The envelope protein of severe acute respiratory syndrome coronavirus interacts with the non-structural protein 3 and is ubiquitinated.
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.
Mesh Terms:
Animals, Cell Line, Cercopithecus aethiops, Chromatography, Affinity, Humans, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protein Processing, Post-Translational, RNA Replicase, SARS Virus, Ubiquitination, Viral Envelope Proteins, Viral Nonstructural Proteins
Animals, Cell Line, Cercopithecus aethiops, Chromatography, Affinity, Humans, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Protein Processing, Post-Translational, RNA Replicase, SARS Virus, Ubiquitination, Viral Envelope Proteins, Viral Nonstructural Proteins
Virology
Date: Jul. 05, 2010
PubMed ID: 20409569
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