Journal of Molecular Imaging & Dynamics
Open Access

Abstract

Saurav Wang*

The halo or crown structure of proteinaceous spike peplomers or
Glycoproteins (SGPs) detected in a transmission electron
microscope image is the basis for the name Coronavirus (CoV),
which is given to viruses that cause a variety of respiratory
illnesses, such as COVID-19 (coronavirus disease of 2019), SARS
(severe acute respiratory syndrome), and MERS (measles,
encephalitis, and respiratory syndrome) (Middle East respiratory
syndrome). SARS-CoV-2 has a shape, size (80 nm-120 nm),
genome, and RNA-based pathogenesis similar to other CoVs.
The extremely pathogenic character of SARS-CoV-2 and its
recent genetic variants suggests that these infections have high
binding affinities for a host cell and can successfully circumvent
or inhibit cytokine (interferon (IFN))-triggered immune
responses. As a result, we must address the following
fundamental problems about SARS-CoV-2 tropism, replication,
and release/transmission. How can SARS-CoV-2 adapt to the
specific SGP genes that add a Furin Cleavage Segment (FCS) to
the virus, allowing it to detect and attach to the Angiotensin-
Converting Enzyme 2 Receptor (ACE2R) efficiently? Is
Hemagglutinin (HA) a coreceptor for attaching to a host cell via
sialic acid (Sia)? How does cleavage by Neuraminidase (NASe) or
Esterase (ES) release a progeny virion? How do non-structural
proteins, Nuclear Capsid (NC) and other structural proteins,
and RNA generate progeny virions by bypassing the IFN-Induced
Janus-Activated Kinase-Signal Transducer and Activator of
Transcription (JAK-STAT) mechanism? SARS-CoV-2 was initially
linked to Rhinolophus affinis, a bat species, according to a 96
percent sequence similarity between SARS-29.9 CoV-2's kb RNA
and the RNA of the RaTG13 virus in R. affinis

Published Date: 2021-11-25;