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Journal articles on the topic 'NS4B protein'

Author: Grafiati

Published: 7 December 2024

Last updated: 31 July 2025

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1

Zou, Jing, Xuping Xie, Qing-Yin Wang, et al. "Characterization of Dengue Virus NS4A and NS4B Protein Interaction." Journal of Virology 89, no. 7 (2015): 3455–70. http://dx.doi.org/10.1128/jvi.03453-14.

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ABSTRACTFlavivirus replication is mediated by a membrane-associated replication complex where viral membrane proteins NS2A, NS2B, NS4A, and NS4B serve as the scaffold for the replication complex formation. Here, we used dengue virus serotype 2 (DENV-2) as a model to characterize viral NS4A-NS4B interaction. NS4A interacts with NS4B in virus-infected cells and in cells transiently expressing NS4A and NS4B in the absence of other viral proteins. Recombinant NS4A and NS4B proteins directly bind to each other with an estimatedKd(dissociation constant) of 50 nM. Amino acids 40 to 76 (spanning the f

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Muñoz-Jordán, Jorge L., Maudry Laurent-Rolle, Joseph Ashour, et al. "Inhibition of Alpha/Beta Interferon Signaling by the NS4B Protein of Flaviviruses." Journal of Virology 79, no. 13 (2005): 8004–13. http://dx.doi.org/10.1128/jvi.79.13.8004-8013.2005.

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ABSTRACT Flaviviruses are insect-borne, positive-strand RNA viruses that have been disseminated worldwide. Their genome is translated into a polyprotein, which is subsequently cleaved by a combination of viral and host proteases to produce three structural proteins and seven nonstructural proteins. The nonstructural protein NS4B of dengue 2 virus partially blocks activation of STAT1 and interferon-stimulated response element (ISRE) promoters in cells stimulated with interferon (IFN). We have found that this function of NS4B is conserved in West Nile and yellow fever viruses. Deletion analysis

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Konan, Kouacou V., Thomas H. Giddings, Masanori Ikeda, Kui Li, Stanley M. Lemon, and Karla Kirkegaard. "Nonstructural Protein Precursor NS4A/B from Hepatitis C Virus Alters Function and Ultrastructure of Host Secretory Apparatus." Journal of Virology 77, no. 14 (2003): 7843–55. http://dx.doi.org/10.1128/jvi.77.14.7843-7855.2003.

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ABSTRACT The nonstructural proteins of hepatitis C virus (HCV) have been shown previously to localize to the endoplasmic reticulum (ER) when expressed singly or in the context of other HCV proteins. To determine whether the expression of HCV nonstructural proteins alters ER function, we tested the effect of expression of NS2/3/4A, NS4A, NS4B, NS4A/B, NS4B/5A, NS5A, and NS5B from genotype 1b HCV on anterograde traffic from the ER to the Golgi apparatus. Only the nominal precursor protein NS4A/B affected the rate of ER-to-Golgi traffic, slowing the rate of Golgi-specific modification of the vesi

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Roosendaal, Jojanneke, Edwin G. Westaway, Alexander Khromykh, and Jason M. Mackenzie. "Regulated Cleavages at the West Nile Virus NS4A-2K-NS4B Junctions Play a Major Role in Rearranging Cytoplasmic Membranes and Golgi Trafficking of the NS4A Protein." Journal of Virology 80, no. 9 (2006): 4623–32. http://dx.doi.org/10.1128/jvi.80.9.4623-4632.2006.

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ABSTRACT A common feature associated with the replication of most RNA viruses is the formation of a unique membrane environment encapsulating the viral replication complex. For their part, flaviviruses are no exception, whereupon infection causes a dramatic rearrangement and induction of unique membrane structures within the cytoplasm of infected cells. These virus-induced membranes, termed paracrystalline arrays, convoluted membranes, and vesicle packets, all appear to have specific functions during replication and are derived from different organelles within the host cell. The aim of this st

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Paredes, Anne M., and Keril J. Blight. "A Genetic Interaction between Hepatitis C Virus NS4B and NS3 Is Important for RNA Replication." Journal of Virology 82, no. 21 (2008): 10671–83. http://dx.doi.org/10.1128/jvi.00875-08.

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ABSTRACT Hepatitis C virus (HCV) nonstructural protein 4B (NS4B), a poorly characterized integral membrane protein, is thought to function as a scaffold for replication complex assembly; however, functional interactions with the other HCV nonstructural proteins within this complex have not been defined. We report that a Con1 chimeric subgenomic replicon containing the NS4B gene from the closely related H77 isolate is defective for RNA replication in a transient assay, suggesting that H77 NS4B is unable to productively interact with the Con1 replication machinery. The H77 NS4B sequences that pr

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Koupriyanov, V. V., L. I. Nikolaeva, A. A. Zykova, et al. "IMMUNOGENIC PROPERTIES OF RECOMBINANT MOZAIC PROTEINS BASED ON ANTIGENS NS4A AND NS4B OF HEPATITIS C VIRUS." Problems of Virology, Russian journal 63, no. 3 (2018): 138–43. http://dx.doi.org/10.18821/0507-4088-2018-63-3-138-143.

