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Updated: Dec 10, 2025
Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Serotype specific epitopes identified by neutralizing antibodies underpin immunogenic differences in Enterovirus B
Kang Wang1,2,3, Binyang Zheng1,2,3, Li Zhang3
1State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences and College of Pharmacy and Drug Discovery Center for Infectious Diseases, Nankai University, 300353, Tianjin, China.
Abstract:
Echovirus 30 (E30), a serotype of Enterovirus B (EV-B), recently emerged as a major causative agent of aseptic meningitis worldwide. E30 is particularly devastating in the neonatal population and currently no vaccine or antiviral therapy is available. Here we characterize two highly potent E30-specific monoclonal antibodies, 6C5 and 4B10, which efficiently block binding of the virus to its attachment receptor CD55 and uncoating receptor FcRn. Combinations of 6C5 and 4B10 augment the sum of their individual anti-viral activities. High-resolution structures of E30-6C5-Fab and E30-4B10-Fab define the location and nature of epitopes targeted by the antibodies. 6C5 and 4B10 engage the capsid loci at the north rim of the canyon and in-canyon, respectively. Notably, these regions exhibit antigenic variability across EV-Bs, highlighting challenges in development of broad-spectrum antibodies. Our structures of these neutralizing antibodies of E30 are instructive for development of vaccines and therapeutics against EV-B infections.
Insights
Two new monoclonal antibodies, 6C5 and 4B10, effectively neutralize Echovirus 30 (E30), a cause of aseptic meningitis. These antibodies block viral entry and offer potential for developing new E30 vaccines and antivirals.
Area of Science:
- Virology
- Immunology
- Structural Biology
Background:
- Echovirus 30 (E30), an Enterovirus B (EV-B) serotype, is a leading global cause of aseptic meningitis.
- E30 poses a significant threat to neonates, with no current vaccine or antiviral treatments available.
Purpose of the Study:
- To characterize two potent E30-specific monoclonal antibodies, 6C5 and 4B10.
- To elucidate the neutralizing mechanisms and structural basis of antibody-virus interactions for E30.
Main Methods:
- Characterization of monoclonal antibodies 6C5 and 4B10 against Echovirus 30.
- Structural analysis using high-resolution crystallography of antibody-virus complexes (E30-6C5-Fab and E30-4B10-Fab).
- Assessment of antibody efficacy in blocking viral attachment and uncoating receptor interactions.
Main Results:
- Monoclonal antibodies 6C5 and 4B10 potently neutralize E30 by blocking its interaction with CD55 and FcRn receptors.
- Combined administration of 6C5 and 4B10 demonstrated synergistic antiviral activity.
- Structural data revealed distinct epitopes targeted by 6C5 (north rim of the canyon) and 4B10 (in-canyon), highlighting antigenic variability within EV-B.
Conclusions:
- The characterized neutralizing antibodies provide a foundation for developing E30-specific therapeutics.
- Understanding the structural basis of neutralization and epitope variability is crucial for designing effective vaccines and broad-spectrum antivirals against EV-B infections.
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