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.
| Original language | English |
|---|---|
| Pages (from-to) | 769-779 |
| Number of pages | 11 |
| Journal | Journal of Molecular Biology |
| Volume | 341 |
| Issue number | 3 |
| DOIs | |
| State | Published - 13 Aug 2004 |
Bibliographical note
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.
Keywords
- BCoV, bovine coronavirus
- MHV, mouse hepatitis virus
- SARS coronavirus
- SARS, severe acute respiratory syndrome
- SCoV, SARS coronavirus
- TGEV, transmissible gastroenteritis virus
- membrane proteins
- transmembrane helices
- viral budding
