A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein

Eyal Arbely; Ziad Khattari; Guillaume Brotons; Mutaz Akkawi; Tim Salditt; Isaiah T. Arkin

doi:10.1016/j.jmb.2004.06.044

A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein

Eyal Arbely
, Ziad Khattari
, Guillaume Brotons
, Mutaz Akkawi
, Tim Salditt
, Isaiah T. Arkin

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

86 Citations (Scopus)

Abstract

The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity. © 2004 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	769-779
Journal	Journal of Molecular Biology
Volume	341
Issue number	3
DOIs	https://doi.org/10.1016/j.jmb.2004.06.044
Publication status	Published - 13 Aug 2004
Externally published	Yes

Bibliographical note

Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Keywords

BCoV, bovine coronavirus
membrane proteins
MHV, mouse hepatitis virus
SARS coronavirus
SARS, severe acute respiratory syndrome
SCoV, SARS coronavirus
TGEV, transmissible gastroenteritis virus
transmembrane helices
viral budding

Access Output

10.1016/j.jmb.2004.06.044

Other Access Options

Check CityUHK Library

Permanent Link

Right click to copy link

Cite this

@article{2dbc2c8ffefb4290ae00437f4a2d76cf,

title = "A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein",

abstract = "The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity. {\textcopyright} 2004 Elsevier Ltd. All rights reserved.",

keywords = "BCoV, bovine coronavirus, membrane proteins, MHV, mouse hepatitis virus, SARS coronavirus, SARS, severe acute respiratory syndrome, SCoV, SARS coronavirus, TGEV, transmissible gastroenteritis virus, transmembrane helices, viral budding",

author = "Eyal Arbely and Ziad Khattari and Guillaume Brotons and Mutaz Akkawi and Tim Salditt and Arkin, \{Isaiah T.\}",

note = "Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].",

year = "2004",

month = aug,

day = "13",

doi = "10.1016/j.jmb.2004.06.044",

language = "English",

volume = "341",

pages = "769--779",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "3",

}

TY - JOUR

T1 - A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein

AU - Arbely, Eyal

AU - Khattari, Ziad

AU - Brotons, Guillaume

AU - Akkawi, Mutaz

AU - Salditt, Tim

AU - Arkin, Isaiah T.

N1 - Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].

PY - 2004/8/13

Y1 - 2004/8/13

N2 - The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity. © 2004 Elsevier Ltd. All rights reserved.

AB - The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity. © 2004 Elsevier Ltd. All rights reserved.

KW - BCoV, bovine coronavirus

KW - membrane proteins

KW - MHV, mouse hepatitis virus

KW - SARS coronavirus

KW - SARS, severe acute respiratory syndrome

KW - SCoV, SARS coronavirus

KW - TGEV, transmissible gastroenteritis virus

KW - transmembrane helices

KW - viral budding

UR - https://www.scopus.com/pages/publications/4344645639

UR - https://www.scopus.com/pages/publications/4344645639#tab=impact

U2 - 10.1016/j.jmb.2004.06.044

DO - 10.1016/j.jmb.2004.06.044

M3 - RGC 21 - Publication in refereed journal

C2 - 15288785

SN - 0022-2836

VL - 341

SP - 769

EP - 779

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 3

ER -

A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein

Abstract

Bibliographical note

UN SDGs

Research Keywords

Access Output

Other Access Options

Permanent Link

Other Files and Links

Fingerprint

Cite this