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Related Experiment Video

Updated: Jun 19, 2025

Author Spotlight: A Pseudotype Virus System for Assessing Omicron Subvariants and Neutralizing Antibodies in SARS-CoV-2 Research
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Enhanced Omicron Variant Neutralization by a Human Antibody Tailored to Wild-Type and Delta-Variant SARS-CoV-2 RBDs.

Jisun Lee1,2, Bomi Kim1,2, Hye-Min Woo3

  • 1Department of Biomedical Sciences, Graduate School, Korea University, Seoul 02841, Republic of Korea.

Molecular Pharmaceutics
|July 26, 2024
PubMed
Summary

A novel monoclonal antibody, JS18.1, shows enhanced neutralizing activity against SARS-CoV-2 Omicron variants. This antibody, developed using advanced display technologies, offers potential for broad-spectrum therapeutic interventions against emerging viral strains.

Keywords:
SARS-CoV-2antibodyneutralizationnoncompetitive interactionomicron

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Area of Science:

  • Virology
  • Immunology
  • Biotechnology

Background:

  • The unpredictable nature of viral evolution necessitates the development of broad-spectrum neutralizing antibodies.
  • Previous SARS-CoV-2 variants highlighted the need for rapid therapeutic and prophylactic interventions.
  • Targeting diverse epitopes is crucial for effective antibody-based strategies against emerging viral threats.

Purpose of the Study:

  • To engineer a monoclonal antibody with cross-reactivity against SARS-CoV-2 Receptor Binding Domains (RBDs).
  • To evaluate the neutralizing activity of the engineered antibody against various SARS-CoV-2 variants, including Omicron.
  • To investigate the binding characteristics of the antibody in relation to ACE2.

Main Methods:

  • Utilized Escherichia coli inner membrane display of a human naïve antibody library to identify SARS-CoV-2 wild-type RBD-specific antibodies.
  • Employed directed evolution via yeast surface display to optimize antibody affinity and specificity, yielding JS18.1.
  • Assessed antibody binding affinity to multiple RBDs (wild-type, Alpha, Beta, Gamma, Delta, Kappa, Mu) and neutralizing activity against the Omicron variant.

Main Results:

  • Identified and engineered the JS18.1 antibody, demonstrating high binding affinity for Delta and Kappa RBDs and enhanced binding across multiple SARS-CoV-2 variants.
  • JS18.1 exhibited surprisingly enhanced neutralizing activity against the Omicron variant, despite significant mutations.
  • The antibody binds to RBDs noncompetitively with the ACE2 receptor.

Conclusions:

  • Pre-existing antibodies can possess potent neutralizing capabilities against emerging SARS-CoV-2 strains.
  • The JS18.1 antibody represents a promising candidate for therapeutic and prophylactic interventions against a broad range of SARS-CoV-2 variants.
  • This study provides valuable insights into strategies for developing effective countermeasures against rapidly evolving viruses.