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Biophys. J. BioFAST: First Published December 16, 2005. doi:10.1529/biophysj.105.072892
© 2005 by the Biophysical Society.

A more recent version of this article appeared on March 15, 2006.
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MEMBRANES

SARS coronavirus E Protein in Phospholipid Bilayers: A X-ray Study

Ziad Y Khattari 1, Guillaume Brotons 1, Mutaz Akkawi 2, Eyal Arbely 3, Isaiah T Arkin 3 and Tim Salditt 4*

1 University of Goettingen
2 Al-Quds University
3 Hebrew University Jerusalem
4 Universität Göttingen

* To whom correspondence should be addressed. E-mail: tsaldit{at}gwdg.de.

Submitted on August 23, 2005
Revised on September 16, 2005
Accepted on 21 November 2005


  Abstract
We have investigated the structure of the hydrophobic domain of the severe acute respiratory syndrome (SARS) E protein (SCoV E) in model lipid membranes by x-ray reflectivity (XRR) and x-ray scattering. In particular, we have used XRR to study the location of an iodine labelled residue within the lipid bilayer. The label imposes spatial constraints on the protein topology. Experimental data taken as a function of protein-to-lipid ratio P/L and different swelling states support the hairpin conformation of SCoV E reported previously (Arbely et al. 2004}. Changes of the bilayer thickness and acyl chain ordering are presented as a function of P/L, and discussed in view of different structural models.

Key Words: SARS E protein, membrane protein, model membranes, viral ion channels, x-ray reflectivity, x-ray scattering




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J. Torres, K. Parthasarathy, X. Lin, R. Saravanan, A. Kukol, and D. X. Liu
Model of a Putative Pore: The Pentameric {alpha}-Helical Bundle of SARS Coronavirus E Protein in Lipid Bilayers
Biophys. J., August 1, 2006; 91(3): 938 - 947.
[Abstract] [Full Text] [PDF]


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Copyright © 2005 by the Biophysical Society.