Professor of Structural Biology
Viruses are attractive targets for study at the molecular level, since they are sufficiently simple that we may hope to achieve a rather complete understanding of their biology. In practice although their genomes are compact they display astonishing diversity, both in structure and function. Our attempts to relate structure to function have benefited from the developments in X-ray crystallographic methods that have brought very complex structures within reach of description in atomic detail. Our targets range from picornaviruses, small ssRNA viruses, which include a number of important animal and human pathogens, to the larger dsRNA viruses. At both ends of this spectrum (from less than 10,000,000 to about 100,000,000 Daltons) we now have representative atomic structures.
Our efforts are particularly focused on virus-receptor interactions and basic puzzles of virus assembly. Our studies here are highly collaborative, with strong links with a number of virologists (P. Mertens and B. Charleston (Pirbright), D. Rowlands (Leeds), P. Roy (London) as well as numerous groups elsewhere in Europe).
Work on cell-surface molecules is largely performed in collaboration with the group of Prof. E.Y. Jones, whose entry describes many of the projects.
We have a particular interest in studying virus evolution and many of these studies are perfoirmed in collaboration with D. Bamford in Helsinki.
Finally, we are studying a number of viral proteins and enzymes which are potential drug targets and/or illuminate how viruses modulate host responses. For example, the immune modulators of pox viruses.
A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation.
Bahar MW. et al, (2022), Commun Biol, 5
Humoral responses against SARS-CoV-2 Omicron BA.2.11, BA.2.12.1 and BA.2.13 from vaccine and BA.1 serum.
Huo J. et al, (2022), Cell discovery, 8
Production and Characterisation of Stabilised PV-3 Virus-like Particles Using Pichia pastoris.
Sherry L. et al, (2022), Viruses, 14
Alternative pathway dysregulation in tissues drives sustained complement activation and predicts outcome across the disease course in COVID-19.
Siggins MK. et al, (2022), Immunology
Nonlytic cellular release of hepatitis A virus requires dual capsid recruitment of the ESCRT-associated Bro1 domain proteins HD-PTP and ALIX.
Shirasaki T. et al, (2022), PLoS pathogens, 18