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Instruments / Technical Area	Publication Details	Published	Actions
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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I24-Microfocus Macromolecular Crystallography

Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design