A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein

J Mol Biol. 2004 Aug 13;341(3):769-79. doi: 10.1016/j.jmb.2004.06.044.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Membrane / metabolism
  • Coronavirus / metabolism*
  • Lipid Bilayers / chemistry
  • Microscopy, Electron
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Scattering, Radiation
  • Sequence Homology, Amino Acid
  • Severe acute respiratory syndrome-related coronavirus
  • Spectroscopy, Fourier Transform Infrared
  • Thermodynamics
  • Viral Envelope Proteins / chemistry*
  • X-Rays


  • Lipid Bilayers
  • Viral Envelope Proteins