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Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) is a newly identified member of Family Coronaviridae. Coronavirus envelope spike protein S is a class I viral fusion protein which is characterized by the existence of two heptad repeat regions (HR1 and HR2) (forming a complex called fusion core). Here we report that by using in vitro bio-engineering techniques, SARS-CoV HR1 and HR2 bind to each other and form a typical 6-helix bundle. The HR2, either as a synthetic peptide or as a GST-fusion polypeptide, is a potent inhibitor of virus entry. The results do show that SARS-CoV follows the general fusion mechanism of class I viruses and this lays the ground for identification of virus fusion/entry inhibitors for this devastating emerging virus.

Original publication

DOI

10.1016/j.bbrc.2004.04.141

Type

Journal article

Journal

Biochem Biophys Res Commun

Publication Date

18/06/2004

Volume

319

Pages

283 - 288

Keywords

Circular Dichroism, Dose-Response Relationship, Drug, Escherichia coli, Glutathione Transferase, Membrane Glycoproteins, Peptides, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Fusion Proteins, SARS Virus, Spike Glycoprotein, Coronavirus, Temperature, Viral Core Proteins, Viral Envelope Proteins, Viral Fusion Proteins, Viral Proteins