Scribd
Upload
334 views100 pages

Sparvix Publishing House Project

This document discusses the structure and functions of the proteins found in coronaviruses like SARS-CoV-2. It describes the spike, envelope, and nucleocapsid proteins and how they contribute to viral entry, assembly, and replication. The spike protein facilitates viral entry into host cells by binding to receptors like ACE2. The envelope protein influences virulence by affecting morphology and tropism. The nucleocapsid protein packages the viral genome and interacts with other proteins to enhance viral transcription and assembly of new virions.

Uploaded by

Dhiraj Patil
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
334 views100 pages

Sparvix Publishing House Project

This document discusses the structure and functions of the proteins found in coronaviruses like SARS-CoV-2. It describes the spike, envelope, and nucleocapsid proteins and how they contribute to viral entry, assembly, and replication. The spike protein facilitates viral entry into host cells by binding to receptors like ACE2. The envelope protein influences virulence by affecting morphology and tropism. The nucleocapsid protein packages the viral genome and interacts with other proteins to enhance viral transcription and assembly of new virions.

Uploaded by

Dhiraj Patil
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
You are on page 1/ 100

INTRODUCTION

Over the past 2 decades, coronaviruses (CoVs) have


been associated with significant disease outbreaks in
East Asia and the Middle East. The severe acute
respiratory syndrome (SARS) and the Middle East
respiratory syndrome (MERS) began to emerge in 2002
and 2012, respectively. Recently, a novel coronavirus,
severe acute respiratory syndrome coronavirus 2
(SARS-CoV-2), causing coronavirus disease 2019
(COVID-19), emerged in late 2019, and it has posed a
global health threat, causing an ongoing pandemic in
many countries and territories (1).

Health workers worldwide are currently making efforts


to control further disease outbreaks caused by the novel
CoV (originally named 2019-nCoV), which was first
identified in Wuhan City, Hubei Province, China, on 12
December 2019. On 11 February 2020, the World
Health Organization (WHO) announced the official
designation for the current CoV-associated disease to be
COVID-19, caused by SARS-CoV-2. The primary
cluster of patients was found to be connected with the
Huanan South China Seafood Market in Wuhan (2).
CoVs belong to the family Coronaviridae (subfamily
Coronavirinae), the members of which infect a broad
trimerie S1 locates itself on top of the trimerie $2 stalk
(45). Recently, structural analyses of the S proteins of
COVID-19 have revealed 27 amino acid substitutions
within a 1,273-amino-acid stretch (16). Six substitutions
are located in the RBD (amino acids 357 to 528), while
four substitutions are in the RBM at the CTD of the S1
domain (16). Of note, no amino acid change is seen in
the RBM, which binds directly to the angiotensin-
converting enzyme-2 (ACE2) receptor in SARS-CoV
(16, 46). At present, the main emphasis is knowing how
many differences would be required to change the host
tropism. Sequence comparison revealed 17
nonsynonymous changes between the early sequence of
SARS-CoV-2 and the later isolates of SARS-CoV. The
changes were found scattered over the genome of the
virus, with nine substitutions in ORFlab, ORFS (4
substitutions), the spike gene (3 substitutions), and
ORF7a (single substitution) (4). Notably, the same
nonsynonymous changes were found in a familial
cluster, indicating that the viral evolution happened
during person-to-person transmission (4, 47). Such
adaptive evolution events are frequent and constitute a
constantly ongoing process once the virus spreads
among new hosts (47). Even though no functional
changes occur in the virus associated with this adaptive
evolution, close monitoring of the viral
absence of this protein is related to the altered virulence
of coronaviruses due to changes in morphology and
tropism (54). The E protein consists of three domains,
namely, a short hydrophilic amino terminal, a large
hydrophobic transmembrane domain, and an efficient
C-terminal domain (51). The SARS-CoV-2 E protein
reveals a similar amino acid constitution without any
substitution (16).

N Protein
The N protein of coronavirus is multipurpose. Among
several functions, it plays a role in complex formation
with the viral genome, facilitates M protein interaction
needed during virion assembly, and enhances the
transcription efficiency of the virus (55, 56). It contains
three highly conserved and distinct domains, namely, an
NTD, an RNA-binding domain or a linker region
(LKR), and a CTD (57). The NTD binds with the 3' end
of the viral genome, perhaps via electrostatic
interactions, and is highly diverged both in lagth and
sequence (58). The charged LKR is serine and arginine
rich and is also known as the SR (serine and arginine)
domain (59). The LKR is capable of direct interaction
with in vitro RNA interaction and is responsible for cell
signaling (60, 61). It also modulates the antiviral
response of the host by working as an antagonist for
interferon

You might also like

pFad - Phonifier reborn

Pfad - The Proxy pFad of © 2024 Garber Painting. All rights reserved.

Note: This service is not intended for secure transactions such as banking, social media, email, or purchasing. Use at your own risk. We assume no liability whatsoever for broken pages.


Alternative Proxies:

Alternative Proxy

pFad Proxy

pFad v3 Proxy

pFad v4 Proxy