Dr Weston Struwe
Stipendiary Lecturer in Biochemistry &
UKRI Future Leaders Fellow, Department of Chemistry
B.S. (University of Wisconsin - Madison)
Ph.D. (University of New Hampshire)
Academic Background and Previous Positions
I have recently returned to the Department of Chemistry as a UKRI Future Leaders Fellow and Principle Investigator, following two years as Chief Scientific Officer of Refeyn, a University of Oxford spin-out I helped establish. Previously, I was a Senior Research Associate in the Department of Chemistry (2017-2018) and Biochemistry (2015-2017). Prior to coming to Oxford, I was a Post-Doctoral Research Fellow at the newly formed non-profit research institute, NIBRT, based in Ireland that was established with the unique mission to support research and education in biopharma globally
Undergraduate Teaching Areas
Cellular & Molecular Biochemistry
The majority of mammalian proteins are modified by complex oligosaccharides, or glycans, that fine-tune their function, localisation, structural dynamics as well as biophysical properties governing molecular interactions. My research interests centre on understanding the role of glycosylation in protein structure and regulation, particularly in the context of viral infection and immune recognition.
Fusion proteins on the surface of enveloped viruses, frequently referred to as spikes, are also glycosylated and glycans help viruses evade immune detection. This is because they are derived from the infected host cell’s machinery and therefore appear to be immunologically self. However, these so-called “glycan shields” are vulnerable and are commonly a key feature in detection by neutralising antibodies and innate immune lectins.
Our work aims to understand the mechanisms by which viruses glycosylate their proteins, identify molecular similarity among structure-based vaccines and explore how changes in glycosylation modulate immune detection and signalling among the most pressing threats, including Ebola, influenza, HIV and coronaviruses. Our approach is based on advanced methods in mass spectrometry and mass photometry as well as developing tools in chemical biology and glycoprotein engineering that allow us to unravel complex structure-function relationships in viral infection and vaccine design.
Assessing Antigen Structural Integrity through Glycosylation Analysis of the SARS-CoV-2 Viral Spike. Brun J, Vasiljevic S, Gangadharan B, Hensen M, Chandran A, Hill M, Kiappes J, Dwek R, Alonzi D, Struwe W, Zitzmann N. ACS Central Science. 2021
Native Mass Spectrometry meets Glycomics – Resolving Structural Detail and Occupancy of Glycans on Intact Glycoproteins. Chen S, Wu D, Robinson C, Struwe W. Analytical Chemistry. 2021
Quantifying Protein-Protein Interactions by Molecular Counting with Mass Photometry. Soltermann F, Foley E, Pagnoni V, Galpin M, Benesch J, Kukura P, Struwe W. Angewandte Chemie. 2020
Site-Specific Glycosylation of Virion-derived HIV-1 gp120 is Mimicked by a Soluble Trimeric Immunogen. Struwe W, Chertova E, Allen J, Seabright G, Watanabe Y, Harvey D, Medina-Ramirez M, Roser J, Smith R, Westcott D, Keele B, Bess J, Sanders R, Lifson J, Moore J, Crispin M. Cell Reports. 2018
Quantitative Mass Imaging of Single Biological Macromolecules. Young G, Hundt N, Cole D, Fineberg A, Andrecka J, Tyler A, Olerinyova A, Ansari A, Marklund E, Collier M, Chandler S, Tkachenko O, Allen J, Crispin M, Billington N, Takagi Y, Sellers J, Eichmann C, Selenko P, Frey L, Riek R, Galpin M, Struwe W, Benesch J, Kukura P. Science. 2018
Global N-glycan Site Occupancy of HIV-1 gp120 by Metabolic Engineering and High-Resolution Intact Mass Spectrometry. Struwe W, Stuckmann A, Behrens A, Pagel K, Crispin M. ACS Chemical Biology. 2017
The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans. Hopper J, Grant O, Ambrose S, Krumm S, Allison T, Tully M, Prichard L, Ozorowski G, Ward A, Crispin M, Doores K, Woods R, Benesch J, Robinson C, Struwe W. Structure. 2017
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