ArticleJournal of virology2009
Identification of a novel determinant for membrane association in hepatitis C virus nonstructural protein 4B.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Deciphering the membrane topology of the pestiviral non-structural protein 4B (NS4B).Journal of virology · 2025Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- Identification of a Proline-Kinked Amphipathic α-Helix Downstream from the Methyltransferase Domain of a Potexvirus Replicase and Its Role in Virus Replication and Perinuclear Complex Formation.Journal of virology · 2021Article
- Proton-Detected Solid-State NMR of the Cell-Free Synthesized α-Helical Transmembrane Protein NS4B from Hepatitis C Virus.Chembiochem : a European journal of chemical biology · 2020Article
- Glycine Zipper Motifs in Hepatitis C Virus Nonstructural Protein 4B Are Required for the Establishment of Viral Replication Organelles.Journal of virology · 2018Article
- Evolutionary Analysis Provides Insight Into the Origin and Adaptation of HCV.Frontiers in microbiology · 2018Article
- Identification and Molecular Characterization of the Chloroplast Targeting Domain ofFrontiers in plant science · 2017Article
- PTC725, an NS4B-Targeting Compound, Inhibits a Hepatitis C Virus Genotype 3 Replicon, as Predicted by Genome Sequence Analysis and Determined Experimentally.Antimicrobial agents and chemotherapy · 2016Article
- Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus.Journal of biomolecular NMR · 2016Article
- Coevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.Scientific reports · 2016Article
- Hepatitis C virus relies on lipoproteins for its life cycle.World journal of gastroenterology · 2016Review
- Interaction between the NS4B amphipathic helix, AH2, and charged lipid headgroups alters membrane morphology and AH2 oligomeric state--Implications for the Hepatitis C virus life cycle.Biochimica et biophysica acta · 2015Article
- Article
- Flaviviral NS4b, chameleon and jack-in-the-box roles in viral replication and pathogenesis, and a molecular target for antiviral intervention.Reviews in medical virology · 2015Review
- Encoded library technology screening of hepatitis C virus NS4B yields a small-molecule compound series with in vitro replicon activity.Antimicrobial agents and chemotherapy · 2015Article
- Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein Erns.PloS one · 2015Article
- Hepatitis C virus RNA replication and assembly: living on the fat of the land.Cell host & microbe · 2014Review
- Aminoterminal amphipathic α-helix AH1 of hepatitis C virus nonstructural protein 4B possesses a dual role in RNA replication and virus production.PLoS pathogens · 2014Article
- Membrane interacting regions of Dengue virus NS2A protein.The journal of physical chemistry. B · 2014Article
- NS2 proteins of GB virus B and hepatitis C virus share common protease activities and membrane topologies.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is a relatively poorly characterized integral membrane protein predicted to comprise four transmembrane segments in its central portion. Here, we describe a novel determinant for membrane association represented by amino acids (aa) 40 to 69 in the N-terminal portion of NS4B. This segment was sufficient to target and tightly anchor the green fluorescent protein to cellular membranes, as assessed by fluorescence microscopy as well as membrane extraction and flotation analyses. Circular dichroism and nuclear magnetic resonance structural analyses showed that this segment comprises an amphipathic alpha-helix extending from aa 42 to 66. Attenuated total reflection infrared spectroscopy and glycosylation acceptor site tagging revealed that this amphipathic alpha-helix has the potential to traverse the phospholipid bilayer as a transmembrane segment, likely upon oligomerization. Alanine substitution of the fully conserved aromatic residues on the hydrophobic helix side abrogated membrane association of the segment comprising aa 40 to 69 and disrupted the formation of a functional replication complex. These results provide the first atomic resolution structure of an essential membrane-associated determinant of HCV NS4B.
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