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Severe acute respiratory syndrome coronavirus protein 7a interacts with hSGT.

Identifieur interne : 003D07 ( Main/Exploration ); précédent : 003D06; suivant : 003D08

Severe acute respiratory syndrome coronavirus protein 7a interacts with hSGT.

Auteurs : Burtram C. Fielding [Singapour] ; Vithiagaran Gunalan ; Timothy H P. Tan ; Chih-Fong Chou ; Shuo Shen ; Sehaam Khan ; Seng Gee Lim ; Wanjin Hong ; Yee-Joo Tan

Source :

RBID : pubmed:16580632

Descripteurs français

English descriptors

Abstract

Severe acute respiratory syndrome coronavirus (SARS-CoV) 7a is an accessory protein with no known homologues. In this study, we report the interaction of a SARS-CoV 7a and small glutamine-rich tetratricopeptide repeat-containing protein (SGT). SARS-CoV 7a and human SGT interaction was identified using a two-hybrid system screen and confirmed with interaction screens in cell culture and cellular co-localization studies. The SGT domain of interaction was mapped by deletion mutant analysis and results indicated that tetratricopeptide repeat 2 (aa 125-158) was essential for interaction. We also showed that 7a interacted with SARS-CoV structural proteins M (membrane) and E (envelope), which have been shown to be essential for virus-like particle formation. Taken together, our results coupled with data from studies of the interaction between SGT and HIV-1 vpu indicated that SGT could be involved in the life-cycle, possibly assembly of SARS-CoV.

DOI: 10.1016/j.bbrc.2006.03.091
PubMed: 16580632


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) 7a is an accessory protein with no known homologues. In this study, we report the interaction of a SARS-CoV 7a and small glutamine-rich tetratricopeptide repeat-containing protein (SGT). SARS-CoV 7a and human SGT interaction was identified using a two-hybrid system screen and confirmed with interaction screens in cell culture and cellular co-localization studies. The SGT domain of interaction was mapped by deletion mutant analysis and results indicated that tetratricopeptide repeat 2 (aa 125-158) was essential for interaction. We also showed that 7a interacted with SARS-CoV structural proteins M (membrane) and E (envelope), which have been shown to be essential for virus-like particle formation. Taken together, our results coupled with data from studies of the interaction between SGT and HIV-1 vpu indicated that SGT could be involved in the life-cycle, possibly assembly of SARS-CoV.</div>
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