DENV type 3 Nonstructural Protein 1 (DAG3064)

DENV type 3 Nonstructural Protein 1 (aa 775-1129), recombinant protein from Baculovirus

Product Overview
Recombinant Dengue Type 3 NS1 Protein
Nature
Recombinant
Tag/Conjugate
Unconjugated
Procedure
5 mM EDTA
Purity
≥ 95% on 12.5% SDS-PAGE
Concentration
≥ 1 mg/ml by Bradford dye assay
Buffer
1X PBS, pH7.4
Preservative
0.1% Thimerosal
Storage
2-8°C short term, -20°C long term
Introduction
NS1 is one of 7 Dengue Virus non-structural proteins which are thought to be involved in viral replication. NS1 exists as a monomer in its immature form but is rapidly processed in the endoplasmic reticulum to form a stable dimer. A small amount of NS1 remains associated with intracellular organelles where it is thought to be involved in viral replication. The rest of NS1 is found either associated with the plasma membrane or secreted as a soluble hexadimer. NS1 is essential for viral viability but its precise biological function is unknown. Antibodies raised in response to NS1 in viral infection can cross react with cell surface antigens on epithelial cells and platelets and this has been implicated in the development of Dengue Hemorrhagic fever.
Keywords
Dengue NS1; Dengue Virus non-structural protein 1; Dengue Virus NS1 glycoprotein; DENV NS1

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References


Dataset of proteins mapped on HepG2 cells and those differentially abundant after expression of the dengue non-structural 1 protein

DATA IN BRIEF

Authors: Rabelo, Kissila; Trugilho, Monique R. O.; Costa, Simone M.; Ferreira, Andre T. S.; Carvalho, Paulo C.; Perales, Jonas; Alves, Ada M. B.

The data supplied in this article are related to the research article entitled "The effect of the dengue non-structural 1 protein expression over the HepG2 cell proteins in a proteomic approach" (K. Rabelo, M.R. Trugillo, S.M. Costa, B.A. Pereira, O.C. Moreira, A.T. Ferreira et al., 2016) [11. The present article provides the inventory of peptides and proteins mapped in a hepatocyte cell line (HepG2) by mass spectrometry in the presence of the non-structural protein 1 (NS1) of Dengue 2 virus (DENV2). Cells were transfected with pcENS1 plasmid, which encodes the DENV2 NS1 protein, or the controls pcDNA3 (negative control) or pMAXGFP, encoding the green fluorescent protein (GFP), a protein unrelated to dengue. Differentially abundant protein lists were obtained by comparing cells transfected with pcENS1 and controls. (C) 2016 The Authors. Published by Elsevier inc. This is an open access article under the CC BY license.

Characterization of in vitro dengue virus resistance to carrageenan

JOURNAL OF MEDICAL VIROLOGY

Authors: Talarico, Laura B.; Damonte, Elsa B.

The -carrageenan (-car) is a potent and selective inhibitor of dengue virus (DENV) infection targeted to virus adsorption and internalization, due to the structural similarities with the mammalian cell receptor heparan sulfate. To further characterize the antiviral activity of -car, the selection and the phenotypic and genomic features of -car resistant DENV-2 variants are studied here in comparison to control virus. Resistant variants were rapidly selected in Vero cells after three passages in presence of the drug. No difference was detected in the growth profiles in Vero and C6/36 cells between resistant and control viruses. By contrast, the kinetics of adsorption and internalization of resistant variants in Vero cells was significantly diminished whereas entry to C6/36 cells was unaffected. By plaque purification and sequence analysis of the population, two types of resistant clones were found: some clones presented two mutations in E protein, K126E, and F422L; but other equally -car resistant clones had no mutations in E. Furthermore, no mutations were found in other viral proteins like prM, C, or NS1. The genomic disparity in E protein was also associated to differences in phenotype stability. The stable genomic resistance here described provides information about determinants in E protein involved in receptor binding and membrane fusion for uncoating. J. Med. Virol. 88:1120-1129, 2016. (c) 2016 Wiley Periodicals, Inc.

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