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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Chimeric O1K foot-and-mouth disease virus with SAT2 outer capsid as an FMD vaccine candidate Abhay Kotecha , Eva Perez-Martin , Yongjie Harvey , Fuquan Zhang , Serban L. Ilca , Elizabeth E. Fry , Ben Jackson , Francois Maree , Katherine Scott , Corey W. Hecksel , Michiel M. Harmsen , Valérie Mioulet , Britta Wood , Nick Juleff , David I. Stuart , Bryan Charleston , Julian Seago Scientific Reports 8 DOI: 10.1038/s41598-018-31856-x Open Access Show Abstract ▼ Abstract: Foot-and-mouth disease virus (FMDV) is highly contagious and infects cloven-hoofed domestic livestock leading to foot-and-mouth disease (FMD). FMD outbreaks have severe economic impact due to production losses and associated control measures. FMDV is found as seven distinct serotypes, but there are numerous subtypes within each serotype, and effective vaccines must match the subtypes circulating in the field. In addition, the O and Southern African Territories (SAT) serotypes, are relatively more thermolabile and their viral capsids readily dissociate into non-immunogenic pentameric subunits, which can compromise the effectiveness of FMD vaccines. Here we report the construction of a chimeric clone between the SAT2 and O serotypes, designed to have SAT2 antigenicity. Characterisation of the chimeric virus showed growth kinetics equal to that of the wild type SAT2 virus with better thermostability, attributable to changes in the VP4 structural protein. Sequence and structural analyses confirmed that no changes from SAT2 were present elsewhere in the capsid as a consequence of the VP4 changes. Following exposure to an elevated temperature the thermostable SAT2-O1K chimera induced higher neutralizing-antibody titres in comparison to wild type SAT2 virus.	Sep 2018
I24-Microfocus Macromolecular Crystallography	Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design Abhay Kotecha , Julian Seago , Katherine Scott , Alison Burman , Silvia Loureiro , Jingshan Ren , Claudine Porta , Helen M Ginn , Terry Jackson , Eva Perez-Martin , C Alistair Siebert , Guntram Paul , Juha T Huiskonen , Ian M Jones , Robert Esnouf , Elizabeth Fry , Francois F Maree , Bryan Charleston , Dave Stuart Nature Structural & Molecular Biology DOI: 10.1038/nsmb.3096 PMID: 26389739 Diamond Proposal Number(s): [10627] Show Abstract ▼ Abstract: Virus capsids are primed for disassembly, yet capsid integrity is key to generating a protective immune response. Foot-and-mouth disease virus (FMDV) capsids comprise identical pentameric protein subunits held together by tenuous noncovalent interactions and are often unstable. Chemically inactivated or recombinant empty capsids, which could form the basis of future vaccines, are even less stable than live virus. Here we devised a computational method to assess the relative stability of protein-protein interfaces and used it to design improved candidate vaccines for two poorly stable, but globally important, serotypes of FMDV: O and SAT2. We used a restrained molecular dynamics strategy to rank mutations predicted to strengthen the pentamer interfaces and applied the results to produce stabilized capsids. Structural analyses and stability assays confirmed the predictions, and vaccinated animals generated improved neutralizing-antibody responses to stabilized particles compared to parental viruses and wild-type capsids.	Sep 2015

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