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The aim of the study was to investigate immunogenic properties of mosaic recombinant proteins constructed on the data of hepatitis C virus NS4A and NS4B antigens. Four mosaic recombinant proteins, containing the T and B epitopes of the NS4A and NS4B antigens, were created by genetic engineering methods in the E. coli system. To enhance the immune response they were linked in different variations to the nucleotide sequences of murine interleukin-2 (IL-2), the Neisseria meningiditis lipopeptide, and the T helper epitope of the core protein of hepatitis C virus. The immunogenic properties of thes

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7

Stone, Michelle, Shuaizheng Jia, Won Do Heo, Tobias Meyer, and Kouacou V. Konan. "Participation of Rab5, an Early Endosome Protein, in Hepatitis C Virus RNA Replication Machinery." Journal of Virology 81, no. 9 (2007): 4551–63. http://dx.doi.org/10.1128/jvi.01366-06.

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ABSTRACT Like most positive-strand RNA viruses, hepatitis C virus (HCV) is believed to replicate its genome on the surface of rearranged membranes. We have shown previously that HCV NS4AB, but not the product NS4B, inhibits endoplasmic reticulum (ER)-to-Golgi protein traffic (K. V. Konan, T. H. Giddings, Jr., M. Ikeda, K. Li, S. M. Lemon, and K. Kirkegaard, J. Virol. 77:7843-7855). However, both NS4AB and NS4B can induce “membranous web” formation, first reported by Egger et al. (D. B Egger, R. Gosert, L. Bianchi, H. E. Blum, D. Moradpour, and K. Bienz, J. Virol. 76:5974-5984), which is also o

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Klaitong, Paeka, and Duncan R. Smith. "Roles of Non-Structural Protein 4A in Flavivirus Infection." Viruses 13, no. 10 (2021): 2077. http://dx.doi.org/10.3390/v13102077.

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Infections with viruses in the genus Flavivirus are a worldwide public health problem. These enveloped, positive sense single stranded RNA viruses use a small complement of only 10 encoded proteins and the RNA genome itself to remodel host cells to achieve conditions favoring viral replication. A consequence of the limited viral armamentarium is that each protein exerts multiple cellular effects, in addition to any direct role in viral replication. The viruses encode four non-structural (NS) small transmembrane proteins (NS2A, NS2B, NS4A and NS4B) which collectively remain rather poorly charac

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De Francesco, Raffaele, Antonello Pessi, and Christian Steinkühler. "The Hepatitis C Virus NS3 Proteinase: Structure and Function of a Zinc-Containing Serine Proteinase." Antiviral Therapy 3, no. 3_suppl (1998): 99–109. http://dx.doi.org/10.1177/135965359800303s01.

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The hepatitis C virus (HCV) NS3 protein contains a serine proteinase domain implicated in the maturation of the viral polyprotein. NS3 forms a stable heterodimer with NS4A, a viral memebrane protein that acts as an activator of the IMS3 proteinase. The three-dimensional structure of the NS3 proteinase complexed with an NS4A-derived peptide has been determined. The NS3 proteinase adopts a chymotrypsin-like fold. A β-strand contributed by NS4A is clamped between two β-strands within the N terminus of NS3. Consistent with the requirement for extraordinarily long peptide substrates (P6-P4’), the s

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Martin, Morgan M., Stephanie A. Condotta, Jeremy Fenn, Andrea D. Olmstead, and François Jean. "In-cell selectivity profiling of membrane-anchored and replicase-associated hepatitis C virus NS3-4A protease reveals a common, stringent substrate recognition profile." Biological Chemistry 392, no. 10 (2011): 927–35. http://dx.doi.org/10.1515/bc.2011.076.

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AbstractThe need to identify anti-Flaviviridaeagents has resulted in intensive biochemical study of recombinant nonstructural (NS) viral proteases; however, experimentation on viral protease-associated replication complexes in host cells is extremely challenging and therefore limited. It remains to be determined if membrane anchoring and/or association to replicase-membrane complexes of proteases, such as hepatitis C virus (HCV) NS3-4A, plays a regulatory role in the substrate selectivity of the protease. In this study, we examined trans-endoproteolytic cleavage activities of membrane-anchored

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11

Selimović, Denis, and Mohamed Hassan. "Inhibition of Hepatitis C virus (HCV) Core protein- induced Cell Growth by Non-structural Protein 4A (NS4A) is Mediated by Mitochondrial Dysregulation." Bosnian Journal of Basic Medical Sciences 8, no. 1 (2008): 4–11. http://dx.doi.org/10.17305/bjbms.2008.2988.

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Hepatitis C virus (HCV) is a significant health problem facing the world. More than 170 million people are infected with HCV worldwide. HCV encodes a large polyprotein precursor that is processed into at least 10 distinct products including structural (core, E1 and E2) and non-structural (NS2, NS3, NS4A, NS4B, NS5A and NS5B). Besides its importance in virus replication, NS4A functions as a cofactor for NS3 and contributes to viral pathogenesis by influencing cellular functions. Here, we investigated the effect of NS4A protein on the growth rate induced by core protein in liver cells. Using our

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12

Kaufusi, Pakieli H., Alanna C. Tseng, James F. Kelley, and Vivek R. Nerurkar. "Selective Reactivity of Anti-Japanese Encephalitis Virus NS4B Antibody Towards Different Flaviviruses." Viruses 12, no. 2 (2020): 212. http://dx.doi.org/10.3390/v12020212.

