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A monoclonal antibody that recognizes the predicted tick-borne encephalitis virus E protein fusion sequence blocks
T D Volkova1, M F Vorovitch, V T Ivanov
1Shimyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, Moscow, Russia.
Archives of Virology
|July 23, 1999
Abstract:
The fusion motif of tick-borne encephalitis virus E protein has been predicted to be located within its conserved region (98-120). Results are presented to demonstrate that non-neutralizing monoclonal antibody which recognizes a synthetic peptide corresponding to residues 98-113 of the E protein sequence can block the fusion of the virus particles with artificial membranes.
Insights
A monoclonal antibody targeting the tick-borne encephalitis virus E protein
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Tick-borne encephalitis virus (TBEV) is a significant human pathogen.
- The E protein of TBEV is crucial for viral entry.
- A specific region (98-120) of the E protein is predicted to be involved in fusion.
Purpose of the Study:
- To investigate the role of the conserved region of the TBEV E protein in viral fusion.
- To determine if antibodies targeting this region can inhibit viral fusion.
Main Methods:
- Synthesis of a peptide corresponding to residues 98-113 of the TBEV E protein.
- Generation of a non-neutralizing monoclonal antibody against this peptide.
- Assay to measure the inhibition of TBEV fusion with artificial membranes.
Main Results:
- A non-neutralizing monoclonal antibody was generated that recognizes a synthetic peptide (residues 98-113) of the TBEV E protein.
- This antibody effectively blocked the fusion of TBEV particles with artificial membranes.
Conclusions:
- The conserved region (98-113) of the TBEV E protein plays a critical role in the fusion process.
- Targeting this fusion motif with antibodies can inhibit viral entry, offering potential therapeutic strategies.