Abstract:
Abstract
Introduction: Many of the global pandemics threaten human existence over
the decades among which coronavirus disease (COVID‐19) is the newest
exposure circulating worldwide. The RNA encoded severe acute respiratory
syndrome coronavirus 2 (SARS‐CoV‐2) virus is referred as the pivotal agent of
this deadly disease that induces respiratory tract infection by interacting host
ACE2 receptor with its spike glycoprotein. Rapidly evolving nature of this
virus modified into new variants helps in perpetrating immune escape and
protection against host defense mechanism. Consequently, a new isolate, delta
variant originated from India is spreading perilously at a higher infection rate.
Methods: In this study, we focused to understand the conformational and
functional significance of the missense mutations found in the spike glycoprotein
of SARS‐CoV‐2 delta variant performing different computational analysis.
Results: From physiochemical analysis, we found that the acidic isoelectric
point of the virus elevated to basic pH level due to the mutations. The targeted
mutations were also found to change the interactive bonding pattern and
conformational stability analyzed by the molecular dynamic's simulation. The
molecular docking study also revealed that L452R and T478K mutations
found in the RBD domain of delta variant spike protein contributed to alter
interaction with the host ACE2 receptor.
Conclusions: Overall, this study provided insightful evidence to understand
the morphological and attributive impact of the mutations on SARS‐CoV‐2
delta variant.
KEYWORDS
ACE2, COVID‐19, delta variant, mutations, SARS‐CoV‐2, spike protein
