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Updated: Sep 26, 2025
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Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
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Receptor binding domain of SARS-CoV-2 is a functional αv-integrin agonist
Emma G Norris1, Xuan Sabrina Pan2, Denise C Hocking1,2
1Department of Pharmacology and Physiology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642.
Biorxiv : the Preprint Server for Biology
|April 20, 2022
Summary
The SARS-CoV-2 spike protein
Area of Science:
- Virology and Cell Biology: Investigating molecular interactions between viral proteins and host cell receptors.
Background:
- SARS-CoV-2 spike protein contains a K403R mutation in its receptor-binding domain (RBD), creating an RGD motif.
- This RGD motif mimics sequences in extracellular matrix proteins like fibronectin, known to bind cell surface integrins.
Approach:
- Assessed the binding of recombinant S1-RBD to integrins on fibronectin-null fibroblasts and human airway cells.
- Compared S1-RBD's ability to trigger cell adhesion, signaling, and proliferation with fibronectin fragments.
- Utilized surface plasmon resonance to confirm direct binding of S1-RBD to specific integrin subtypes (αvβ3, αvβ6).
Key Points:
- S1-RBD mediated cation- and RGD-dependent cell adhesion, specifically involving αvβ3 and αvβ6 integrins.
- Adhesion to S1-RBD induced cell spreading, focal adhesion formation, and actin organization.
- S1-RBD activated key signaling pathways (FAK, Src, paxillin, Akt) and promoted cell proliferation.
Conclusions:
- The RGD sequence in SARS-CoV-2 S1-RBD acts as an αv-selective integrin agonist.
- Host cell surface integrins can functionally respond to the viral spike protein.
- S1-mediated integrin activation may contribute to SARS-CoV-2 pathogenesis and long COVID.
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