Dengue-2 C-terminal

Dengue virus (DENV) is a significant global health concern, with millions of infections occurring annually. The virus is transmitted by Aedes mosquitoes and can cause severe diseases such as dengue fever, dengue hemorrhagic fever, and dengue shock syndrome. There are four serotypes of the dengue virus (DENV-1, DENV-2, DENV-3, and DENV-4), each capable of causing disease. The envelope (E) protein of the dengue virus plays a crucial role in the virus’s ability to infect host cells and is a primary target for vaccine development.

The envelope protein of the dengue virus is a glycoprotein that mediates the virus’s entry into host cells. It is composed of three domains: domain I (DI), domain II (DII), and domain III (DIII). The hydrophobic domain of the envelope protein is particularly important for the fusion of the viral membrane with the host cell membrane, a critical step in the viral infection process. The E protein forms homodimers on the surface of the virus, and these dimers undergo significant conformational changes during the fusion process.

Recombinant technology has enabled the production of dengue virus envelope proteins in various expression systems. Recombinant proteins are produced by inserting the gene encoding the protein of interest into a host organism, such as bacteria, yeast, or mammalian cells. This technology allows for the large-scale production of proteins that are identical or similar to those found in the virus, facilitating research and vaccine development.

The Dengue-2 Envelope Hydrophobic Domain Recombinant refers to a recombinant form of the hydrophobic domain of the envelope protein from the DENV-2 serotype. This recombinant protein is used in various research applications, including the study of viral entry mechanisms, the development of diagnostic tools, and the creation of vaccines.

One of the primary applications of the Dengue-2 Envelope Hydrophobic Domain Recombinant is in vaccine development. Traditional vaccine approaches, such as live-attenuated or inactivated vaccines, have faced challenges in providing balanced protection against all four dengue serotypes. Recombinant subunit vaccines, which use specific viral proteins rather than whole viruses, offer a promising alternative. The recombinant envelope protein can be engineered to enhance its immunogenicity and stability, making it a suitable candidate for vaccine development .

Recent studies have focused on improving the expression and stability of recombinant dengue envelope proteins. For example, researchers have designed mutations in the DENV-2 envelope protein that promote dimerization and enhance production yield. These stabilized dimers have been shown to elicit higher levels of neutralizing antibodies in animal models compared to wild-type envelope proteins . Additionally, novel adjuvants and delivery systems are being explored to further enhance the immune response to recombinant dengue vaccines .