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Engineering Antiviral Agents via Surface Plasmon Resonance

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Published on: June 14, 2022

Engineering recombinantly expressed lectin-based antiviral agents.

¹Department of Environmental Health Sciences, University of California Los Angeles, CA, Los Angeles, United States.

Frontiers in Cellular and Infection Microbiology

|October 10, 2022

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Cyanovirin-N (CV-N), a lectin, inhibits human immunodeficiency virus (HIV)-1. It binds SARS-CoV-2 spike protein with low affinity, but mutations enhance binding, suggesting potential for enveloped virus neutralization.

Area of Science:

Biochemistry and Molecular Biology
Virology
Structural Biology

Background:

Cyanovirin-N (CV-N) is a lectin from Nostoc ellipsosporum with known inhibitory effects on human immunodeficiency virus (HIV)-1.
Viral spike glycoproteins, including those from HIV-1, Ebola, and SARS-CoV-2, are crucial for viral entry and are often decorated with N-linked glycans.
Lectins are proteins that bind carbohydrates, playing roles in biological recognition, including interactions with viral glycoproteins.

Purpose of the Study:

To investigate the binding interactions of Cyanovirin-N (CV-N) with the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) spike protein.
To explore how modifications to CV-N, specifically substitutions near carbohydrate-binding sites, affect its binding affinity and specificity.
To compare the binding characteristics of CV-N to different viral glycoproteins and review lectin mechanisms for potential antiviral applications.

Keywords:

SARS-CoV-2 carbohydrate-binding agent cyanovirin-N lectin virus

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Main Methods:

Surface Plasmon Resonance (SPR) and Isothermal Titration Calorimetry (ITC) were employed to measure binding affinities (dissociation constant, K_D) and stoichiometry.
Site-directed mutagenesis was used to create CV-N variants (CVN2) with altered residues near high-affinity carbohydrate-binding sites.
Saturation Transfer Difference Nuclear Magnetic Resonance (STD-NMR) was utilized to investigate lectin-glycan interactions.

Main Results:

CV-N exhibited low-affinity binding to the SARS-CoV-2 spike protein (K_D = 18.6 µM) and its receptor-binding domain (RBD) (K_D = 260 µM).
Mutations in CVN2, particularly those introducing polar interactions by substituting disulfide bonds, significantly increased binding affinity to carbohydrate ligands.
The study revealed the stoichiometry and affinity of CVN2 interactions with dimannose units, differentiating between high- and low-affinity binding sites.

Conclusions:

CV-N demonstrates a low-affinity interaction with the SARS-CoV-2 spike protein, contrasting with its higher affinity for other viral glycoproteins.
Engineered CV-N variants with enhanced polar interactions show improved binding affinity, highlighting the potential for structure-based design of antiviral lectins.
Understanding lectin-glycoprotein interactions is crucial for developing novel strategies to inhibit viral entry and fusion, offering a potential avenue for antiviral therapies.