemistry in Sapienza, University of Rome, where she initially approached mass spectrometry with the analysis of small molecules and peptides. She won a national competition for Italian graduated students in STEM, which allowed her to spend a research period abroad. She worked at the Institut Pasteur in Paris, where she gained experience in bottom-up and top-down proteomics and PTM profiling. She then got fascinated by structural mass spectrometry and undertook a Marie Skłodowska-Curie PhD fellowship between the University of Copenhagen and GSK vaccines in Italy, developing hydrogen-deuterium exchange mass spectrometry (HDX-MS) methods for the analysis of vaccine antigens and membrane proteins in native state. After her PhD, Valeria worked as a postdoctoral researcher at the Chemistry department of King’s College London, and, in collaboration with the Crick Institute, focused on the study of the dynamics of viral structures and their assemblies by HDX-MS, besides being involved in a variety of HDX-MS projects, including the analysis of intrinsically disordered and membrane proteins. Since February 2023, Valeria joined the Struwe group where she will continue developing HDX-MS methods applied to viral glycoproteins and integrate dynamics information with glycoproteomics and mass photometry data, with the aim to get a complete picture of how these proteins modulate their conformational states during the virus lifecycle and infectious process.
