4RR3

Crystal structure of a recombinant EV71 virus particle


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.236 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structures of enterovirus 71 (EV71) recombinant virus particles provide insights into vaccine design.

Lyu, K.Wang, G.C.He, Y.L.Han, J.F.Ye, Q.Qin, C.F.Chen, R.

(2015) J Biol Chem 290: 3198-3208

  • DOI: https://doi.org/10.1074/jbc.M114.624536
  • Primary Citation of Related Structures:  
    4RQP, 4RR3, 4RS5

  • PubMed Abstract: 

    Hand-foot-and-mouth disease (HFMD) remains a major health concern in the Asia-Pacific regions, and its major causative agents include human enterovirus 71 (EV71) and coxsackievirus A16. A desirable vaccine against HFMD would be multivalent and able to elicit protective responses against multiple HFMD causative agents. Previously, we have demonstrated that a thermostable recombinant EV71 vaccine candidate can be produced by the insertion of a foreign peptide into the BC loop of VP1 without affecting viral replication. Here we present crystal structures of two different naturally occurring empty particles, one from a clinical C4 strain EV71 and the other from its recombinant virus containing an insertion in the VP1 BC loop. Crystal structure analysis demonstrated that the inserted foreign peptide is well exposed on the particle surface without significant structural changes in the capsid. Importantly, such insertions do not seem to affect the virus uncoating process as illustrated by the conformational similarity between an uncoating intermediate of another recombinant virus and that of EV71. Especially, at least 18 residues from the N terminus of VP1 are transiently externalized. Altogether, our study provides insights into vaccine development against HFMD.


  • Organizational Affiliation

    From the Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai 200031, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP1A [auth E],
D [auth Q],
E [auth I],
F [auth M],
G [auth A]
303Enterovirus A71Mutation(s): 0 
UniProt
Find proteins for F6KTB0 (Human enterovirus 71)
Explore F6KTB0 
Go to UniProtKB:  F6KTB0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupF6KTB0
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP3B [auth F],
H [auth R],
I [auth J],
J [auth N],
K [auth B]
242Enterovirus A71Mutation(s): 1 
UniProt
Find proteins for F6KTB0 (Human enterovirus 71)
Explore F6KTB0 
Go to UniProtKB:  F6KTB0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupF6KTB0
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP0C [auth G],
L [auth S],
M [auth K],
N [auth O],
O [auth C]
323Enterovirus A71Mutation(s): 0 
UniProt
Find proteins for F6KTB0 (Human enterovirus 71)
Explore F6KTB0 
Go to UniProtKB:  F6KTB0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupF6KTB0
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.236 
  • Space Group: P 42 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 350.599α = 90
b = 350.599β = 90
c = 350.599γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHENIXmodel building
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-12-17
    Type: Initial release
  • Version 1.1: 2015-04-15
    Changes: Database references
  • Version 1.2: 2024-02-28
    Changes: Data collection, Database references