5D8A
Crystal structure of recombinant foot-and-mouth-disease virus A22-H2093F empty capsid
Summary for 5D8A
| Entry DOI | 10.2210/pdb5d8a/pdb |
| Related | 4IV1 4IV3 |
| Descriptor | VP1, VP2, VP3, ... (5 entities in total) |
| Functional Keywords | foot and mouth disease virus, virus, picornavirus, vaccine, aphthovirus |
| Biological source | Foot-and-mouth disease virus - type A More |
| Total number of polymer chains | 4 |
| Total formula weight | 80760.26 |
| Authors | Kotecha, A.,Seago, J.,Scott, K.,Burman, A.,Loureiro, S.,Ren, J.,Porta, C.,Ginn, H.M.,Jackson, T.,Perez-Martin, E.,Siebert, C.A.,Paul, G.,Huiskonen, J.T.,Jones, I.M.,Esnouf, R.M.,Fry, E.E.,Maree, F.F.,Charleston, B.,Stuart, D.I. (deposition date: 2015-08-16, release date: 2015-09-23, Last modification date: 2024-01-10) |
| Primary citation | Kotecha, A.,Seago, J.,Scott, K.,Burman, A.,Loureiro, S.,Ren, J.,Porta, C.,Ginn, H.M.,Jackson, T.,Perez-Martin, E.,Siebert, C.A.,Paul, G.,Huiskonen, J.T.,Jones, I.M.,Esnouf, R.M.,Fry, E.E.,Maree, F.F.,Charleston, B.,Stuart, D.I. Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design. Nat.Struct.Mol.Biol., 22:788-794, 2015 Cited by PubMed 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. PubMed: 26389739DOI: 10.1038/nsmb.3096 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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