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AntibodySystem
Recombinant Proteins
Recombinant DENV-2 Envelope protein E is a key component of the Dengue virus, which is a mosquito-borne virus that causes Dengue fever. The Dengue virus has four distinct serotypes (DENV-1, DENV-2, DENV-3, and DENV-4) and the Envelope protein E is a major antigenic component of all four serotypes. In this article, we will discuss the structure, activity, and application of Recombinant DENV-2 Envelope protein E.
The Envelope protein E is a glycoprotein that is found on the surface of the Dengue virus. It is a type I transmembrane protein that consists of three domains: domain I, II, and III. Domain I and II are located on the outer surface of the virus, while domain III is buried within the viral envelope. The protein has a molecular weight of approximately 50 kDa and is composed of 495 amino acids.
Domain I is the central domain of the Envelope protein E and is responsible for receptor binding and fusion with the host cell membrane. It is composed of 80 amino acids and contains a highly conserved fusion loop that is essential for viral entry into the host cell.
Domain II is the dimerization domain of the Envelope protein E and is responsible for the formation of the viral envelope. It consists of 50 amino acids and is highly conserved among all four serotypes of Dengue virus.
Domain III is the immunoglobulin-like domain of the Envelope protein E and is responsible for eliciting neutralizing antibodies. It is composed of 175 amino acids and contains the majority of the antigenic sites of the protein.
The Envelope protein E plays a crucial role in the pathogenesis of Dengue virus infection. It is involved in viral entry into the host cell and is a major target for neutralizing antibodies. The fusion loop of domain I is responsible for binding to the host cell receptor, while domain III is responsible for eliciting neutralizing antibodies.
The Envelope protein E binds to the host cell receptor, which is a protein called DC-SIGN, through its fusion loop in domain I. This interaction triggers a conformational change in the protein, exposing domain II, which then mediates fusion between the viral and host cell membranes.
Domain III of the Envelope protein E contains the majority of the antigenic sites of the protein. These sites are targeted by neutralizing antibodies, which prevent the virus from entering the host cell and causing infection. This makes the Envelope protein E a key target for vaccine development against Dengue virus.
Recombinant DENV-2 Envelope protein E has several applications in the field of Dengue virus research and vaccine development.
The Envelope protein E is a major target for vaccine development against Dengue virus. Recombinant forms of the protein can be produced in large quantities and used to elicit neutralizing antibodies in the host, providing protection against infection.
Recombinant DENV-2 Envelope protein E can also be used as a diagnostic tool for Dengue virus infection. Antibodies against the protein can be used to detect the presence of the virus in patient samples, allowing for early diagnosis and treatment.
The Envelope protein E is also a valuable tool for studying the structure and function of the Dengue virus. Recombinant forms of the protein can be used in various experiments to understand the mechanisms of viral entry and the role of the protein in
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