The coronavirus E protein: Assembly and beyond

Travis R. Ruch; Carolyn E. Machamer

doi:10.3390/v4030363

The coronavirus E protein: Assembly and beyond

Travis R. Ruch, Carolyn E. Machamer

School of Medicine

Research output: Contribution to journal › Review article › peer-review

100 Scopus citations

Abstract

The coronavirus E protein is a small membrane protein that has an important role in the assembly of virions. Recent studies have indicated that the E protein has functions during infection beyond assembly, including in virus egress and in the host stress response. Additionally, the E protein has ion channel activity, interacts with host proteins, and may have multiple membrane topologies. The goal of this review is to highlight the properties and functions of the E protein, and speculate on how they may be related.

Original language	English (US)
Pages (from-to)	363-382
Number of pages	20
Journal	Viruses
Volume	4
Issue number	3
DOIs	https://doi.org/10.3390/v4030363
State	Published - Mar 2012

Keywords

Coronavirus assembly
Envelope protein
Golgi complex
Ion channel
Membrane protein topology

ASJC Scopus subject areas

Infectious Diseases
Virology

Access to Document

10.3390/v4030363

Cite this

@article{ed16af6bb7714a71be722d669df09a48,

title = "The coronavirus E protein: Assembly and beyond",

abstract = "The coronavirus E protein is a small membrane protein that has an important role in the assembly of virions. Recent studies have indicated that the E protein has functions during infection beyond assembly, including in virus egress and in the host stress response. Additionally, the E protein has ion channel activity, interacts with host proteins, and may have multiple membrane topologies. The goal of this review is to highlight the properties and functions of the E protein, and speculate on how they may be related.",

keywords = "Coronavirus assembly, Envelope protein, Golgi complex, Ion channel, Membrane protein topology",

author = "Ruch, {Travis R.} and Machamer, {Carolyn E.}",

year = "2012",

month = mar,

doi = "10.3390/v4030363",

language = "English (US)",

volume = "4",

pages = "363--382",

journal = "Viruses",

issn = "1999-4915",

publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",

number = "3",

}

TY - JOUR

T1 - The coronavirus E protein

T2 - Assembly and beyond

AU - Ruch, Travis R.

AU - Machamer, Carolyn E.

PY - 2012/3

Y1 - 2012/3

N2 - The coronavirus E protein is a small membrane protein that has an important role in the assembly of virions. Recent studies have indicated that the E protein has functions during infection beyond assembly, including in virus egress and in the host stress response. Additionally, the E protein has ion channel activity, interacts with host proteins, and may have multiple membrane topologies. The goal of this review is to highlight the properties and functions of the E protein, and speculate on how they may be related.

AB - The coronavirus E protein is a small membrane protein that has an important role in the assembly of virions. Recent studies have indicated that the E protein has functions during infection beyond assembly, including in virus egress and in the host stress response. Additionally, the E protein has ion channel activity, interacts with host proteins, and may have multiple membrane topologies. The goal of this review is to highlight the properties and functions of the E protein, and speculate on how they may be related.

KW - Coronavirus assembly

KW - Envelope protein

KW - Golgi complex

KW - Ion channel

KW - Membrane protein topology

UR - http://www.scopus.com/inward/record.url?scp=84858973962&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84858973962&partnerID=8YFLogxK

U2 - 10.3390/v4030363

DO - 10.3390/v4030363

M3 - Review article

C2 - 22590676

AN - SCOPUS:84858973962

SN - 1999-4915

VL - 4

SP - 363

EP - 382

JO - Viruses

JF - Viruses

IS - 3

ER -

The coronavirus E protein: Assembly and beyond

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this