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Biomimetic SARS-CoV-2 Spike Protein Nanoparticles
Alvin Phan1, Hugo Avila1, J Andrew MacKay1,2,3
1Department of Pharmacology and Pharmaceutical Sciences, USC Alfred E. Mann School of Pharmacy and Pharmaceutical Sciences, University of Southern California, 1985 Zonal Avenue, Los Angeles, California 90089, United States.
Biomacromolecules
|March 31, 2023
Summary
Researchers engineered a fusion protein to study the SARS-CoV-2 receptor binding domain (RBD). This novel nanoparticle system aids in understanding COVID-19 virus interactions and developing new therapies.
Area of Science:
- Biotechnology
- Virology
- Nanotechnology
Background:
- COVID-19, caused by SARS-CoV-2, utilizes a receptor binding domain (RBD) on its spike protein to infect cells.
- Understanding the RBD is critical for developing targeted COVID-19 therapies.
Purpose of the Study:
- To create a novel nanoparticle system for studying the SARS-CoV-2 RBD.
- To investigate the biophysical properties and therapeutic potential of RBD-ELP fusion nanoparticles.
Main Methods:
- Genetic engineering of fusion proteins combining SARS-CoV-2 RBD with elastin-like polypeptides (ELPs).
- Expression in *Escherichia coli*, purification via ELP-mediated phase separation.
- Characterization of nanoparticle size, shape, binding affinity to hACE2, and cellular uptake.
Main Results:
- High yield expression (79 mg/L) and purification of RBD-ELP fusions.
- Self-assembly into peptide-based nanoparticles (Rh = 71.4 nm) driven by RBD oligomerization and ELP stabilization.
- Demonstrated binding affinity to human angiotensin-converting enzyme 2 (hACE2) and cellular uptake.
Conclusions:
- Engineered RBD-ELP fusion proteins form stable, biomimetic nanoparticles.
- These nanoparticles provide a valuable tool for studying SARS-CoV-2 interactions.
- Potential for developing novel therapeutic strategies targeting SARS-CoV-2 entry pathways.
