DENV type 4 Envelope protein [His] (DAG459)

DENV type 4 Envelope protein [His], recombinant protein from E. coli

Product Overview
Recombinant Dengue Type-4 Envelope contains a common antigen for Dengue type 1, 2 and 3 and contains a 6-His fusion partner, was expressed in E. coli. Recombinant Dengue Type-4 Envelope can reacts strongly with Dengue IgG, and can reacts with Dengue IgM i
> 95% pure (10% PAGE (Coomassie)). Proprietary chromatographic technique
Purified, Liquid
1.78 mg/ml
PBS, pH 7.4
2-8°C short term, -20°C long term
Dengue virus (DENV) in one of four serotypes is the cause of dengue fever. It is a mosquito-borne single positive-stranded RNA virus of the family Flaviviridae; genus Flavivirus. All four serotypes can cause the full spectrum of disease. Its genome is about 11000 bases that codes for three structural proteins, capsid protein C, membrane protein M, envelope protein E; seven nonstructural proteins, NS1, NS2a, NS2b, NS3, NS4a, NS4b, NS5; and short non-coding regions on both the 5' and 3' ends. Further classification of each serotype into genotypes often relates to the region where particular strains are commonly found or were first found.
DENV; Dengue Virus Envelope Protein; DENV Envelope Protein; Dengue virus


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A MVA construct expressing a secretable form of the Dengue virus 3 envelope protein protects immunized mice from dengue-induced encephalitis


Authors: Quinan, Barbara R.; Versiani, Alice Freitas; da Fonseca, Flavio G.

Dengue is no longer restricted to tropical developing countries, but is now a major global public health problem. Despite the recent license approval of the CYD-TDV vaccine in some countries, efforts to develop a more efficient vaccine against Dengue virus (DENV) continue. Herein, we evaluate the immunogenicity and level of protection of two potential vaccines against DENV based on recombinant modified vaccinia virus Ankara (rMVA). The vaccine addressing the Envelope protein from DENV serotype 3 to the endoplasmic reticulum elicited neutralizing antibodies titers which correlate with protection, and also confers protection upon challenge in a mouse model. Our results support the development of a tetravalent dengue vaccine with the further construction of rMVAs expressing proteins from the other DENV serotypes. (C) 2016 Elsevier Ltd. All rights reserved.

Surface proteins of C6/36 cells involved in dengue virus 4 binding and entry


Authors: Olivia Vega-Almeida, Tania; Salas-Benito, Mariana; Ascension De Nova-Ocampo, Monica; Maria del Angel, Rosa; Santiago Salas-Benito, Juan

Dengue virus (DENV) is the causative agent of the most important mosquito-borne viral disease, which is endemic to over 100 countries in tropical and subtropical areas of the world. It is transmitted to humans by Aedes mosquitoes. The first step in the viral infection of host cells is virion attachment to the plasma membrane, which is mediated by specific surface molecules. There are several molecules that participate in DENV infection of mosquitoes, but only a few have been identified. In this work, we co-purified 4 proteins from C6/36 cells using a recombinant DENV 4 E protein and identified them as 70 kDa Heat Shock and 70 kDa Heat Shock cognate proteins (HSP70/HSc70), Binding immunoglobulin protein (BiP), Thioredoxin/protein disulphide isomerase (PDI), and 44 kDa Endoplasmic reticulum resident protein (ERp44) via matrix-assisted laser desorption/ionisation time of flight (Maldi-ToF) analysis. Using immunofluorescence and flow cytometry assays, we observed re-localisation of HSP70/HSc70 and, to a lesser extent, BiP to the plasma membrane under stress conditions, such as during DENV infection. By performing binding and infection assays independently, we found that all 4 proteins participate in both processes, but to differing extents: HSP70/HSc70 is the most critical component, while ERp44 is less important. Viral infection was not inhibited when the cells were incubated with antibodies against all of the surface proteins after virus binding, which suggests that DENV entry to C6/36 cells is mediated by these proteins at the same step and not sequentially.

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