Structure-based approaches to mapping immunologically dominant epitopes on human enteric virus capsids.

Dr David J Allen (primary)
Department of Infection Biology
London School of Hygiene and Tropical Medicine
Dr Renos Savva (secondary)
Rosalind Franklin Molecular Biology Laboratory / Department of Biological Sciences
Birkbeck, University of London


Enteric viruses are major causes of morbidity worldwide, associated with diseases including gastroenteritis, hepatitis and meningitis. For most, there are no specific therapeutics or vaccines, leaving the population susceptible to (re)infection throughout life, and risk-groups (children, pregnant women, immunocompromised individuals) may have prolonged or more severe disease.

Analysis of virus genomic data has identified putative epitopes important in virus-host interactions and predicted to drive the dynamic epidemiology of these viruses. However, precise characterisation of these sites is lacking. This project will interrogate surface-exposed sites predicted to be immunologically dominant epitopes using structural biology and in vitro assay-based approaches.


1 Carmona-Vicente, N., Vila-Vicent, S., Allen, D.J., Gozalbo-Rovira, R., Iturriza-Gómara, M., Buesa, J., & Rodríguez-Díaz, J. (2016). Characterization of a Novel Conformational GII.4 Norovirus Epitope: Implications for Norovirus-Host Interactions.. Journal of virology, 90(17), 7703-14. doi:10.1128/JVI.01023-16
2 Carmona-Vicente, N., Allen, D. J., Rodríguez-Díaz, J., Iturriza-Gómara, M., & Buesa, J. (2016). Antibodies against Lewis antigens inhibit the binding of human norovirus GII.4 virus-like particles to saliva but not to intestinal Caco-2 cells.. Virology journal, 13, 82. doi:10.1186/s12985-016-0538-y
3 Allen, D. J., Noad, R., Samuel, D., Gray, J. J., Roy, P., & Iturriza-Gómara, M. (2009). Characterisation of a GII-4 norovirus variant-specific surface-exposed site involved in antibody binding. Virology journal, 6, 150. doi:10.1186/1743-422X-6-150
4 Earl, C., Bagnéris, C., Zeman, K., Cole, A., Barrett, T., & Savva, R. (2018). A structurally conserved motif in γ-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping. Nucleic Acids Research, 46(8), 4286–4300. doi:10.1093/nar/gky217
5 Villanueva, H., Sattar, S., Javed, A., Vasciaveo, S., Pinheiro, V., Savva, R., & Orlova, E. (manuscript in preparation). Multidisciplinary structural analysis of diverse picovirinae portal proteins enables applied particle engineering.

Genes, development and STEM* approaches to biology
Area of Biology
MicrobiologyStructural Biology
Techniques & Approaches
BiochemistryBioinformaticsBiophysicsMicroscopy / ElectrophysiologyMolecular Biology