Targeted intracellular degradation of SARS-CoV-2 via computationally optimized peptide fusions.
The COVID-19 pandemic, caused by the novel coronavirus SARS-CoV-2, has elicited a global health crisis of catastrophic proportions. With only a few vaccines approved for early or limited use, there is a critical need for effective antiviral strategies. In this study, we report a unique antiviral platform, through computational design of ACE2-derived peptides which both target the viral spike protein receptor binding domain (RBD) and recruit E3 ubiquitin ligases for subsequent intracellular degradation of SARS-CoV-2 in the proteasome. Our engineered peptide fusions demonstrate robust RBD degradation capabilities in human cells and are capable of inhibiting infection-competent viral production, thus prompting their further experimental characterization and therapeutic development.
Duke Scholars
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Related Subject Headings
- Virus Attachment
- Ubiquitin-Protein Ligases
- Spike Glycoprotein, Coronavirus
- SARS-CoV-2
- Ribonucleoproteins
- Recombinant Fusion Proteins
- Receptors, Virus
- Proteolysis
- Protein Engineering
- Protein Domains
Citation
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Issue
Start / End Page
Related Subject Headings
- Virus Attachment
- Ubiquitin-Protein Ligases
- Spike Glycoprotein, Coronavirus
- SARS-CoV-2
- Ribonucleoproteins
- Recombinant Fusion Proteins
- Receptors, Virus
- Proteolysis
- Protein Engineering
- Protein Domains