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Studies investigating West Nile virus (WNV) NS4B protein function are hindered by the lack of an antibody recognizing WNV NS4B protein. Few laboratories have produced WNV NS4B antibodies, and none have been shown to work consistently. In this report, we describe a NS4B antibody against Japanese encephalitis virus (JEV) NS4B protein that cross-reacts with the NS4B protein of WNV but not of dengue virus (DENV). This JEV NS4B antibody not only recognizes WNV NS4B in infected cells, but also recognizes the NS4B protein expressed using transfection. It is evident from this data that the JEV NS4B an

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Lundin, Marika, Magnus Monné, Anders Widell, Gunnar von Heijne, and Mats A. A. Persson. "Topology of the Membrane-Associated Hepatitis C Virus Protein NS4B." Journal of Virology 77, no. 9 (2003): 5428–38. http://dx.doi.org/10.1128/jvi.77.9.5428-5438.2003.

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ABSTRACT Hepatitis C virus (HCV) belongs to the Hepacivirus genus in the Flaviviridae family. Among the least known viral proteins in this family is the nonstructural protein NS4B, which has been suggested to be a part of the replication complex. Hydrophobicity plots indicate a common profile among the NS4B proteins from different members of the Flaviviridae family, suggesting a common function. In order to gain a deeper understanding of the nature of HCV NS4B, we have determined localization and topology of this protein by using recombinant HCV NS4B constructs. The protein localized to the en

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Yu, Guann-Yi, Ki-Jeong Lee, Lu Gao, and Michael M. C. Lai. "Palmitoylation and Polymerization of Hepatitis C Virus NS4B Protein." Journal of Virology 80, no. 12 (2006): 6013–23. http://dx.doi.org/10.1128/jvi.00053-06.

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ABSTRACT Hepatitis C Virus (HCV) NS4B protein induces a specialized membrane structure which may serve as the replication platform for HCV RNA replication. In the present study, we demonstrated that NS4B has lipid modifications (palmitoylation) on two cysteine residues (cysteines 257 and 261) at the C-terminal end. Site-specific mutagenesis of these cysteine residues on individual NS4B proteins and on an HCV subgenomic replicon showed that the lipid modifications, particularly of Cys261, are important for protein-protein interaction in the formation of the HCV RNA replication complex. We furth

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Chagnon, Fanny, Alain Lamarre, Claude Lachance, et al. "Characterization of the expression and immunogenicity of the ns4b protein of human coronavirus 229E." Canadian Journal of Microbiology 44, no. 10 (1998): 1012–17. http://dx.doi.org/10.1139/w98-089.

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Sequencing of complementary DNAs prepared from various coronaviruses has revealed open reading frames encoding putative proteins that are yet to be characterized and are so far only described as nonstructural (ns). As a first step in the elucidation of its function, we characterized the expression and immunogenicity of the ns4b gene product from strain 229E of human coronavirus (HCV-229E), a respiratory virus with a neurotropic potential. The gene was cloned and expressed in bacteria. A fusion protein of ns4b with maltose-binding protein was injected into rabbits to generate specific antibodie

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Gummow, Jason, Yanrui Li, Wenbo Yu, et al. "A Multiantigenic DNA Vaccine That Induces Broad Hepatitis C Virus-Specific T-Cell Responses in Mice." Journal of Virology 89, no. 15 (2015): 7991–8002. http://dx.doi.org/10.1128/jvi.00803-15.

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ABSTRACTThere are 3 to 4 million new hepatitis C virus (HCV) infections annually around the world, but no vaccine is available. Robust T-cell mediated responses are necessary for effective clearance of the virus, and DNA vaccines result in a cell-mediated bias. Adjuvants are often required for effective vaccination, but during natural lytic viral infections damage-associated molecular patterns (DAMPs) are released, which act as natural adjuvants. Hence, a vaccine that induces cell necrosis and releases DAMPs will result in cell-mediated immunity (CMI), similar to that resulting from natural ly

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Kong, Lingbao, Akira Fujimoto, Mariko Nakamura, et al. "Prolactin Regulatory Element Binding Protein Is Involved in Hepatitis C Virus Replication by Interaction with NS4B." Journal of Virology 90, no. 6 (2016): 3093–111. http://dx.doi.org/10.1128/jvi.01540-15.

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ABSTRACTIt has been proposed that the hepatitis C virus (HCV) NS4B protein triggers the membranous HCV replication compartment, but the underlying molecular mechanism is not fully understood. Here, we screened for NS4B-associated membrane proteins by tandem affinity purification and proteome analysis and identified 202 host proteins. Subsequent screening of replicon cells with small interfering RNA identified prolactin regulatory element binding (PREB) to be a novel HCV host cofactor. The interaction between PREB and NS4B was confirmed by immunoprecipitation, immunofluorescence, and proximity

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Lundin, Marika, Hannah Lindström, Caroline Grönwall, and Mats A. A. Persson. "Dual topology of the processed hepatitis C virus protein NS4B is influenced by the NS5A protein." Journal of General Virology 87, no. 11 (2006): 3263–72. http://dx.doi.org/10.1099/vir.0.82211-0.

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Among the least-known hepatitis C virus proteins is the non-structural protein 4B (NS4B). It localizes to the endoplasmic reticulum (ER) membrane and induces membrane changes, resulting in a membranous web that is reported to be the locale for virus replication. A model was presented previously for the topology of recombinant HCV NS4B of the 1a genotype based on in vitro data. In this model, the N-terminal tail of a considerable fraction of the NS4B molecules was translocated into the ER lumen via a post-translational process, giving the protein a dual transmembrane topology. It is now reporte

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Vajdy, Michael, Mark Selby, Angelica Medina-Selby, et al. "Hepatitis C virus polyprotein vaccine formulations capable of inducing broad antibody and cellular immune responses." Journal of General Virology 87, no. 8 (2006): 2253–62. http://dx.doi.org/10.1099/vir.0.81849-0.

