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Título: | The envelope protein of severe acute respiratory syndrome coronavirus interacts with the non-structural protein 3 and is ubiquitinated |
Autor: | Álvarez, Enrique ; DeDiego, Marta L. CSIC ORCID ; Nieto-Torres, José L. ; Jiménez-Guardeño, José Manuel CSIC ORCID ; Marcos-Villar, Laura CSIC ORCID ; Enjuanes Sánchez, Luis CSIC ORCID | Palabras clave: | Coronavirus Proteomics Envelope proteinm Ubiquitination |
Fecha de publicación: | 5-jul-2010 | Editor: | Elsevier | Citación: | Virology 402(2): 281-291 (2010) | Resumen: | To 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. | Versión del editor: | http://dx.doi.org/10.1016/j.virol.2010.03.015 | URI: | http://hdl.handle.net/10261/204772 | DOI: | 10.1016/j.virol.2010.03.015 | Identificadores: | doi: 10.1016/j.virol.2010.03.015 issn: 0042-6822 |
Aparece en las colecciones: | (CNB) Artículos (PTI Salud Global) Colección Especial COVID-19 |
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