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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