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Although approximately 3 % of the world's population is infected with Hepatitis C virus (HCV), there is no prophylactic vaccine available. This study reports the design, cloning and purification of a single polyprotein comprising the HCV core protein and non-structural proteins NS3, NS4a, NS4b, NS5a and NS5b. The immunogenicity of this polyprotein, which was formulated in alum, oil-in-water emulsion MF59 or poly(dl-lactide co-glycolide) in the presence or absence of CpG adjuvant, was then determined in a murine model for induction of B- and T-cell responses. The addition of adjuvants or a deli

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Gao, Lu, Hideki Aizaki, Jian-Wen He, and Michael M. C. Lai. "Interactions between Viral Nonstructural Proteins and Host Protein hVAP-33 Mediate the Formation of Hepatitis C Virus RNA Replication Complex on Lipid Raft." Journal of Virology 78, no. 7 (2004): 3480–88. http://dx.doi.org/10.1128/jvi.78.7.3480-3488.2004.

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ABSTRACT The lipid raft membrane has been shown to be the site of hepatitis C virus (HCV) RNA replication. The mechanism of formation of the replication complex is not clear. We show here that the formation of the HCV RNA replication complex on lipid raft (detergent-resistant membranes) requires interactions among the HCV nonstructural (NS) proteins and may be initiated by the precursor of NS4B, which has the intrinsic property of anchoring to lipid raft membrane. In hepatocyte cell lines containing an HCV RNA replicon, most of the other NS proteins, including NS5A, NS5B, and NS3, were also lo

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Bashir, Shahbaz, Andrey Kossarev, Violeta Cascon Martin, and Jan Paeshuyse. "Deciphering the Role of Bovine Viral Diarrhea Virus Non-Structural NS4B Protein in Viral Pathogenesis." Veterinary Sciences 7, no. 4 (2020): 169. http://dx.doi.org/10.3390/vetsci7040169.

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Bovine viral diarrhea virus (BVDV) is a (+) ssRNA virus that belongs to the family Flaviviridae. BVDV is a significant animal pathogen causing substantial economic losses to the cattle industry worldwide through respiratory and gastrointestinal infections and abortion or birth of persistently infected calves. While the immunogenic profile of some of the BVDV proteins (i.e., Erns, E2 and NS3) is well established during viral pathogenesis, very little information is available about most of BVDV’s non-structural proteins in this regard. In recent times, the NS4B protein has emerged as an interest

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Zou, Jing, Le Tian Lee, Qing Yin Wang, et al. "Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus." Journal of Virology 89, no. 7 (2015): 3471–83. http://dx.doi.org/10.1128/jvi.03454-14.

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ABSTRACTFlavivirus RNA synthesis is mediated by a multiprotein complex associated with the endoplasmic reticulum membrane, named the replication complex (RC). Within the flavivirus RC, NS4B, an integral membrane protein with a role in virulence and regulation of the innate immune response, binds to the NS3 protease-helicase. NS4B modulates the RNA helicase activity of NS3, but the molecular details of their interaction remain elusive. Here, we used dengue virus (DENV) to map the determinants for the NS3-NS4B interaction. Coimmunoprecipitation and anin situproximity ligation assay confirmed tha

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Wahaab, Abdul, Ke Liu, Muddassar Hameed, et al. "Identification of Cleavage Sites Proteolytically Processed by NS2B-NS3 Protease in Polyprotein of Japanese Encephalitis Virus." Pathogens 10, no. 2 (2021): 102. http://dx.doi.org/10.3390/pathogens10020102.

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Understanding the proteolytic processing of polyprotein mediated by NS2B-NS3 protease contributes to the exploration of the mechanisms underlying infection of Japanese encephalitis virus (JEV), a zoonotic flavivirus. In this study, eukaryotic and prokaryotic cell models were employed to identify the cleavage sites mediated by viral NS2B-NS3 protease in JEV polyprotein. Artificial green fluorescent protein (GFP) substrates that contained the predicted cleavage site sequences of JEV polyprotein were expressed in swine testicle (ST) cells in the presence and absence of JEV infection, or co-expres

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Condotta, Stephanie A., Morgan M. Martin, Martine Boutin, and François Jean. "Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates." Biological Chemistry 391, no. 5 (2010): 549–59. http://dx.doi.org/10.1515/bc.2010.051.

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AbstractFlaviviral NS2B/NS3 heterocomplex serine proteases are a primary target for anti-flavivirus drug discovery. To gain insights into the enzymatic properties and molecular determinants of flaviviral NS2B/NS3 protease substrate specificity in host cells, we developed and applied a novel series of membrane-anchored red-shifted fluorescent protein substrates to detect West Nile virus (WNV) NS2B/NS3 endoproteolytic activity in human cells. The substrate consists of a fluorescent reporter group (DsRed) tethered to the endoplasmic reticulum membrane by a membrane-anchoring domain. Between the t

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Naik, Nenavath Gopal, and Huey-Nan Wu. "Mutation of Putative N-Glycosylation Sites on Dengue Virus NS4B Decreases RNA Replication." Journal of Virology 89, no. 13 (2015): 6746–60. http://dx.doi.org/10.1128/jvi.00423-15.

