4IV3

Crystal structure of recombinant foot-and-mouth-disease virus A22-H2093C empty capsid


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.235 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Rational engineering of recombinant picornavirus capsids to produce safe, protective vaccine antigen.

Porta, C.Kotecha, A.Burman, A.Jackson, T.Ren, J.Loureiro, S.Jones, I.M.Fry, E.E.Stuart, D.I.Charleston, B.

(2013) PLoS Pathog 9: e1003255-e1003255

  • DOI: https://doi.org/10.1371/journal.ppat.1003255
  • Primary Citation of Related Structures:  
    4IV1, 4IV3

  • PubMed Abstract: 

    Foot-and-mouth disease remains a major plague of livestock and outbreaks are often economically catastrophic. Current inactivated virus vaccines require expensive high containment facilities for their production and maintenance of a cold-chain for their activity. We have addressed both of these major drawbacks. Firstly we have developed methods to efficiently express recombinant empty capsids. Expression constructs aimed at lowering the levels and activity of the viral protease required for the cleavage of the capsid protein precursor were used; this enabled the synthesis of empty A-serotype capsids in eukaryotic cells at levels potentially attractive to industry using both vaccinia virus and baculovirus driven expression. Secondly we have enhanced capsid stability by incorporating a rationally designed mutation, and shown by X-ray crystallography that stabilised and wild-type empty capsids have essentially the same structure as intact virus. Cattle vaccinated with recombinant capsids showed sustained virus neutralisation titres and protection from challenge 34 weeks after immunization. This approach to vaccine antigen production has several potential advantages over current technologies by reducing production costs, eliminating the risk of infectivity and enhancing the temperature stability of the product. Similar strategies that will optimize host cell viability during expression of a foreign toxic gene and/or improve capsid stability could allow the production of safe vaccines for other pathogenic picornaviruses of humans and animals.


  • Organizational Affiliation

    The Pirbright Insitute, Pirbright, Woking, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP1211Foot-and-mouth disease virus AMutation(s): 0 
UniProt
Find proteins for Q6PN23 (Foot-and-mouth disease virus A)
Explore Q6PN23 
Go to UniProtKB:  Q6PN23
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6PN23
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP2218Foot-and-mouth disease virus AMutation(s): 1 
UniProt
Find proteins for Q6PN23 (Foot-and-mouth disease virus A)
Explore Q6PN23 
Go to UniProtKB:  Q6PN23
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6PN23
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP3221Foot-and-mouth disease virus AMutation(s): 0 
UniProt
Find proteins for Q6PN23 (Foot-and-mouth disease virus A)
Explore Q6PN23 
Go to UniProtKB:  Q6PN23
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6PN23
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP485Foot-and-mouth disease virus AMutation(s): 0 
UniProt
Find proteins for Q6PN23 (Foot-and-mouth disease virus A)
Explore Q6PN23 
Go to UniProtKB:  Q6PN23
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6PN23
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.235 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 328.02α = 90
b = 341.49β = 90
c = 363.37γ = 90
Software Package:
Software NamePurpose
GDAdata collection
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-04-17
    Type: Initial release
  • Version 1.1: 2021-06-02
    Changes: Database references, Source and taxonomy
  • Version 1.2: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description