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Title

The envelope protein of severe acute respiratory syndrome coronavirus interacts with the non-structural protein 3 and is ubiquitinated

AuthorsÁlvarez, Enrique ; DeDiego, Marta L. CSIC ORCID ; Nieto-Torres, José L. ; Jiménez-Guardeño, José Manuel CSIC ; Marcos-Villar, Laura CSIC ORCID ; Enjuanes Sánchez, Luis CSIC ORCID
KeywordsCoronavirus
Proteomics
Envelope proteinm
Ubiquitination
Issue Date5-Jul-2010
PublisherElsevier
CitationVirology 402(2): 281-291 (2010)
AbstractTo analyze the proteins interacting with the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope (E) protein, a SARS-CoV was engineered including two tags associated to the E protein. Using this virus, complexes of SARS-CoV E and other proteins were purified using a tandem affinity purification system. Several viral and cell proteins including spike, membrane, non-structural protein 3 (nsp3), dynein heavy chain, fatty acid synthase and transmembrane protein 43 bound E protein. In the present work, we focused on the binding of E protein to nsp3 in infected cells and cell-free systems. This interaction was mediated by the N-terminal acidic domain of nsp3. Moreover, nsp3 and E protein colocalized during the infection. It was shown that E protein was ubiquitinated in vitro and in cell culture, suggesting that the interaction between nsp3 and E protein may play a role in the E protein ubiquitination status and therefore on its turnover. © 2010 Elsevier Inc.
Publisher version (URL)http://dx.doi.org/10.1016/j.virol.2010.03.015
URIhttp://hdl.handle.net/10261/204772
DOI10.1016/j.virol.2010.03.015
Identifiersdoi: 10.1016/j.virol.2010.03.015
issn: 0042-6822
Appears in Collections:(CNB) Artículos
(VICYT) Colección Especial COVID-19

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