Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain.
Biophys Chem
; 266: 106452, 2020 11.
Article
in English
| MEDLINE | ID: covidwho-706407
ABSTRACT
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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Pneumonia, Viral
/
Cell Membrane
/
Viral Envelope Proteins
/
Coronavirus Infections
/
Betacoronavirus
Type of study:
Observational study
Limits:
Animals
/
Humans
Language:
English
Journal:
Biophys Chem
Year:
2020
Document Type:
Article
Affiliation country:
J.bpc.2020.106452
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