SARS Coronavirus E protein in phospholipid bilayers: An X-ray study

Z. Khattari; G. Brotons; M. Akkawi; E. Arbely; I. T. Arkin; T. Salditt

doi:10.1529/biophysj.105.072892

SARS Coronavirus E protein in phospholipid bilayers: An X-ray study

Z. Khattari
, G. Brotons
, M. Akkawi
, E. Arbely
, I. T. Arkin
, T. Salditt^*

^*Corresponding author for this work

Department of Biological Chemistry

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

Abstract

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

Original language	English
Pages (from-to)	2038-2050
Number of pages	13
Journal	Biophysical Journal
Volume	90
Issue number	6
DOIs	https://doi.org/10.1529/biophysj.105.072892
State	Published - Mar 2006

Bibliographical note

Funding Information:
We gratefully acknowledge financial support from the Deutsche Forschungsgemeinschaft through the German-Israel-Palestine trilateral project SA 7772/6-1.

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10.1529/biophysj.105.072892

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

author = "Z. Khattari and G. Brotons and M. Akkawi and E. Arbely and Arkin, \{I. T.\} and T. Salditt",

note = "Funding Information: We gratefully acknowledge financial support from the Deutsche Forschungsgemeinschaft through the German-Israel-Palestine trilateral project SA 7772/6-1.",

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doi = "10.1529/biophysj.105.072892",

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AU - Brotons, G.

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AU - Arbely, E.

AU - Arkin, I. T.

AU - Salditt, T.

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

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SARS Coronavirus E protein in phospholipid bilayers: An X-ray study

Abstract

Bibliographical note

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