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ABSTRACTDengue virus (DENV) nonstructural protein 4B (NS4B) is an endoplasmic reticulum (ER) membrane-associated protein, and mutagenesis studies have revealed its significance in viral genome replication. In this work, we demonstrated that NS4B is an N-glycosylated protein in virus-infected cells as well as in recombinant protein expression. NS4B is N glycosylated at residues 58 and 62 and exists in two forms, glycosylated and unglycosylated. We manipulated full-length infectious RNA clones and subgenomic replicons to generate N58Q, N62Q, and N58QN62Q mutants. Each of the single mutants had d

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Blight, Keril J. "Allelic Variation in the Hepatitis C Virus NS4B Protein Dramatically Influences RNA Replication." Journal of Virology 81, no. 11 (2007): 5724–36. http://dx.doi.org/10.1128/jvi.02481-06.

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ABSTRACT In the Huh-7.5 hepatoma cell line, replication of the genotype 1a H77 strain of hepatitis C virus (HCV) is attenuated compared to that of the genotype 1b Con1 strain. This study identifies the poorly characterized integral membrane protein, NS4B, as a major determinant for this replication difference. Chimeric H77 subgenomic replicons containing the entire NS4B gene from Con1 in place of the H77 NS4B sequence replicated approximately 10-fold better than the H77 parent and to levels similar to that of the adapted Con1 replicon. An intermediate level of replication enhancement was confe

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Chang, Yu-Shiu, Ching-Len Liao, Chang-Huei Tsao, et al. "Membrane Permeabilization by Small Hydrophobic Nonstructural Proteins of Japanese Encephalitis Virus." Journal of Virology 73, no. 8 (1999): 6257–64. http://dx.doi.org/10.1128/jvi.73.8.6257-6264.1999.

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ABSTRACT Infection with Japanese encephalitis virus (JEV), a mosquito-borne flavivirus, may cause acute encephalitis in humans and induce severe cytopathic effects in various types of cultured cells. We observed that JEV replication rendered infected baby hamster kidney (BHK-21) cells sensitive to the translational inhibitor hygromycin B or α-sarcine, to which mock-infected cells were insensitive. However, little is known about whether any JEV nonstructural (NS) proteins contribute to virus-induced changes in membrane permeability. Using an inducibleEscherichia coli system, we investigated whi

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Jones, Daniel M., Arvind H. Patel, Paul Targett-Adams, and John McLauchlan. "The Hepatitis C Virus NS4B Protein Can trans-Complement Viral RNA Replication and Modulates Production of Infectious Virus." Journal of Virology 83, no. 5 (2008): 2163–77. http://dx.doi.org/10.1128/jvi.01885-08.

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ABSTRACT Studies of the hepatitis C virus (HCV) life cycle have been aided by development of in vitro systems that enable replication of viral RNA and production of infectious virus. However, the functions of the individual proteins, especially those engaged in RNA replication, remain poorly understood. It is considered that NS4B, one of the replicase components, creates sites for genome synthesis, which appear as punctate foci at the endoplasmic reticulum (ER) membrane. In this study, a panel of mutations in NS4B was generated to gain deeper insight into its functions. Our analysis identified

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Chatel-Chaix, Laurent, Wolfgang Fischl, Pietro Scaturro, et al. "A Combined Genetic-Proteomic Approach Identifies Residues within Dengue Virus NS4B Critical for Interaction with NS3 and Viral Replication." Journal of Virology 89, no. 14 (2015): 7170–86. http://dx.doi.org/10.1128/jvi.00867-15.

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ABSTRACTDengue virus (DENV) infection causes the most prevalent arthropod-borne viral disease worldwide. Approved vaccines are not available, and targets suitable for the development of antiviral drugs are lacking. One possible drug target is nonstructural protein 4B (NS4B), because it is absolutely required for virus replication; however, its exact role in the DENV replication cycle is largely unknown. With the aim of mapping NS4B determinants critical for DENV replication, we performed a reverse genetic screening of 33 NS4B mutants in the context of an infectious DENV genome. While the major

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Van Slyke, Greta A., Yongqing Jia, Melissa C. Whiteman, Jason A. Wicker, Alan D. T. Barrett, and Laura D. Kramer. "Vertebrate attenuated West Nile virus mutants have differing effects on vector competence in Culex tarsalis mosquitoes." Journal of General Virology 94, no. 5 (2013): 1069–72. http://dx.doi.org/10.1099/vir.0.049833-0.

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Previous mutational analyses of naturally occurring West Nile virus (WNV) strains and engineered mutant WNV strains have identified locations in the viral genome that can have profound phenotypic effect on viral infectivity, temperature sensitivity and neuroinvasiveness. We chose six mutant WNV strains to evaluate for vector competence in the natural WNV vector Culex tarsalis, two of which contain multiple ablations of glycosylation sites in the envelope and NS1 proteins; three of which contain mutations in the NS4B protein and an attenuated natural bird isolate (Bird 1153) harbouring an NS4B

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Fanunza, Elisa, Nicole Grandi, Marina Quartu, et al. "INMI1 Zika Virus NS4B Antagonizes the Interferon Signaling by Suppressing STAT1 Phosphorylation." Viruses 13, no. 12 (2021): 2448. http://dx.doi.org/10.3390/v13122448.

