Dengue Envelope-2 22kDa
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
Description
The E.coli derived recombinant 22 kDa protein is genetically engineered peptide which is derived from Dengue Type-2 Envelope. This region also contains a common antigen for Dengue IgG & IgM. This protein is fused to 6xHis tag.
Product Specs
Purified by proprietary chromatographic technique.
Product Science Overview
The Dengue Virus (DENV) is a mosquito-borne virus that causes dengue fever, a significant public health concern in tropical and subtropical regions. There are four serotypes of the virus, namely DENV-1, DENV-2, DENV-3, and DENV-4. Each serotype can cause the full spectrum of disease, from mild dengue fever to severe 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 vital role in the virus’s ability to infect host cells. The E protein is responsible for mediating the fusion of the viral membrane with the host cell membrane, a crucial step in the viral entry process. The E protein is also the primary target for neutralizing antibodies, making it a key focus for vaccine development.
The E protein is composed of three domains: domain I (DI), domain II (DII), and domain III (DIII). These domains are involved in various functions, including receptor binding and membrane fusion. The E protein exists as a homodimer on the surface of the mature virion, and this dimerization is essential for its function.
The recombinant 22kDa envelope protein of Dengue Virus Subtype-2 (DENV-2) is a genetically engineered peptide derived from the E protein. This recombinant protein is produced in E. coli and is fused to a 6xHis tag to facilitate purification. The 22kDa protein represents a specific region of the E protein that contains common antigens for DENV-2, DENV-3, and DENV-4 .
The recombinant 22kDa envelope protein is of significant interest in the development of dengue vaccines. Traditional live-attenuated vaccines have faced challenges due to uneven replication of vaccine virus strains, leading to a dominant immune response to one serotype and weaker responses to the others . Protein subunit vaccines, such as those based on the recombinant E protein, offer a promising alternative as antigen dosing can be precisely controlled.
Recent studies have shown that stabilized DENV-2 E protein homodimers can stimulate higher levels of neutralizing antibodies compared to the wild-type E antigen . These findings highlight the potential of recombinant E proteins in eliciting a robust and broad immune response, making them valuable candidates for subunit vaccine development.
