Impact of the Temperature on the Interactions Between Common Variants of the SARS-CoV-2 Receptor Binding Domain and the Human ACE2

Overview

Journal Sci Rep

Specialty Science

Date 2022 Jul 7

PMID 35798770

Authors

Catherine Forest-Nault

Izel Koyuturk

Jimmy Gaudreault

Alex Pelletier

Denis LAbbe

Brian Cass

Louis Bisson

Alina Burlacu

Laurence Delafosse

Matthew Stuible

Olivier Henry

Gregory De Crescenzo

Yves Durocher

Affiliations

Soon will be listed here.

Abstract

Several key mutations in the Spike protein receptor binding domain (RBD) have been identified to influence its affinity for the human Angiotensin-Converting Enzyme 2 (ACE2). Here, we perform a comparative study of the ACE2 binding to the wild type (Wuhan) RBD and some of its variants: Alpha B.1.1.7, Beta B.1.351, Delta B.1.617.2, Kappa B.1.617.1, B.1.1.7 + L452R and Omicron B.1.1.529. Using a coiled-coil mediated tethering approach of ACE2 in a novel surface plasmon resonance (SPR)-based assay, we measured interactions at different temperatures. Binding experiments at 10 °C enhanced the kinetic dissimilarities between the RBD variants and allowed a proper fit to a Langmuir 1:1 model with high accuracy and reproducibility, thus unraveling subtle differences within RBD mutants and ACE2 glycovariants. Our study emphasizes the importance of SPR-based assay parameters in the acquisition of biologically relevant data and offers a powerful tool to deepen our understanding of the role of the various RBD mutations in ACE2 interaction binding parameters.

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