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The evasion of the Interferon response has important implications in Zika virus (ZIKV) disease. Mutations in ZIKV viral protein NS4B, associated with modulation of the interferon (IFN) system, have been linked to increased pathogenicity in animal models. In this study, we unravel ZIKV NS4B as antagonist of the IFN signaling cascade. Firstly, we reported the genomic characterization of NS4B isolated from a strain of the 2016 outbreak, ZIKV Brazil/2016/INMI1, and we predicted its membrane topology. Secondly, we analyzed its phylogenetic correlation with other flaviviruses, finding a high similar

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Lin, C., J. W. Wu, K. Hsiao, and M. S. Su. "The hepatitis C virus NS4A protein: interactions with the NS4B and NS5A proteins." Journal of virology 71, no. 9 (1997): 6465–71. http://dx.doi.org/10.1128/jvi.71.9.6465-6471.1997.

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Wölk, Benno, Domenico Sansonno, Hans-Georg Kräusslich, et al. "Subcellular Localization, Stability, andtrans-Cleavage Competence of the Hepatitis C Virus NS3-NS4A Complex Expressed in Tetracycline-Regulated Cell Lines." Journal of Virology 74, no. 5 (2000): 2293–304. http://dx.doi.org/10.1128/jvi.74.5.2293-2304.2000.

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ABSTRACT A tetracycline-regulated gene expression system and a panel of novel monoclonal antibodies were used to examine the subcellular localization, stability, and trans-cleavage competence of the hepatitis C virus (HCV) NS3-NS4A complex in inducible cell lines. The NS3 serine protease domain and the full-length NS3 protein expressed in the absence of the NS4A cofactor were diffusely distributed in the cytoplasm and nucleus. Coexpression of NS4A, however, directed NS3 to the endoplasmic reticulum (ER) or an ER-like modified compartment, as demonstrated by colocalization with 3,3′-dihexyloxac

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Suda, Yuto, Daisuke Yamane, Muhammad Atif Zahoor, et al. "Unique Localization of Bovine Viral Diarrhea Virus Non-Structural NS4B Protein in Infected Cells." JOURNAL OF ADVANCES IN AGRICULTURE 6, no. 1 (2016): 914–21. http://dx.doi.org/10.24297/jaa.v6i1.5396.

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Bovine viral diarrhea virus (BVDV), an important pathogen infecting ruminants, has 2 biotypes: cytopathic (cp) and noncytopathic (ncp), which are related to the onset of disease. The viral replication complex is composed of viral non-structural (NS) proteins, raising the possibility that NS protein(s) play a role in viral biotypes. To gain insight into this possible role, we analysed the intracellular localization of each NS protein in both cp and ncp virus-infected cells, and found that NS4B protein, a possible anchor protein of the viral replication complex, showed a unique dotted localizati

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Zou, J., X. Xie, L. T. Lee, et al. "Dimerization of Flavivirus NS4B Protein." Journal of Virology 88, no. 6 (2014): 3379–91. http://dx.doi.org/10.1128/jvi.02782-13.

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Gretton, Sarah N., Annette I. Taylor, and John McLauchlan. "Mobility of the hepatitis C virus NS4B protein on the endoplasmic reticulum membrane and membrane-associated foci." Journal of General Virology 86, no. 5 (2005): 1415–21. http://dx.doi.org/10.1099/vir.0.80768-0.

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The hepatitis C virus (HCV) non-structural protein NS4B induces morphological changes in the endoplasmic reticulum (ER) membrane that may have a direct role in viral RNA replication. A chimeric GFP–NS4B fusion protein located to the ER membrane and to foci that were attached to the ER. These membrane-associated foci (MAFs) could be related to the membrane alterations observed in cells that replicate HCV RNA. The relationship of MAFs to pre-existing cellular structures is not known. Indirect immunofluorescence analysis demonstrated that they did not contain a cellular marker for vesicles, which

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Pouliot, Jeffrey J., Michael Thomson, Mi Xie, et al. "Preclinical Characterization andIn VivoEfficacy of GSK8853, a Small-Molecule Inhibitor of the Hepatitis C Virus NS4B Protein." Antimicrobial Agents and Chemotherapy 59, no. 10 (2015): 6539–50. http://dx.doi.org/10.1128/aac.00813-15.

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ABSTRACTThe hepatitis C virus (HCV) NS4B protein is an antiviral therapeutic target for which small-molecule inhibitors have not been shown to exhibitin vivoefficacy. We describe here thein vitroandin vivoantiviral activity of GSK8853, an imidazo[1,2-a]pyrimidine inhibitor that binds NS4B protein. GSK8853 was active against multiple HCV genotypes and developedin vitroresistance mutations in both genotype 1a and genotype 1b replicons localized to the region of NS4B encoding amino acids 94 to 105. A 20-dayin vitrotreatment of replicons with GSK8853 resulted in a 2-log drop in replicon RNA levels

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Pascut, Devis, Minh Hoang, Nhu N. Q. Nguyen, Muhammad Yogi Pratama, and Claudio Tiribelli. "HCV Proteins Modulate the Host Cell miRNA Expression Contributing to Hepatitis C Pathogenesis and Hepatocellular Carcinoma Development." Cancers 13, no. 10 (2021): 2485. http://dx.doi.org/10.3390/cancers13102485.

