The E.Coli derived Recombinant Zika Envelope protein 40-400 a.a. having an Mw of 45kDa. The Zika Envelope full length protein without a C-terminal hydrophobic region.
The Zika Envelope full length protein is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.
Zika virus (ZIKV) is an arthropod-borne virus belonging to the family Flaviviridae and the genus Flavivirus. It was first identified in a rhesus monkey in the Zika forest of Uganda in 1947 . ZIKV is primarily transmitted through the bite of infected Aedes mosquitoes, but it can also be transmitted through sexual contact, blood transfusion, and from mother to fetus during pregnancy .
The envelope (E) protein is a crucial component of the Zika virus. It is responsible for virus attachment, entry into host cells, and fusion of the viral and cellular membranes . The E protein is the major target for neutralizing antibodies, making it a critical component for vaccine development . The full-length E protein consists of three domains: domain I (DI), domain II (DII), and domain III (DIII). These domains play essential roles in the virus’s ability to infect host cells and evade the immune system .
Recombinant Zika Envelope Full Length Protein is produced using various expression systems, including mammalian cells, insect cells, and bacterial cells . The recombinant protein is designed to mimic the native structure of the viral E protein, allowing it to be used in research, diagnostics, and vaccine development .
The production of recombinant Zika Envelope Protein involves the use of gene expression constructs that include the prM (precursor membrane) and E genes. These constructs are optimized to enhance protein expression and secretion in the chosen expression system . For example, in mammalian HEK293 cells, the C-terminus transmembrane domain of the E protein can be replaced with a rat CD4 domain to improve protein solubility and yield . The resulting recombinant protein can be purified and used in various applications, such as enzyme-linked immunosorbent assays (ELISAs) and vaccine development .
Recombinant Zika Envelope Protein is widely used in research to study the immune response to Zika virus infection and to develop diagnostic assays . It is also a key component in the development of Zika virus vaccines. Several vaccine candidates based on the E protein have shown promise in preclinical and clinical studies . These vaccines aim to induce a robust immune response that can neutralize the virus and prevent infection .
One of the challenges in using recombinant Zika Envelope Protein for vaccine development is the potential for antibody-dependent enhancement (ADE) of infection. ADE occurs when non-neutralizing antibodies facilitate viral entry into host cells, leading to increased viral replication and disease severity . To address this issue, researchers are exploring modifications to the E protein, such as mutations in the conserved fusion loop, to reduce cross-reactivity and enhance vaccine safety .
In conclusion, the recombinant Zika Envelope Full Length Protein plays a vital role in advancing our understanding of Zika virus biology and in the development of effective diagnostics and vaccines. Continued research and optimization of this protein will be essential in the fight against Zika virus and other related flaviviruses.