Purified by proprietary chromatographic technique
Dengue fever is a mosquito-borne viral infection caused by one of four closely related viruses, known as serotypes, within the genus Flavivirus and family Flaviviridae. These serotypes are designated as Dengue Virus 1 (DV1), Dengue Virus 2 (DV2), Dengue Virus 3 (DV3), and Dengue Virus 4 (DV4). Infection with one serotype provides lifelong immunity to that specific serotype but only partial and temporary immunity to the others .
The envelope (E) glycoprotein of the dengue virus plays a crucial role in the virus’s life cycle. It mediates the attachment of the virion to the host cell receptor and facilitates the fusion of the viral envelope with the target cell membrane . The E protein is also a major target for neutralizing antibodies, making it a key component in vaccine development and diagnostic assays.
The recombinant Dengue Virus Subtype 1 Envelope 45kDa protein is a laboratory-produced version of the E protein specific to DV1. This recombinant protein is typically produced in Escherichia coli (E. coli) and includes important epitopes for dengue antibody recognition. It is often fused to a 6xHis tag to facilitate purification and detection .
The recombinant DV1 E protein is expressed in E. coli and purified using proprietary chromatographic techniques. The protein is greater than 95% pure, as determined by 10% PAGE (coomassie staining) . It is formulated in phosphate-buffered saline with 25mM arginine to maintain stability. Although stable at 4°C for one week, it should be stored below -18°C to prevent freeze-thaw cycles .
The recombinant DV1 E protein is used in various diagnostic assays, including lateral flow and ELISA assays, to detect dengue-specific antibodies. It is suitable for gold conjugation and has been tested for strong reactivity with Dengue IgG and IgM antibodies . These applications are crucial for the rapid and accurate diagnosis of dengue infections, which is essential for effective patient management and control of outbreaks.
Research has identified specific epitopes on the DV1 E protein that are recognized by neutralizing monoclonal antibodies (mAbs). For instance, two mAbs, DV1-E1 and DV1-E2, have shown strong binding specificity and neutralizing activity against DV1. These mAbs target a unique epitope on the later-ridge of domain III of the DV1 E protein, centered near residues T346 and D360 . This epitope is highly conserved among different genotypes of DV1 but varies significantly from other dengue serotypes and flaviviruses .