The Chemo-Genomics Research Institute of Afe Babalola University, Ado-Ekiti, CRIA, in collaboration with the ABUAD Multi-system Hospital, AMSH, have gained new understanding about the reasons humans are more vulnerable to infections by the new variant of COVID-19, popularly known as N501Y SARS-CoV-2 mutant.
One of the reasons provided by the bio-medical scientists and researchers, led by Dr. Olaposi Omotuyi, is that the new variant is 80 times more effective at binding to human cells and is characterized by faster human-to-human transmission, more rapid progression of symptoms and death.
Since the country is not on total lockdown, the scientists and researchers advised that people should adhere to the laid down non-pharmacologic preventive procedures.
The Bio-medical scientists and Researchers at the two-sister institutions took advantage of the cutting-edge Bio-computing platform at the research institute to calculate and re-evaluate the interaction between SARS-CoV-2 spike glycoprotein receptor-binding domain (RBD) and angiotensin-converting enzyme 2 surface (ACE2) for the wild type in comparison with the new variant.
One of the outstanding discoveries of the research efforts is the improved RBD binding with ACE2 following N501 mutation.
This scientific breakthrough becomes more important and germane bearing in mind the coming of the second wave of COVID-19 which boasts of more deaths and infection than the parent pandemic.
In the heart of this second wave is the change in structure to the genetic material of the parent virus SARS-CoV-2. Although quite a number of changes in structure have been in existence before now, of higher importance is the spike-glycoprotein N501Y change. The spike glycoprotein is responsible for recognizing and binding of human cells at the angiotensin-converting enzyme2 surface (ACE2); thus, making human beings more vulnerable to the infection.
Another critical insight gained in the study is the role of N501Ymutation in altering the interface water dynamics. It should be noted that interface water acts as a stabilizing force for protein-protein interaction through enhanced hydrophobic attractions. The free energy calculation showed that N501Y-SARS-CoV-2 spike glycoprotein RBD would bind ACE2 80-times more efficiently compared to the wild type.
According to Omotuyi, these findings should therefore serve as a wake-up call for enforcement of COVID-19 protocol by all institutions, stressing that at the level of individuals, personal protection must be enforced at all times.
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