tailieunhanh - Báo cáo khoa học: Prevalence of intrinsic disorder in the hepatitis C virus ARFP/Core+1/S protein

The hepatitis C virus (HCV) Core+1/S polypeptide, also known as alter-native reading frame protein (ARFP)/S, is an ARFP expressed from the Core coding region of the viral genome. Core+1/S is expressed as a result of internal initiation at AUG codons (85–87) located downstream of the polyprotein initiator codon, and corresponds to the C-terminal part of most ARFPs. | Prevalence of intrinsic disorder in the hepatitis C virus ARFP Core 1 S protein Anissa Boumlic1 2 Yves Nominé1 Sebastian Charbonnier1 Georgia Dalagiorgou2 Niki Vassilaki2 Bruno Kieffer3 Gilles Trave1 Penelope Mavromara2 and Georges Orfanoudakis1 1 Oncoproteins Group Universite de Strasbourg CNRS FRE 3211 Ecole Superieure de Biotechnologie de Strasbourg Illkirch France 2 Molecular Virology Laboratory Hellenic Pasteur Institute Athens Greece 3 Biomolecular NMR Group UMR CNRS 7104 Institut de Genetique et de Biologie Moleculaire et Cellulaire Illkirch France Keywords ARFP Core 1 S hepatitis C virus HCV intrinsic disorder IUP IDP NMR Correspondence G. Orfanoudakis Oncoproteins Group Universite de Strasbourg CNRS FRE 3211 Ecole Superieure de Biotechnologie de Strasbourg Illkirch France Fax 33 3 68 85 47 70 Tel 33 3 68 85 47 65 E-mail These authors contributed equally to this work Received 25 October 2009 revised 30 November 2009 accepted 1 December 2009 doi The hepatitis C virus HCV Core 1 S polypeptide also known as alternative reading frame protein ARFP S is an ARFP expressed from the Core coding region of the viral genome. Core 1 S is expressed as a result of internal initiation at AUG codons 85-87 located downstream of the polyprotein initiator codon and corresponds to the C-terminal part of most ARFPs. Core 1 S is a highly basic polypeptide and its function still remains unclear. In this work untagged recombinant Core 1 S was expressed and purified from Escherichia coli in native conditions and was shown to react with sera of HCV-positive patients. We subsequently undertook the biochemical and biophysical characterization of Core 1 S. The conformation and oligomeric state of Core 1 S were investigated using size exclusion chromatography dynamic light scattering fluorescence CD and NMR. Consistent with sequence-based disorder predictions Core 1 S lacks significant secondary structure in vitro which .

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