The effect of amino acid substitutions in variants of concern on RBD:ACE2 bond kinetics biorxivpreprint Stanford TU_Muenchen UW UniUtrecht aminoacid ACE2 COVID19 coronavirus covid kinetics infection
By Bhavana KunkalikarJan 12 2023Reviewed by Danielle Ellis, B.Sc. In a recent study posted to the bioRxiv* preprint server, researchers explored the effects of mutations in the severe acute respiratory syndrome coronavirus 2 variants of concern on viral transmission.
The team proposed fusion protein constructs consisting of the human ACE2 receptor ectodomain connected via a polypeptide link to the SARS-CoV-2 RBD for the wild-type strain as well as the SARS-CoV-2 Alpha, Beta, Delta, and Gamma VOCs. The tethered ligand complexes and a magnetic bead were attached to a glass surface. Using magnetic tweezers , the team examined the interaction between RBD and ACE2 under varied amounts of constant force.
Results At forces greater than 25 pN, ACE2 unfolded with a distinctive unfolding signature, allowing the identification of certain tethers. At forces less than 10 pN, when the protein domains are in a folded configuration, the linker ensures that the ligand and receptor remain close to one another during dissociation, facilitating re-binding.
The team found excellent concurrence in absolute values and the differences between VOCs whose F1/2 values were calculated employing the two-state model. For all structures, the dissociated state's lifetimes rise exponentially with rising force. In contrast, the bound state's lifetimes were reduced with the force associated with all VOCs. Nonetheless, the dependency of taubound on force varies amongst VOCs.
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