SARS coronavirus E protein in phospholipid bilayers: an x-ray study

Biophys J. 2006 Mar 15;90(6):2038-50. doi: 10.1529/biophysj.105.072892. Epub 2005 Dec 16.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Dimyristoylphosphatidylcholine / chemistry*
  • Lipid Bilayers / chemistry*
  • Membrane Fluidity*
  • Membrane Proteins / chemistry
  • Membrane Proteins / ultrastructure
  • Phase Transition
  • Phospholipids / chemistry*
  • Protein Conformation
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / ultrastructure*
  • Viroporin Proteins
  • X-Ray Diffraction


  • E protein, SARS coronavirus
  • Lipid Bilayers
  • Membrane Proteins
  • Phospholipids
  • Viral Envelope Proteins
  • Viroporin Proteins
  • Dimyristoylphosphatidylcholine