5GZN

Structure of neutralizing antibody bound to Zika envelope protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.258 
  • R-Value Work: 0.223 
  • R-Value Observed: 0.224 

Starting Models: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Molecular determinants of human neutralizing antibodies isolated from a patient infected with Zika virus

Wang, Q.Yang, H.Liu, X.Dai, L.Ma, T.Qi, J.Wong, G.Peng, R.Liu, S.Li, J.Li, S.Song, J.Liu, J.He, J.Yuan, H.Xiong, Y.Liao, Y.Li, J.Yang, J.Tong, Z.Griffin, B.D.Bi, Y.Liang, M.Xu, X.Qin, C.Cheng, G.Zhang, X.Wang, P.Qiu, X.Kobinger, G.Shi, Y.Yan, J.Gao, G.F.

(2016) Sci Transl Med 8: 369ra179-369ra179

  • DOI: https://doi.org/10.1126/scitranslmed.aai8336
  • Primary Citation of Related Structures:  
    5GZN, 5GZO, 5GZR

  • PubMed Abstract: 

    The 2015-2016 outbreak of Zika virus (ZIKV) disease has affected many countries and is a major public health concern. ZIKV is associated with fetal microcephaly and neurological complications, and countermeasures are needed to treat and prevent ZIKV infection. We report the isolation of 13 specific human monoclonal antibodies from a single patient infected with ZIKV. Two of the isolated antibodies (Z23 and Z3L1) demonstrated potent ZIKV-specific neutralization in vitro without binding or neutralizing activity against strains 1 to 4 of dengue virus, the closest relative to ZIKV. These two antibodies provided postexposure protection to mice in vivo. Structural studies revealed that Z23 and Z3L1 bound to tertiary epitopes in envelope protein domain I, II, or III, indicating potential targets for ZIKV-specific therapy. Our results suggest the potential of antibody-based therapeutics and provide a structure-based rationale for the design of future ZIKV-specific vaccines.


  • Organizational Affiliation

    CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Genome polyproteinA,
D [auth B],
G [auth E],
H [auth G]
409Zika virusMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for A0A1B0XTC8 (Zika virus)
Explore A0A1B0XTC8 
Go to UniProtKB:  A0A1B0XTC8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1B0XTC8
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Antibody Heavy chainB [auth H],
E [auth C]
228Homo sapiensMutation(s): 0 
Entity Groups  
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Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Antibody light chainC [auth L],
F [auth D]
216Homo sapiensMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.258 
  • R-Value Work: 0.223 
  • R-Value Observed: 0.224 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 124.708α = 90
b = 129.385β = 90
c = 428.711γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing

Structure Validation

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Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2016-12-28
    Type: Initial release
  • Version 1.1: 2017-09-27
    Changes: Data collection
  • Version 1.2: 2023-11-08
    Changes: Data collection, Database references, Refinement description
  • Version 1.3: 2024-10-23
    Changes: Structure summary