6IEB

Structure of RVFV Gn and human monoclonal antibody R15


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.41 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Neutralization mechanism of human monoclonal antibodies against Rift Valley fever virus.

Wang, Q.Ma, T.Wu, Y.Chen, Z.Zeng, H.Tong, Z.Gao, F.Qi, J.Zhao, Z.Chai, Y.Yang, H.Wong, G.Bi, Y.Wu, L.Shi, R.Yang, M.Song, J.Jiang, H.An, Z.Wang, J.Yilma, T.D.Shi, Y.Liu, W.J.Liang, M.Qin, C.Gao, G.F.Yan, J.

(2019) Nat Microbiol 4: 1231-1241

  • DOI: https://doi.org/10.1038/s41564-019-0411-z
  • Primary Citation of Related Structures:  
    6IEA, 6IEB, 6IEC, 6IEK

  • PubMed Abstract: 

    Rift Valley fever virus (RVFV) is a mosquito-borne pathogen that causes substantial morbidity and mortality in livestock and humans. To date, there are no licensed human vaccines or therapeutics available. Here, we report the isolation of monoclonal antibodies from a convalescent patient, targeting the RVFV envelope proteins Gn and Gc. The Gn-specific monoclonal antibodies exhibited much higher neutralizing activities in vitro and protection efficacies in mice against RVFV infection, compared to the Gc-specific monoclonal antibodies. The Gn monoclonal antibodies were found to interfere with soluble Gn binding to cells and prevent infection by blocking the attachment of virions to host cells. Structural analysis of Gn complexed with four Gn-specific monoclonal antibodies resulted in the definition of three antigenic patches (A, B and C) on Gn domain I. Both patches A and B are major neutralizing epitopes. Our results highlight the potential of antibody-based therapeutics and provide a structure-based rationale for designing vaccines against RVFV.


  • Organizational Affiliation

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


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
R15 H chainA [auth H],
E
218Homo sapiensMutation(s): 0 
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
R15 L chainB [auth L],
F
207Homo sapiensMutation(s): 0 
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
NSmGnGcC [auth B],
D [auth A]
316Rift Valley fever virusMutation(s): 0 
UniProt
Find proteins for P03518 (Rift valley fever virus)
Explore P03518 
Go to UniProtKB:  P03518
Entity Groups  
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UniProt GroupP03518
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.41 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.002α = 85.09
b = 70.521β = 84.71
c = 99.33γ = 70.7
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of ChinaChina31390432

Revision History  (Full details and data files)

  • Version 1.0: 2019-04-10
    Type: Initial release
  • Version 1.1: 2019-07-10
    Changes: Data collection, Database references