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Hepatitis C virus (HCV) genome encodes for one long polyprotein that is processed by cellular and viral proteases to generate 10 polypeptides. The viral structural proteins include the core protein, and the envelope glycoproteins E1 and E2, present at the surface of HCV particles. Non-structural (NS) proteins consist of NS1, NS2, NS3, NS4A, NS4B, NS5a, and NS5b and have a variable function in HCV RNA replication and particle assembly. Recent findings evidenced the capacity of HCV virus to modulate host cell factors to create a favorable environment for replication. Indeed, increasing evidence

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Gouttenoire, Jérôme, Philippe Roingeard, François Penin та Darius Moradpour. "Amphipathic α-Helix AH2 Is a Major Determinant for the Oligomerization of Hepatitis C Virus Nonstructural Protein 4B". Journal of Virology 84, № 24 (2010): 12529–37. http://dx.doi.org/10.1128/jvi.01798-10.

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ABSTRACT Nonstructural protein 4B (NS4B) is a key organizer of hepatitis C virus (HCV) replication complex formation. It induces a specific membrane rearrangement, designated membranous web, that serves as a scaffold for the HCV replication complex. However, the mechanisms underlying membranous web formation are poorly understood. Based on fluorescence resonance energy transfer (FRET) and confirmatory coimmunoprecipitation analyses, we provide evidence for an oligomerization of NS4B in the membrane environment of intact cells. Several conserved determinants were found to be involved in NS4B ol

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Luo, Huanle, Guorui Xie, Michael Diamond, Michael Gale, Alan Barrett, and Tian Wang. "A West Nile virus NS4B P38G mutant induces MAVS-dependent type 1 interferon and the host anti-viral responses (INC1P.353)." Journal of Immunology 194, no. 1_Supplement (2015): 54.10. http://dx.doi.org/10.4049/jimmunol.194.supp.54.10.

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Abstract The nonstructural (NS) proteins of West Nile virus (WNV) are important determinants of viral pathogenesis. WNV NS4B-P38G mutant, which has a P38G substitution in the NS4B protein is highly attenuated in mice, but induces stronger type 1 interferon (IFN) and T cell responses than the wild-type WNV. Here, we investigated mice lacking the RIG-I-like receptor adaptor gene Mavs, and found increased viremia and lethality following WNV NS4B-P38G infection. MAVS-/- mice had a reduced IFNβ production and impaired primary T cell response after infection. WNV NS4B-P38G also induced lower levels

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Gu, Zhengxian, Jason D. Graci, Frederick C. Lahser, et al. "Identification of PTC725, an Orally Bioavailable Small Molecule That Selectively Targets the Hepatitis C Virus NS4B Protein." Antimicrobial Agents and Chemotherapy 57, no. 7 (2013): 3250–61. http://dx.doi.org/10.1128/aac.00527-13.

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ABSTRACTWhile new direct-acting antiviral agents for the treatment of chronic hepatitis C virus (HCV) infection have been approved, there is a continued need for novel antiviral agents that act on new targets and can be used in combination with current therapies to enhance efficacy and to restrict the emergence of drug-resistant viral variants. To this end, we have identified a novel class of small molecules, exemplified by PTC725, that target the nonstructural protein 4B (NS4B). PTC725 inhibited HCV 1b (Con1) replicons with a 50% effective concentration (EC50) of 1.7 nM and an EC90of 9.6 nM a

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Svitkin, Yuri V., Arnim Pause, Marcelo Lopez-Lastra, Sandra Perreault, and Nahum Sonenberg. "Complete Translation of the Hepatitis C Virus Genome In Vitro: Membranes Play a Critical Role in the Maturation of All Virus Proteins except for NS3." Journal of Virology 79, no. 11 (2005): 6868–81. http://dx.doi.org/10.1128/jvi.79.11.6868-6881.2005.

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ABSTRACT We developed an in vitro translation extract from Krebs-2 cells that translates the entire open reading frame of the hepatitis C virus (HCV) strain H77 and properly processes the viral protein precursors when supplemented with canine microsomal membranes (CMMs). Translation of the C-terminal portion of the viral polyprotein in this system is documented by the synthesis of NS5B. Evidence for posttranslational modification of the viral proteins, the N-terminal glycosylation of E1 and the E2 precursor (E2-p7), and phosphorylation of NS5A is presented. With the exception of NS3, efficient

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Fernandez-Sainz, I., D. P. Gladue, L. G. Holinka, et al. "Mutations in Classical Swine Fever Virus NS4B Affect Virulence in Swine." Journal of Virology 84, no. 3 (2009): 1536–49. http://dx.doi.org/10.1128/jvi.02050-09.

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ABSTRACT NS4B is one of the nonstructural proteins of classical swine fever virus (CSFV), the etiological agent of a severe, highly lethal disease of swine. Protein domain analysis of the predicted amino acid sequence of the NS4B protein of highly pathogenic CSFV strain Brescia (BICv) identified a putative Toll/interleukin-1 receptor (TIR)-like domain. This TIR-like motif harbors two conserved domains, box 1 and box 2, also observed in other members of the TIR superfamily, including Toll-like receptors (TLRs). Mutations within the BICv NS4B box 2 domain (V2566A, G2567A, I2568A) produced recomb

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Florese, Ruth H., Motoko Nagano-Fujii, Yasuhiro Iwanaga, Rachmat Hidajat, and Hak Hotta. "Inhibition of protein synthesis by the nonstructural proteins NS4A and NS4B of hepatitis C virus." Virus Research 90, no. 1-2 (2002): 119–31. http://dx.doi.org/10.1016/s0168-1702(02)00146-6.

