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PDBsum entry 6ieb

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protein Protein-protein interface(s) links
Structural protein/immune system PDB id
6ieb

 

 

 

 

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Contents
Protein chains
211 a.a.
207 a.a.
293 a.a.
182 a.a.
Waters ×341
PDB id:
6ieb
Name: Structural protein/immune system
Title: Structure of rvfv gn and human monoclonal antibody r15
Structure: R15 h chain. Chain: h, e. Engineered: yes. R15 l chain. Chain: l, f. Engineered: yes. Nsmgngc. Chain: b, a. Synonym: glycoprotein n,gn.
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Rift valley fever virus. Rvfv. Organism_taxid: 11588. Expressed in: insect cell expression vector ptie1. Expression_system_taxid: 266783
Resolution:
2.41Å     R-factor:   0.197     R-free:   0.246
Authors: Q.H.Wang,Y.Wu,F.Gao,J.X.Qi,G.F.Gao
Key ref: Q.Wang et al. (2019). Neutralization mechanism of human monoclonal antibodies against Rift Valley fever virus. Nat Microbiol, 4, 1231-1241. PubMed id: 30936489 DOI: 10.1038/s41564-019-0411-z
Date:
13-Sep-18     Release date:   10-Apr-19    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 211 a.a.
Protein chains
No UniProt id for this chain
Struc: 207 a.a.
Protein chains
Pfam   ArchSchema ?
P03518  (GP_RVFV) -  Envelopment polyprotein from Rift valley fever virus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1206 a.a.
293 a.a.*
Protein chain
No UniProt id for this chain
Struc: 182 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1038/s41564-019-0411-z Nat Microbiol 4:1231-1241 (2019)
PubMed id: 30936489  
 
 
Neutralization mechanism of human monoclonal antibodies against Rift Valley fever virus.
Q.Wang, T.Ma, Y.Wu, Z.Chen, H.Zeng, Z.Tong, F.Gao, J.Qi, Z.Zhao, Y.Chai, H.Yang, G.Wong, Y.Bi, L.Wu, R.Shi, M.Yang, J.Song, H.Jiang, Z.An, J.Wang, T.D.Yilma, Y.Shi, W.J.Liu, M.Liang, C.Qin, G.F.Gao, J.Yan.
 
  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.
 

 

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