Immunological, structural, and preliminary X-ray diffraction characterizations of the fusion core of the SARS-coronavirus spike protein

Chun Hua Hsu, Tzu Ping Ko, Hui Ming Yu, Tswen Kei Tang, Shui Tsung Chen, Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

The SARS-CoV spike protein, a glycoprotein essential for viral entry, is a primary target for vaccine and drug development. Two peptides denoted HR-N(SN50) and HR-C(SC40), corresponding to the Leu/Ile/Val-rich heptad-repeat regions from the N-terminal and C-terminal segments of the SARS-CoV spike S2 sequence, respectively, were synthesized and predicted to form trimeric assembly of hairpin-like structures. The polyclonal antibodies produced by recombinant S2 protein were tested for antigenicity of the two heptad repeats. We report here the first crystallographic study of the SARS spike HR-N/HR-C complex. The crystal belongs to the triclinic space group P1 and the data-set collected to 2.98 Å resolution showed noncrystallographic pseudo-222 and 3-fold symmetries. Based on these data, comparative modeling of the SARS-CoV fusion core was performed. The immunological and structural information presented herein may provide a more detailed understanding of the viral fusion mechanism as well as the development of effective therapy against SARS-CoV infection.

Original languageEnglish
Pages (from-to)761-767
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume324
Issue number2
DOIs
Publication statusPublished - Nov 12 2004
Externally publishedYes

Keywords

  • Coiled coil
  • Heptad repeat
  • Pseudo-symmetry
  • SARS
  • Spike
  • Synchrotron radiation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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