Henry Wellcome Building of Genomic Medicine
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.
Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10
Zhao Y. et al, (2020), Nature Communications, 11
Low-dose phase retrieval of biological specimens using cryo-electron ptychography
Zhou L. et al, (2020), Nature Communications, 11
Structural and functional analysis of protective antibodies targeting the threefold plateau of enterovirus 71.
Huang K-YA. et al, (2020), Nature communications, 11
Author Correction: Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2.
Huo J. et al, (2020), Nature structural & molecular biology
Symmetrical arrangement of positively charged residues around the 5-fold axes of SAT type foot-and-mouth disease virus enhances cell culture of field viruses.
Chitray M. et al, (2020), PLoS pathogens, 16