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Short Communication |
1 Axxima Pharmaceuticals AG, Am Klopferspitz 19, 82152 Martinsried, Germany
2 Department of Molecular Virology, University of Heidelberg, Im Neuenheimer Feld 350, 69120 Heidelberg, Germany
3 Department of Internal Medicine, Johannes Gutenberg University Mainz, Obere Zahlbacher Stra
e 63, 55131 Mainz, Germany
4 Department of Biochemistry, Technical University of Braunschweig, Mascheroder Weg 1, 38124 Braunschweig, Germany
Correspondence
Henrik Daub
daub{at}axxima.com
The hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be integrated in cellular kinase signalling, we isolated phosphoproteins from HuH-7 hepatoma cells that specifically interacted with recombinant NS5A protein. Subsequent mass spectrometry identified the adaptor protein amphiphysin II as a novel interaction partner of NS5A. Mutational analysis revealed that complex formation is primarily mediated by a proline-rich region in the C-terminal part of NS5A, which interacts with the amphiphysin II Src homology 3 domain. Importantly, we could further demonstrate specific co-precipitation and cellular co-localization of endogenous amphiphysin II with NS5A in HuH-7 cells carrying a persistently replicating subgenomic HCV replicon. Although the NS5A–amphiphysin II interaction appeared to be dispensable for replication of these HCV RNAs in cell culture, our results indicate that NS5A–amphiphysin II complex formation might be of physiological relevance for the HCV life cycle.
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