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 - Funding Information:
This research was supported in part by a grant from the Israel Science Foundation (784/01) to ITA, a grant from the Deutsche Forschungsgemeinschaft grant to ITA, MA and TS and by a grant from Niedersachsen to ITA. ITA wishes to thank Professors A. Panet, I. Ohad and Dr M. Kosloff for helpful discussions.
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.
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.
KW - BCoV, bovine coronavirus
KW - MHV, mouse hepatitis virus
KW - SARS coronavirus
KW - SARS, severe acute respiratory syndrome
KW - SCoV, SARS coronavirus
KW - TGEV, transmissible gastroenteritis virus
KW - membrane proteins
KW - transmembrane helices
KW - viral budding
UR - http://www.scopus.com/inward/record.url?scp=4344645639&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2004.06.044
DO - 10.1016/j.jmb.2004.06.044
M3 - Article
AN - SCOPUS:4344645639
SN - 0022-2836
VL - 341
SP - 769
EP - 779
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -
