Dengue Type 2 EP Recombinant Dengue Type 2 Envelope Protein (EP) (a.a. 281-675) Recombinant Product contains Histidine tag. Molecular Weight: ~50 kDa
Nature
Recombinant
Tag/Conjugate
His
Molecular Weight
50 kDa
Alternative Names
Flaviviridae; Flavivirus; Dengue virus; Dengue Virus Type 2; DENV; DENV EP; Dengue virus envelope protein E; Dengue virus envelope glycoprotein E; DENV Type 2 EP; DENV-2 EP
Purity
> 85% Pure (SDS-PAGE).
Format
Purified, Liquid
Concentration
Batch dependent - please inquire should you have specific requirements
Buffer
Phosphate Buffered Saline, pH 7.4
Preservative
0.09% Sodium Azide
Storage
Store at -20°C
Antigen Description
Dengue virus is a major threat to health in tropical countries around the world. It is limited primarily to the tropics because it is transmitted by a tropical mosquito, but even with this limitation, 50-100 million people are infected each year. Dengue virus enters a host cell when the viral envelope glycoprotein, E, binds to a receptor and responds by conformational rearrangement to the reduced pH of an endosome. The conformational change induces fusion of viral and host-cell membranes.
Keywords
Flaviviridae;Flavivirus;Dengue virus;Dengue Virus Type 2;DENV;DENV EP;Dengue virus envelope protein E;Dengue virus envelope glycoprotein E;DENV Type 2 EP;DENV-2 EP
Inactivation
Not Applicable
Citations
Publication ()
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Background
Dengue virus (DENV) is a member of the Flaviviridae family, and it is characterized by its enveloped structure and single-stranded, positive-sense RNA genome. The virus consists of four distinct serotypes, namely DENV1, DENV2, DENV3, and DENV4, which share similarities but also exhibit differences in their genetic makeup and antigenic properties. DENV produces three structural proteins (capsid (C) protein, membrane (M) protein, and envelope (E) protein) and seven non-structural proteins (NS1, -2a, -2b, -3, -4a, -4b, and -5).
Figure 1. The Dengue virus (DENV) structure and genome. (A) General structure of DENV. (B) Genomic organization of DENV. (Source: Panda, K. et al., 2021)
The envelope glycoprotein, also known as E protein, plays a crucial role in the viral life cycle and host interactions. It is responsible for mediating the attachment of the virus to specific receptors on the surface of target cells. It facilitates the initial interaction between the viral particle and the host cell, allowing the virus to gain entry into the cell. Additionally, the E protein is involved in the fusion of the viral envelope with the target cell membrane, enabling the release of the viral genetic material into the host cell cytoplasm. Due to its critical functions in viral entry and fusion, the DENV E protein is a primary target for the host immune response. It elicits the production of neutralizing antibodies, which can prevent viral attachment and entry into susceptible cells. The E protein also contains immunodominant epitopes that can be targeted by the host immune system, leading to the generation of specific antibodies. In diagnostic settings, the recombinant DENV E protein has been employed in various assays to detect the presence of dengue infection. These assays utilize the recombinant E protein to detect either primary or secondary dengue infections in patient samples. By using the recombinant protein, potential safety concerns associated with the use of whole virus preparations can be addressed. The recombinant DENV E protein has also been extensively studied as a candidate antigen for dengue vaccines. It has been incorporated into vaccine formulations to elicit a protective immune response against dengue infection. Vaccines based on the E protein aim to induce the production of neutralizing antibodies, which can effectively target and neutralize the virus upon subsequent exposure.
Alternative Names
Recombinant DENV Type 2 EP Recombinant DENV Type 2 Envelope Protein Recombinant Dengue Virus Type 2 Envelope Protein Dengue Type 2 Envelope Protein (EP) (aa 281-675) Recombinant Dengue Type 2 EP Recombinant
References
1. Panda K, et al. Oligonucleotide-based approaches to inhibit dengue virus replication. Molecules. 2021, 26(4): 956.
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References
Dengue Virus Type 2: Protein Binding and Active Replication in Human Central Nervous System Cells
The Scientific World Journal
Authors: Salazar M I, Pérez-García M, Terreros-Tinoco M, et al.
An increased number of dengue cases with neurological complications have been reported in recent years. The lack of reliable animal models for dengue has hindered studies on dengue virus (DENV) pathogenesis and cellular tropism in vivo. We further investigate the tropism of DENV for the human central nervous system (CNS), characterizing DENV interactions with cell surface proteins in human CNS cells by virus overlay protein binding assays (VOPBA) and coimmunoprecipitations. In VOPBA, three membrane proteins (60, 70, and 130 kDa) from the gray matter bound the entire virus particle, whereas only a 70 kDa protein bound in white matter. The coimmunoprecipitation assays revealed three proteins from gray matter consistently binding virus particles, one clearly distinguishable protein (~32 kDa) and two less apparent proteins (100 and 130 kDa). Monoclonal anti-NS3 targeted the virus protein in primary cell cultures of human CNS treated with DENV-2, which also stained positive for NeuH, a neuron-specific marker. Thus, our results indicate (1) that DENV-2 exhibited a direct tropism for human neurons and (2) that human neurons sustain an active DENV replication as was demonstrated by the presence of the NS3 viral antigen in primary cultures of these cells treated with DENV-2.
Identification of novel target sites and an inhibitor of the dengue virus E protein
Journal of Computer-Aided Molecular Design
Authors: Yennamalli R, Subbarao N, Kampmann T, et al.
Dengue and related flaviviruses represent a significant global health threat. The envelope glycoprotein E mediates virus attachment to a host cell and the subsequent fusion of viral and host cell membranes. The fusion process is driven by conformational changes in the E protein and is an essential step in the virus life cycle. In this study, we analyzed the pre-fusion and post-fusion structures of the dengue virus E protein to identify potential novel sites that could bind small molecules, which could interfere with the conformational transitions that mediate the fusion process. We used an in silico virtual screening approach combining three different docking algorithms (DOCK, GOLD and FlexX) to identify compounds that are likely to bind to these sites. Seven structurally diverse molecules were selected to test experimentally for inhibition of dengue virus propagation. The best compound showed an IC50 in the micromolar range against dengue virus type 2.
COA
Publication 
Figure 1. The Dengue virus (DENV) structure and genome. (A) General structure of DENV. (B) Genomic organization of DENV.![The purity of Recombinant DENV type 4 NS2B-NS3 (Fragment) [His] >85%, determined by SDS-PAGE](https://resource.creative-diagnostics.com/diagnostics/productimages-1/DAGA-1069-1.jpg)
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