Related Experiment Video
Updated: Sep 18, 2025
05:15
Detection of Neutralization-sensitive Epitopes in Antigens Displayed on Virus-Like Particle VLP-Based Vaccines Using a Capture Assay
Published on: February 10, 2022
3.7K
Antibody Binding and Neutralizing Targets within the Predicted Structure of the Poxvirus Multiprotein Entry-Fusion
Huibin Yu1, Wolfgang Resch2, Catherine A Cotter1
1Laboratory of Viral Diseases, NIAID, NIH, Bethesda MD, USA.
Biorxiv : the Preprint Server for Biology
|June 26, 2025
Summary
New research identifies key viral targets for improved mpox vaccines. Antibodies against two specific proteins, A16 and G9, neutralize orthopoxviruses and protect against lethal vaccinia virus infection.
Area of Science:
- Virology
- Immunology
- Vaccine Development
Background:
- The rising incidence of mpox necessitates novel vaccine strategies.
- Poxviruses utilize a conserved but understudied 11-protein entry-fusion complex (EFC) with potential antigenic targets.
Purpose of the Study:
- To identify and characterize neutralizing antibody targets within the poxvirus EFC.
- To evaluate the immunogenic and protective potential of novel EFC targets.
Main Methods:
- Antibody induction and neutralization assays against EFC proteins.
- AlphaFold3 modeling to predict EFC structure and antibody epitope locations.
- Vaccinia virus (VACV) challenge studies in female mice.
Main Results:
- Antibodies against six of 10 EFC proteins demonstrated neutralizing activity.
- Two novel targets, A16 and G9, located at the EFC apex, induced cross-neutralizing antibodies.
- A16 and G9 antibodies conferred protection against lethal VACV infection in mice.
- Antibodies to A16 and G9 were absent after VACV infection, suggesting immune evasion.
Conclusions:
- A structural model of the EFC's immunogenic and antigenic properties was established.
- A16 and G9 represent promising immunogens for next-generation recombinant poxvirus vaccines.
- Physical sequestration of A16 and G9 may be a novel poxvirus immune evasion mechanism.
