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[Protein E 98-113 sequence is a fusion site of tick-borne encephalitis virus with cellular membrane]
T D Volkova1, O M Vol'pina, V T Ivanov
1Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia. fmdv@ibch.siobc.ras.ru
Abstract:
The synthetic peptide with the conservative 98-113 sequence of protein E of tick-borne encephalitis virus was studied in order to elucidate its role in the functioning of flaviviruses. The peptide was shown to inhibit the in vitro infection of macrophages with the virus. An antibody that specifically binds this peptide was found among the set of monoclonal antibodies produced against protein E. This antibody was found to prevent penetration of the virus into liposomes. A correlation was found between our results and data on the spatial structure of protein E and its interspecies homology. The protein E 98-113 sequence of the tick-borne encephalitis virus was found to be the fusion site of the viral envelope with a cellular membrane.
Insights
A synthetic peptide from tick-borne encephalitis virus protein E inhibits viral infection of macrophages. This peptide, located at the fusion site, is crucial for viral entry into host cells.
Area of Science:
- Virology
- Molecular Biology
- Immunology
Context:
- Tick-borne encephalitis virus (TBEV) is a significant human pathogen.
- Protein E is a key component of the flavivirus envelope.
- The function of conserved protein sequences in flavivirus infection is not fully understood.
Purpose:
- To investigate the role of the conserved 98-113 sequence of TBEV protein E in flavivirus functioning.
- To identify potential targets for antiviral therapies.
Summary:
- A synthetic peptide corresponding to the 98-113 sequence of TBEV protein E was synthesized and studied.
- This peptide demonstrated inhibition of in vitro macrophage infection by TBEV.
- An antibody targeting this peptide blocked viral entry into liposomes, suggesting its role in membrane fusion.
- The 98-113 sequence is identified as the fusion site for viral envelope and cellular membrane interaction.
Impact:
- Identifies a critical fusion site within TBEV protein E.
- Provides a potential target for developing novel antiviral strategies against TBEV and other flaviviruses.
- Enhances understanding of flavivirus-host cell interactions at the molecular level.