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Related Experiment Video

Updated: Sep 10, 2025

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors

Published on: February 10, 2014

Kinetic Analysis of SARS-CoV-2 S1-Integrin Binding Using Live-Cell, Label-Free Optical Biosensing.

Nicolett Kanyo^1,2, Krisztina Borbely^1,2, Beatrix Peter¹

¹Nanobiosensorics Laboratory, Institute of Technical Physics and Materials Science, HUN-REN Centre for Energy Research, Konkoly-Thege Miklós út 29-33, H-1121 Budapest, Hungary.

|August 27, 2025

Summary

The SARS-CoV-2 spike protein can bind to cells via integrins, an alternative to ACE2 receptors. This study quantifies this interaction using label-free biosensing, revealing a new viral entry pathway.

Keywords:

HeLa cell adhesion RGD motif SARS-CoV-2 spike protein integrin binding label-free optical biosensing resonant waveguide grating

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Published on: April 25, 2019

Area of Science:

Virology
Cell Biology
Biophysics

Background:

The SARS-CoV-2 spike (S1) protein primarily uses ACE2 for viral entry.
The S1 protein also possesses an Arg-Gly-Asp (RGD) motif, suggesting potential interactions with RGD-binding integrins on ACE2-negative cells.

Purpose of the Study:

To provide quantitative evidence for an alternative SARS-CoV-2 binding pathway mediated by integrins.
To characterize the strength and kinetics of the interaction between the S1 protein and RGD-binding integrins.
To evaluate the utility of label-free resonant waveguide grating (RWG) biosensing for studying virus-host interactions.

Main Methods:

Utilized live-cell, label-free resonant waveguide grating (RWG) biosensing to monitor real-time cell adhesion.
Quantified S1-integrin interactions using a live-cell competitive binding assay with soluble S1.
Determined dissociation constants by analyzing cell adhesion kinetics on S1-coated surfaces using a kinetic model.

Main Results:

Demonstrated that the SARS-CoV-2 S1 protein can mediate cell adhesion through RGD-binding integrins.
Estimated that approximately 33% of immobilized S1 molecules on the biosensor surface can initiate integrin-mediated adhesion.
Confirmed the effectiveness of RWG biosensing for label-free, real-time analysis of virus-host cell interactions.

Conclusions:

Provides quantitative evidence for an alternative, integrin-dependent entry route for SARS-CoV-2.
Highlights the potential for SARS-CoV-2 to infect ACE2-negative cells via integrin interactions.
Establishes label-free RWG biosensing as a powerful tool for studying complex virus-host dynamics without isolating interaction partners.