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Yellow fever virus envelope protein has two discrete type-specific neutralizing epitopes
K D Ryman1, T N Ledger, R C Weir
1Center for Tropical Diseases, University of Texas Medical Branch, Galveston 77555, USA.
The Journal of General Virology
|June 1, 1997
Summary
Researchers identified two yellow fever virus (YFV) variants resistant to specific monoclonal antibodies (MAbs). These findings pinpoint YFV type-specific epitopes on the E protein, crucial for vaccine development.
Area of Science:
- Virology
- Immunology
- Vaccinology
Background:
- Yellow fever virus (YFV) 17D-204 is a live-attenuated vaccine.
- Monoclonal antibodies (MAbs) are critical tools for studying virus neutralization.
- Understanding YFV epitopes is essential for vaccine improvement and antiviral strategies.
Purpose of the Study:
- To characterize novel YFV 17D-204 variants resistant to YFV type-specific MAbs.
- To map the locations of YFV type-specific neutralizing epitopes on the YFV envelope (E) protein.
Main Methods:
- Selection and characterization of MAb-neutralization-resistant (MAbR) YFV variants.
- Neutralization assays using a panel of YFV type-specific MAbs.
- Amino acid sequencing to identify mutations in MAbR variants.
Main Results:
- Two YFV 17D-204 variants (B39R) resistant to MAb B39 were generated.
- These variants possessed single amino acid substitutions at positions E-155 or E-158.
- A previously identified epitope mapped to positions E-71/72 (domain II) by MAb 2E10.
- The B39 epitope was localized to domain I of the E protein, representing a novel flavivirus epitope.
Conclusions:
- YFV type-specific neutralizing epitopes are located in distinct regions of the E protein, specifically domain I and domain II.
- The identification of a YFV epitope in domain I provides new insights into flavivirus antigenicity.
- These findings contribute to a deeper understanding of YFV-MAb interactions and have implications for vaccine design.