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Updated: Aug 2, 2025

Engineering Antiviral Agents via Surface Plasmon Resonance

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Published on: June 14, 2022

SARS-CoV-2 evolved variants optimize binding to cellular glycocalyx.

Sang Hoon Kim¹, Fiona L Kearns², Mia A Rosenfeld²

¹Department of Applied Physical Sciences, University of North Carolina - Chapel Hill, 1112 Murray Hall, CB#3050, Chapel Hill, NC 27599-2100, USA.

Cell Reports. Physical Science

|April 20, 2023

Summary

This summary is machine-generated.

SARS-CoV-2 variants like Omicron show increased binding to the host cell

Keywords:

ACE2 Brownian dynamics COVID-19 SARS-CoV-2 biomimetic biosensor electrostatic potential heparan sulfate heparin lateral-flow assay spike

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Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization

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Published on: December 23, 2020

Area of Science:

Virology
Biochemistry
Immunology

Background:

SARS-CoV-2 variants of concern emerge, posing challenges for detection and treatment.
The SARS-CoV-2 spike protein's interaction with host cell receptors is crucial for viral entry.
Heparan sulfate (HS) and angiotensin converting enzyme 2 (ACE2) are key components of the host cell surface involved in viral attachment.

Purpose of the Study:

To investigate the impact of evolving positive charge on the SARS-CoV-2 spike protein.
To analyze the interaction of viral variants with heparan sulfate and ACE2 in the glycocalyx.
To understand how these interactions influence viral infectivity and detection.

Main Methods:

Analysis of spike protein charge evolution in SARS-CoV-2 variants.
Biophysical assays to measure binding rates and affinities between spike proteins, HS, and ACE2.
Characterization of ternary complex formation (spike-HS-ACE2).

Main Results:

The Omicron variant exhibits enhanced binding rates to the negatively charged glycocalyx due to increased spike protein positive charge.
Omicron spike-ACE2 affinity is similar to Delta, but Omicron spike-HS interactions are significantly enhanced.
A ternary complex of spike-HS-ACE2 was observed, with increased double- and triple-bound ACE2, indicating greater reliance on HS for attachment.

Conclusions:

SARS-CoV-2 variants evolve increased dependence on heparan sulfate for viral attachment and infection.
Enhanced HS binding contributes to the infectivity of variants like Omicron.
This understanding facilitates the development of improved diagnostic tools, such as a second-generation lateral-flow test strip using heparin and ACE2.