Functional expression, purification, characterization, and membrane reconstitution of non-structural protein 2 from hepatitis C virus
Non-structural protein 2 (NS2) of the hepatitis C virus (HCV) is an integral membrane protein that contains a cysteine protease and that plays a central organizing role in assembly of infectious progeny virions. While the crystal structure of the protease domain has been solved, the NS2 full-length...
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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
29 August 2015
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| In: |
Protein expression and purification
Year: 2015, Jahrgang: 116, Pages: 1-6 |
| ISSN: | 1096-0279 |
| DOI: | 10.1016/j.pep.2015.08.027 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.pep.2015.08.027 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S1046592815300474 
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| Verfasserangaben: | Marie-Laure Fogeron, David Paul, Vlastimil Jirasko, Roland Montserret, Denis Lacabanne, Jennifer Molle, Aurélie Badillo, Célia Boukadida, Sonia Georgeault, Philippe Roingeard, Annette Martin, Ralf Bartenschlager, François Penin, Anja Böckmann |
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| 520 | |a Non-structural protein 2 (NS2) of the hepatitis C virus (HCV) is an integral membrane protein that contains a cysteine protease and that plays a central organizing role in assembly of infectious progeny virions. While the crystal structure of the protease domain has been solved, the NS2 full-length form remains biochemically and structurally uncharacterized because recombinant NS2 could not be prepared in sufficient quantities from cell-based systems. We show here that functional NS2 in the context of the NS2-NS3pro precursor protein, ensuring NS2-NS3 cleavage, can be efficiently expressed by using a wheat germ cell-free expression system. In this same system, we subsequently successfully produce and purify milligram amounts of a detergent-solubilized form of full-length NS2 exhibiting the expected secondary structure content. Furthermore, immuno-electron microscopy analyses of reconstituted proteoliposomes demonstrate NS2 association with model membranes. | ||
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| 650 | 4 | |a Hepatitis C virus | |
| 650 | 4 | |a Lipid reconstitution | |
| 650 | 4 | |a Membrane protein | |
| 650 | 4 | |a Non-structural protein 2 | |
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