5XS4

Structure of Coxsackievirus A6 (CVA6) virus A-particle

  • Classification: VIRUS
  • Organism(s): Coxsackievirus A6
  • Mutation(s): No 

  • Deposited: 2017-06-12 Released: 2017-09-27 
  • Deposition Author(s): Zheng, Q.B., He, M.Z., Xu, L.F., Yu, H., Li, S.W., Cheng, T.
  • Funding Organization(s): National Natural Science Foundation of China, National Science and Technology Major Projects for Major New Drugs Innovation and Development, National Science and Technology Major Project of Infectious Diseases, Natural Science Foundation of Fujian Province, National Institutes of Health

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Atomic structures of Coxsackievirus A6 and its complex with a neutralizing antibody

Xu, L.Zheng, Q.Li, S.He, M.Wu, Y.Li, Y.Zhu, R.Yu, H.Hong, Q.Jiang, J.Li, Z.Li, S.Zhao, H.Yang, L.Hou, W.Wang, W.Ye, X.Zhang, J.Baker, T.S.Cheng, T.Zhou, Z.H.Yan, X.Xia, N.

(2017) Nat Commun 8: 505-505

  • DOI: https://doi.org/10.1038/s41467-017-00477-9
  • Primary Citation of Related Structures:  
    5XS4, 5XS5, 5XS7

  • PubMed Abstract: 

    Coxsackievirus A6 (CVA6) has recently emerged as a major cause of hand, foot and mouth disease in children worldwide but no vaccine is available against CVA6 infections. Here, we demonstrate the isolation of two forms of stable CVA6 particles-procapsid and A-particle-with excellent biochemical stability and natural antigenicity to serve as vaccine candidates. Despite the presence (in A-particle) or absence (in procapsid) of capsid-RNA interactions, the two CVA6 particles have essentially identical atomic capsid structures resembling the uncoating intermediates of other enteroviruses. Our near-atomic resolution structure of CVA6 A-particle complexed with a neutralizing antibody maps an immune-dominant neutralizing epitope to the surface loops of VP1. The structure-guided cell-based inhibition studies further demonstrate that these loops could serve as excellent targets for designing anti-CVA6 vaccines.Coxsackievirus A6 (CVA6) causes hand, foot and mouth disease in children. Here the authors present the CVA6 procapsid and A-particle cryo-EM structures and identify an immune-dominant neutralizing epitope, which can be exploited for vaccine development.


  • Organizational Affiliation

    State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Public Health, Xiamen University, Xiamen, 361102, PR China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Genome polyprotein305Coxsackievirus A6Mutation(s): 0 
UniProt
Find proteins for A0A0K2BNC7 (Coxsackievirus A6)
Explore A0A0K2BNC7 
Go to UniProtKB:  A0A0K2BNC7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0K2BNC7
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Genome polyprotein256Coxsackievirus A6Mutation(s): 0 
UniProt
Find proteins for A0A0K2BNC7 (Coxsackievirus A6)
Explore A0A0K2BNC7 
Go to UniProtKB:  A0A0K2BNC7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0K2BNC7
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Genome polyprotein240Coxsackievirus A6Mutation(s): 0 
UniProt
Find proteins for A0A0K2BNC7 (Coxsackievirus A6)
Explore A0A0K2BNC7 
Go to UniProtKB:  A0A0K2BNC7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0K2BNC7
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION1.4
MODEL REFINEMENTCoot
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of ChinaChina31670933
National Natural Science Foundation of ChinaChina81401669
National Science and Technology Major Projects for Major New Drugs Innovation and DevelopmentChina2017ZX09101005-005-003
National Science and Technology Major Project of Infectious DiseasesChina2017ZX10304402-002-003
Natural Science Foundation of Fujian ProvinceChina2015J05073
National Institutes of HealthUnited StatesR37-GM33050

Revision History  (Full details and data files)

  • Version 1.0: 2017-09-27
    Type: Initial release
  • Version 1.1: 2024-03-27
    Changes: Data collection, Database references, Derived calculations