Impact of the temperature on the interactions between common variants of the SARS-CoV-2 receptor binding domain and the human ACE2.
Sci Rep
; 12(1): 11520, 2022 07 07.
Article
in English
| MEDLINE | ID: covidwho-1921710
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 11 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.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Temperature
/
Spike Glycoprotein, Coronavirus
/
Angiotensin-Converting Enzyme 2
/
COVID-19
Type of study:
Experimental Studies
Topics:
Variants
Limits:
Humans
Language:
English
Journal:
Sci Rep
Year:
2022
Document Type:
Article
Affiliation country:
S41598-022-15215-5
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