Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain

Autor: Shruti Mukherjee, Dipita Bhattacharyya, Anirban Bhunia
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Models
Molecular
TMD
transmembrane domain
Val
Valine
Biochemistry
IDRs
intrinsically disordered regions
MERS-CoV
Middle East respiratory syndrome Coronavirus
Viral Envelope Proteins
SARS
Severe Acute Respiratory Syndrome
CoV
Coronavirus
Peptide sequence
SDS-PAGE
sodium dodecyl sulfate–polyacrylamide gel electrophoresis
chemistry.chemical_classification
Chemistry
ERGIC
Endoplasmic Reticulum-Golgi intermediate compartment
Membrane
ER
Endoplasmic Reticulum
Cell biology
Amino acid
mRNA
Messenger RNA
Transmembrane domain
Host-Pathogen Interactions
Covid-19
Coronavirus Infections
Intracellular
S
spike
IBV
Infectious bronchitis virus
Protein domain
cDNA
complementary Deoxyribonucleic Acid
Pneumonia
Viral
Biophysics
Sequence alignment
E
envelope
CoV-2
Coronavirus-2
ORFs
open reading frames
NMR
Nuclear Magnetic Resonance
LLPS
liquid-liquid phase separation
HMA
5-(N
N-hexamethylene)amiloride
ACE2
angiotensin-converting enzyme 2
Article
Pro
Proline
Betacoronavirus
Coronavirus Envelope Proteins
Asp
Aspartate
Protein Domains
LCDs
low complexity domains
Organelle
Animals
Humans
Amino Acid Sequence
MHV
Mouse hepatitis virus
BLAST
basic local alignment search tool
Cys
Cystein
Pandemics
SARS-CoV-2
C-terminus
Organic Chemistry
Cell Membrane
Structure
RNA
Ribonucleic Acid
Bcl-xL
B-cell lymphoma-extra-large
Leu
Leucine
Amyloidogenesis
M
membrane protein
SARS CoV E protein
MEGA
Molecular Evolutionary Genetics Analysis
PBD
PDZ-binding domain
Sequence Alignment
N
nucleocapsid
Zdroj: Biophysical Chemistry
ISSN: 1873-4200
0301-4622
Popis: The Envelope (E) protein in SARS Coronavirus (CoV) is a small structural protein, incorporated as part of the envelope. A major fraction of the protein has been known to be associated with the host membranes, particularly organelles related to intracellular trafficking, prompting CoV packaging and propagation. Studies have elucidated the central hydrophobic transmembrane domain of the E protein being responsible for much of the viroporin activity in favor of the virus. However, newer insights into the organizational principles at the membranous compartments within the host cells suggest further complexity of the system. The lesser hydrophobic Carboxylic-terminal of the protein harbors interesting amino acid sequences- suggesting at the prevalence of membrane-directed amyloidogenic properties that remains mostly elusive. These highly conserved segments indicate at several potential membrane-associated functional roles that can redefine our comprehensive understanding of the protein. This should prompt further studies in designing and characterizing of effective targeted therapeutic measures.
Graphical abstract Unlabelled Image
Highlights • The SARS CoV Envelope protein is a small structural protein of the virus, responsible for viroporin like activity. • Membrane- E protein interaction provides an useful insight into gaining mechanistic insight into its viroporin functions. • The central hydrophobic transmembrane domain of E protein, known to affect ion-channel formation. • The C-terminal region of the protein show further potential host-membrane directed functional roles. • The highly conserved amyloidogenic amino acid stretches of the C-terminal suggest for its contribution to CoV propagation.
Databáze: OpenAIRE
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