Purified by proprietary chromatographic technique.
Dengue virus (DENV) is a mosquito-borne pathogen belonging to the Flaviviridae family. It is transmitted to humans primarily through the bites of infected Aedes aegypti and Aedes albopictus mosquitoes. There are four antigenically distinct serotypes of dengue virus (DENV-1, DENV-2, DENV-3, and DENV-4), each capable of causing dengue fever, dengue hemorrhagic fever, and dengue shock syndrome .
The envelope (E) protein of the dengue virus is a critical component of the viral structure and plays a significant role in the virus’s ability to infect host cells. The E protein is responsible for binding to host cell receptors and facilitating the fusion of the viral and host cell membranes, allowing the virus to enter the host cell . The E protein is also a major target for the host immune response, as it induces the production of neutralizing antibodies that can protect against infection .
The E protein is composed of three domains: DI, DII, and DIII. Domain III (EDIII) is of particular interest because it contains epitopes that are recognized by neutralizing antibodies. This makes EDIII a promising candidate for vaccine development and diagnostic applications . The EDIII of DENV-3 has been extensively studied for its potential to induce a protective immune response and its use in recombinant protein production .
Recombinant production of the EDIII protein involves the use of various expression systems to produce the protein in large quantities. One such system is the yeast Pichia pastoris, which has been optimized for the secretory over-expression of DENV-3 EDIII . The production process involves the use of a methanol-inducible promoter (AOX1) and the supplementation of culture media with casamino acids (CA) to enhance the secretion of the recombinant protein . This method has been shown to significantly increase the yield of EDIII, making it suitable for research and industrial applications .
The recombinant EDIII protein has several important applications: