Journal
VIROLOGY
Volume 402, Issue 2, Pages 281-291Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2010.03.015
Keywords
Coronavirus; Proteomics; Envelope protein; Ubiquitination
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Funding
- Ministry of Science and Innovation of Spain [BIO2007-60978]
- European Union [SSPE-CT-2005-022639, 223498]
- U.S. National Institutes of Health [ARRA-W000151845]
- National Institute of Health (ISCIII) of Spain
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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. (C) 2010 Elsevier Inc. All rights reserved.
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