Research interests
The spike proteins of many enveloped viruses are key targets for vaccine design due to their susceptibility to neutralising antibodies during natural infection. Enveloped viruses undergo post-translational modification by the host’s N-linked glycosylation pathway in an act to evade the immune system. By decorating viral spike proteins with host-derived N-linked glycans, a shielding effect may arise to hide the underlying antigenic protein surface from neutralising antibodies. As glycan processing is heterogeneous, specific workflows are required to fully characterize the glycosylation of viral envelopes, which form a portion of the antigenic surface of the virus. Using a combination of biophysical techniques, with a focus on mass spectrometry, I aim to determine the glycosylation of viral glycoproteins at the site-specific level for a number of viruses, including HIV-1, SARS-CoV-2, Ebola and Hepatitis C virus. Discovering shared mechanisms by which viral spike proteins are glycosylated will inform the vaccine design process and additionally help to understand the role of viral spike glycosylation in disease pathogenesis.
PhD Supervision
Professor Max Crispin, Professor Bill Keevil
Memberships
Member of the British Pharmacological Society
Research group
Molecular and Cellular Biosciences
Affiliate research group
Institute for Life Sciences (IfLS)