The binding of the spike protein of novel coronavirus to the ACE2 receptor of the host cells initiates the cascades of reactions that allow the virus to enter the host cell and cause infection. However, the inability of the human ACE2 receptor to recognize Sars-CoV-2 virus has laid to the foundation of the hypothesis that suggests mutation as the possible cause for the association.
To understand it deeper, the researchers went on to examine nearly 2,340 ACE2 mutations, after which they settled for a variant that had a combination of three mutations namely sACE2.v2.4. This variant was observed to not only bind to the virus with 50 times greater potency in the live cell cultures but also neutralize it. This binding affinity was found comparable with the monoclonal antibodies that have been identified so far against COVID-19.
Furthermore, continuous research and scientific development have allowed the researchers to isolate several highly potent neutralizing antibodies from COVID-19 exposed patients, which can directly block the biological activities of the pathogen. However, the ability of the novel coronavirus’ spike protein to undergo mutations has helped it to evade these antibodies. In contrast to this, the utilization of soluble ACE2 offers better advantages as it provides no space for these previously faced resistances. Also, the binding affinity of the ACE2 variant was found comparable to the monoclonal antibodies that have been identified so far against COVID-19. The discovery of such variants can be proved useful against the disease that previously existed or the ones that we may encounter in future.
The variant for ACE2 can:
· Binds to the virus with 50 times greater force
· Prevent its entry into the system
· Neutralize the virus
· Evade the highly mutant nature of spike protein S of Virus
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