ArticleBiopolymers2011
Expression and purification of the membrane protein p7 from hepatitis C virus.
Article in Biopolymers, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Interactions of SARS-CoV-2 envelope protein with amilorides correlate with antiviral activity.PLoS pathogens · 2021Article
- Viroporins and inflammasomes: A key to understand virus-induced inflammation.The international journal of biochemistry & cell biology · 2020Review
- Hepatitis C virus sequence divergence preserves p7 viroporin structural and dynamic features.Scientific reports · 2019Article
- Mutagenesis-Based Characterization and Improvement of a Novel Inclusion Body Tag.Frontiers in bioengineering and biotechnology · 2019Article
- Coupling neutron reflectivity with cell-free protein synthesis to probe membrane protein structure in supported bilayers.Scientific reports · 2017Article
- Application of an E. coli signal sequence as a versatile inclusion body tag.Microbial cell factories · 2017Article
- Current strategies for protein production and purification enabling membrane protein structural biology.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016Review
- Functional characterization of p7 viroporin from hepatitis C virus produced in a cell-free expression system.Protein expression and purification · 2016Article
- Relating structure and function of viral membrane-spanning miniproteins.Current opinion in virology · 2015Review
- Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA).Journal of biomolecular NMR · 2015Article
- Structure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion release.Hepatology (Baltimore, Md.) · 2014Article
- Three-dimensional structure and interaction studies of hepatitis C virus p7 in 1,2-dihexanoyl-sn-glycero-3-phosphocholine by solution nuclear magnetic resonance.Biochemistry · 2013Article
- The lipophilic bullet hits the targets: medicinal chemistry of adamantane derivatives.Chemical reviews · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
- Hepatitis C virus network based classification of hepatocellular cirrhosis and carcinoma.PloS one · 2012Article
- Secondary structure, dynamics, and architecture of the p7 membrane protein from hepatitis C virus by NMR spectroscopy.Biochimica et biophysica acta · 2011Article
- Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1.Biochimica et biophysica acta · 2011Review
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Authors and funding
3 authors.
Funding
Abstract
A small 63-residue membrane protein, p7, has essential roles in the infectivity of the hepatitis C virus in humans. This hydrophobic membrane protein forms homo-oligomeric ion channels in bilayers, which can be blocked by known channel-blocking compounds. To perform structural studies of p7 by nuclear magnetic resonance (NMR) spectroscopy, it is necessary to produce milligram quantities of isotopically labeled protein; as is the case for most membrane-associated proteins, this is challenging. We describe the successful expression of full-length p7 and two truncated constructs in Escherichia coli using a fusion partner that directs the overexpressed protein to inclusion bodies. Following isolation of the fusion proteins by affinity chromatography, they were chemically cleaved with cyanogen bromide. The p7-polypeptides were purified by size-exclusion chromatography. Solution NMR two-dimensional heteronuclear single quantum coherence spectra of uniformly (15) N-labeled p7-polypeptides in 1,2-dihexyl-1-sn-glycero-3-phosphocholine isotropic micelles are fully resolved, with a single resonance for each amide site. The solid-state NMR spectra of the same polypeptides in magnetically aligned 14-O-PC/6-O-PC bicelles demonstrate their reconstitution into planar phospholipid bilayers.
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