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

Eyal Arbely, Ziad Khattari, Guillaume Brotons, Mutaz Akkawi, Tim Salditt, Isaiah T. Arkin

Research output: Contribution to journalArticlepeer-review

80 Scopus citations


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.

Original languageEnglish
Pages (from-to)769-779
Number of pages11
JournalJournal of Molecular Biology
Issue number3
StatePublished - 13 Aug 2004
Externally publishedYes


  • BCoV, bovine coronavirus
  • MHV, mouse hepatitis virus
  • SARS coronavirus
  • SARS, severe acute respiratory syndrome
  • SCoV, SARS coronavirus
  • TGEV, transmissible gastroenteritis virus
  • membrane proteins
  • transmembrane helices
  • viral budding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


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