Back to Search
Start Over
A Highly Unusual Palindromic Transmembrane Helical Hairpin Formed by SARS Coronavirus E Protein
- Source :
-
Journal of Molecular Biology . Aug2004, Vol. 341 Issue 3, p769-779. 11p. - Publication Year :
- 2004
-
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. [Copyright &y& Elsevier]
- Subjects :
- *MEMBRANE proteins
*AQUAPORINS
*HEPATITIS viruses
*HEPATITIS D virus
Subjects
Details
- Language :
- English
- ISSN :
- 00222836
- Volume :
- 341
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Journal of Molecular Biology
- Publication Type :
- Academic Journal
- Accession number :
- 13958464
- Full Text :
- https://doi.org/10.1016/j.jmb.2004.06.044