Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure-based energetics of protein interfaces guides foot-and-mouth disease virus vaccine design.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 22, Issue 10, Page 788-794, Year 2015
Publish date	Sep 21, 2015
Authors	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 M Esnouf / Elizabeth E Fry / Francois F Maree / Bryan Charleston / David I Stuart /
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 ...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.
External links	Nat Struct Mol Biol / PubMed:26389739 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.4 - 3.5 Å
Structure data	3129 5ac9 EMDB-3129: Structure-based energetics of protein interfaces guide FMDV vaccine design PDB-5ac9: Structure-based energetics of protein interfaces guide Foot-and-Mouth disease virus vaccine design Method: EM (single particle) / Resolution: 3.2 Å 3130 5aca EMDB-3130: Structure-based energetics of protein interfaces guide FMDV vaccine design PDB-5aca: Structure-based energetics of protein interfaces guide Foot-and-Mouth disease virus vaccine design Method: EM (single particle) / Resolution: 3.5 Å PDB-5d8a: Crystal structure of recombinant foot-and-mouth-disease virus A22-H2093F empty capsid Method: X-RAY DIFFRACTION / Resolution: 2.4 Å PDB-5ddj: Crystal structure of recombinant foot-and-mouth-disease virus O1M-S2093Y empty capsid Method: X-RAY DIFFRACTION / Resolution: 3.5 Å
Chemicals	ChemComp-HOH: WATER / Water
Source	foot-and-mouth disease virus - type o foot-and-mouth disease virus - type sat 2 foot-and-mouth disease virus - type a
Keywords	VIRUS / VACCINE / FOOT AND MOUTH DISEASE VIRUS / FMDV / picornavirus / aphthovirus