๐ A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein
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. ยฉ 2004 Elsevier Ltd.
author
๐ค Arbely, Eyal
๐ค Khattari, Ziad
๐ค Brotons, Guillaume
๐ค Akkawi, Mutaz
๐ค Salditt, Tim
๐ค Arkin, Isaiah T.
year
โฐ 2004
issn
๐ 00222836
volume
341
number
3
page
769-779
citedbycount
47
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