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Casseb, Samir Mansour Moraes, Karla Fabiane Lopes de Melo, Carlos Alberto Marques de Carvalho, Carolina Ramos dos Santos, Edna Cristina Santos Franco, and Pedro Fernando da Costa Vasconcelos. "Experimental Dengue Virus Type 4 Infection Increases the Expression of MicroRNAs-15/16, Triggering a Caspase-Induced Apoptosis Pathway." Current Issues in Molecular Biology 45, no. 6 (2023): 4589–99. http://dx.doi.org/10.3390/cimb45060291.

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The World Health Organization has estimated the annual occurrence of approximately 392 million dengue virus (DENV) infections in more than 100 countries where the virus is endemic, which represents a serious threat to humanity. DENV is a serologic group with four distinct serotypes (DENV-1, DENV-2, DENV-3, and DENV-4) belonging to the genus Flavivirus, in the family Flaviviridae. Dengue is the most widespread mosquito-borne disease in the world. The ~10.7 kb DENV genome encodes three structural proteins (capsid (C), pre-membrane (prM), and envelope (E)) and seven non-structural (NS) proteins (

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Fernandez, Stefan, Emily D. Cisney, Alexander P. Tikhonov, et al. "Antibody Recognition of the Dengue Virus Proteome and Implications for Development of Vaccines." Clinical and Vaccine Immunology 18, no. 4 (2011): 523–32. http://dx.doi.org/10.1128/cvi.00016-11.

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ABSTRACTDengue is a mosquito-borne infection caused by four distinct serotypes of dengue virus, each appearing cyclically in the tropics and subtropics along the equator. Although vaccines are currently under development, none are available to the general population. One of the main impediments to the successful advancement of these vaccines is the lack of well-defined immune correlates of protection. Here, we describe a protein microarray approach for measuring antibody responses to the complete viral proteome comprised of the structural (capsid, membrane, and envelope) and nonstructural (NS1

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Gallinari, Paola, Debra Brennan, Chiara Nardi, et al. "Multiple Enzymatic Activities Associated with Recombinant NS3 Protein of Hepatitis C Virus." Journal of Virology 72, no. 8 (1998): 6758–69. http://dx.doi.org/10.1128/jvi.72.8.6758-6769.1998.

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ABSTRACT The hepatitis C virus (HCV) nonstructural 3 protein (NS3) contains at least two domains associated with multiple enzymatic activities; a serine protease activity resides in the N-terminal one-third of the protein, whereas RNA helicase activity and RNA-stimulated nucleoside triphosphatase activity are associated with the C-terminal portion. To study the possible mutual influence of these enzymatic activities, a full-length NS3 polypeptide of 67 kDa was expressed as a nonfusion protein in Escherichia coli, purified to homogeneity, and shown to retain all three enzymatic activities. The

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Oliver Koch, Jan, and Ralf Bartenschlager. "Modulation of Hepatitis C Virus NS5A Hyperphosphorylation by Nonstructural Proteins NS3, NS4A, and NS4B." Journal of Virology 73, no. 9 (1999): 7138–46. http://dx.doi.org/10.1128/jvi.73.9.7138-7146.1999.

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ABSTRACT NS5A of the hepatitis C virus (HCV) is a highly phosphorylated protein involved in resistance against interferon and required most likely for replication of the viral genome. Phosphorylation of this protein is mediated by a cellular kinase(s) generating multiple proteins with different electrophoretic mobilities. In the case of the genotype 1b isolate HCV-J, in addition to the basal phosphorylated NS5A (designated pp56), a hyperphosphorylated form (pp58) was found on coexpression of NS4A (T. Kaneko, Y. Tanji, S. Satoh, M. Hijikata, S. Asabe, K. Kimura, and K. Shimotohno, Biochem. Biop

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Egger, Denise, Benno Wölk, Rainer Gosert, et al. "Expression of Hepatitis C Virus Proteins Induces Distinct Membrane Alterations Including a Candidate Viral Replication Complex." Journal of Virology 76, no. 12 (2002): 5974–84. http://dx.doi.org/10.1128/jvi.76.12.5974-5984.2002.

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ABSTRACT Plus-strand RNA viruses characteristically replicate their genome in association with altered cellular membranes. In the present study, the capacity of hepatitis C virus (HCV) proteins to elicit intracellular membrane alterations was investigated by expressing, in tetracycline-regulated cell lines, a comprehensive panel of HCV proteins individually as well as in the context of the entire HCV polyprotein. As visualized by electron microscopy (EM), expression of the combined structural proteins core-E1-E2-p7, the NS3-4A complex, and protein NS4B induced distinct membrane alterations. By

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Gouttenoire, Jérôme, Roland Montserret, Audrey Kennel, François Penin та Darius Moradpour. "An Amphipathic α-Helix at the C Terminus of Hepatitis C Virus Nonstructural Protein 4B Mediates Membrane Association". Journal of Virology 83, № 21 (2009): 11378–84. http://dx.doi.org/10.1128/jvi.01122-09.

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ABSTRACT Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is an integral membrane protein that has been only poorly characterized to date. It is believed to comprise a cytosolic N-terminal part, a central part harboring four transmembrane passages, and a cytosolic C-terminal part. Here, we describe an amphipathic α-helix at the C terminus of NS4B (amino acid residues 229 to 253) that mediates membrane association and is involved in the formation of a functional HCV replication complex.

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