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.
An Observational Cohort Study on the Incidence of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Infection and B.1.1.7 Variant Infection in Healthcare Workers by Antibody and Vaccination Status
Lumley SF. et al, (2022), Clinical Infectious Diseases, 74, 1208 - 1219
Antibody responses and correlates of protection in the general population after two doses of the ChAdOx1 or BNT162b2 vaccines
Wei J. et al, (2022), Nature Medicine
SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
Dejnirattisai W. et al, (2022), Cell, 185, 467 - 484.e15
Purification of African Swine Fever Virus.
Shimmon GL. et al, (2022), Methods in molecular biology (Clifton, N.J.), 2503, 179 - 186
Structures and therapeutic potential of anti-RBD human monoclonal antibodies against SARS-CoV-2
Huang K-YA. et al, (2022), THERANOSTICS, 12, 1 - 17