Related Experiment Video
Updated: Nov 1, 2025
Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Directed evolution of potent neutralizing nanobodies against SARS-CoV-2 using CDR-swapping mutagenesis
Jennifer M Zupancic1, Alec A Desai1, John S Schardt2
1Department of Chemical Engineering, University of Michigan, North Campus Research Complex, 2800 Plymouth Road, Ann Arbor, MI 48109, USA; Biointerfaces Institute, University of Michigan, Ann Arbor, MI 48109, USA.
A new directed evolution method simplifies the creation of high-affinity nanobodies for neutralizing SARS-CoV-2. This technique enhances antibody discovery for combating current and future viral pandemics.
Area of Science:
- Biotechnology
- Immunology
- Virology
Background:
- Developing effective neutralizing antibodies against SARS-CoV-2 is crucial for pandemic preparedness.
- Current methods of antibody isolation are limited by the natural immune response.
Purpose of the Study:
- To develop a facile method for generating high-affinity nanobodies against SARS-CoV-2.
- To create potent neutralizing agents for current and future coronavirus threats.
Main Methods:
- Directed evolution using complementarity-determining region (CDR) swapping in nanobodies.
- Systematic implementation of CDR swapping on low-affinity lead nanobodies.
Main Results:
- CDR swapping significantly increased nanobody affinity.
- Matured nanobodies potently neutralized SARS-CoV-2 pseudovirus and live virus.
- Generated nanobodies exhibited drug-like biophysical properties.
Conclusions:
- The described directed evolution method is a simple and effective approach for nanobody discovery.
- This technique can accelerate the development of neutralizing nanobodies against SARS-CoV-2 and other coronaviruses.
More Related Videos
07:55Generation of Escape Variants of Neutralizing Influenza Virus Monoclonal Antibodies
Published on: August 29, 2017
10:17Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
Published on: January 14, 2020