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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.

Identifieur interne : 005349 ( Main/Exploration ); précédent : 005348; suivant : 005350

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.

Auteurs : Jieqing Zhu [République populaire de Chine] ; Gengfu Xiao ; Yanhui Xu ; Fang Yuan ; Congyi Zheng ; Yueyong Liu ; Huimin Yan ; David K. Cole ; John I. Bell ; Zihe Rao ; Po Tien ; George F. Gao

Source :

RBID : pubmed:15158473

Descripteurs français

English descriptors

Abstract

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.

DOI: 10.1016/j.bbrc.2004.04.141
PubMed: 15158473


Affiliations:


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<term>Glutathione Transferase (metabolism)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Peptides (chemistry)</term>
<term>Protein Conformation</term>
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<term>Recombinant Fusion Proteins (metabolism)</term>
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<term>Spike Glycoprotein, Coronavirus</term>
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<div type="abstract" xml:lang="en">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.</div>
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