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Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
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Engineering Antiviral Agents via Surface Plasmon Resonance.
1Department of Environmental Health Sciences, University of California, Los Angeles; Department of General Surgery, Medical University of Vienna; irene.maier@meduniwien.ac.at.
Journal of Visualized Experiments : Jove
|July 5, 2022
Summary
Cyanovirin-N (CV-N) binds viral spike proteins like HA and Ebola GP. This study shows monomeric CV-N binds SARS-CoV-2 spike glycoprotein with lower affinity than other viruses, offering insights into viral interactions.
Area of Science:
- Biochemistry
- Virology
- Molecular Interactions
Background:
- Cyanovirin-N (CV-N) is a potent antiviral protein known to bind viral envelope glycoproteins.
- Dimeric CV-N exhibits high- and low-affinity binding sites for various viral spikes, including HA, gp120, and Ebola GP.
- Previous studies demonstrated multivalent binding of CV-N to viral glycoproteins, influencing binding affinity and neutralization.
Purpose of the Study:
- To investigate the binding characteristics of monomeric CV-N to the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S) glycoprotein.
- To compare the binding affinity of CV-N to SARS-CoV-2 with its known interactions with other viral spike proteins.
- To explore the role of disulfide bonds in CV-N's binding affinity to hemagglutinin (HA).
Main Methods:
- Surface plasmon resonance (SPR) was employed to quantify binding interactions.
- Dissociation constants (KD) were determined for CV-N binding to various viral glycoproteins.
- Site-directed mutagenesis was used to alter disulfide bonds in dimeric CV-N to assess their impact on HA binding.
Main Results:
- Monomeric CV-N binds the SARS-CoV-2 spike glycoprotein with a dissociation constant (KD) of 18.6 µM.
- This binding affinity is significantly lower compared to the nanomolar KD values observed for other viral spikes like HA and Ebola GP.
- Reducing disulfide bonds in dimeric CV-N decreased its binding affinity to HA, highlighting the structural importance of these bonds.
Conclusions:
- Cyanovirin-N exhibits multispecific binding to viral spike proteins, but its affinity for SARS-CoV-2 spike is in the mid-micromolar range.
- The binding affinity of CV-N to viral glycoproteins is influenced by its oligomeric state and structural features like disulfide bonds.
- These findings provide valuable insights into the molecular interactions between CV-N and different viral surface proteins, potentially informing antiviral drug development.
