Following the rule: formation of the 6-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors. Biochem Biophys Res Commun 2004 Jun 18;319(1):283-8
Date
05/26/2004Pubmed ID
15158473Pubmed Central ID
PMC7111185DOI
10.1016/j.bbrc.2004.04.141Scopus ID
2-s2.0-2442705099 (requires institutional sign-in at Scopus site) 102 CitationsAbstract
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.
Author List
Zhu J, Xiao G, Xu Y, Yuan F, Zheng C, Liu Y, Yan H, Cole DK, Bell JI, Rao Z, Tien P, Gao GFAuthor
Jieqing Zhu PhD Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Circular DichroismDose-Response Relationship, Drug
Escherichia coli
Glutathione Transferase
Membrane Glycoproteins
Peptides
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Fusion Proteins
Spike Glycoprotein, Coronavirus
Temperature
Viral Core Proteins
Viral Envelope Proteins
Viral Fusion Proteins
Viral Proteins
