Rift valley fever virus cDNA and Antigen

Rift Valley fever virus (RVFV) is a species of Phlebovirus in the genus Phlebovirus. It is an insect-borne virus that is primarily transmitted by mosquitoes. It can cause a range of symptoms in humans, including fever, headache, nausea, vomiting, abdominal pain, and joint pain. In severe cases, it can cause encephalitis, meningoencephalitis, and retinitis. It is also known to cause abortions in pregnant women and can cause death in young children and the elderly. In livestock, RVFV can cause a high mortality rate, and can have a major economic impact.

Rift Valley fever virus antigen is a protein found on the surface of the Rift Valley fever virus. It is used in diagnostics to detect the presence of the virus in a sample. The antigen is also used in vaccines to help the body build immunity to the virus.

Rift Valley fever virus (RVFV) is a mosquito-borne virus that causes severe disease in humans and livestock. The RVFV genome is a single-stranded, positive-sense RNA genome that is approximately 12.2 kb in length. It contains three open reading frames (ORFs) encoding the non-structural proteins NSs, NSm, and NSm2, as well as seven structural proteins including the glycoprotein precursor, the nucleocapsid protein, the matrix protein, and the envelope proteins Gn and Gc.The virus is comprised of several important proteins, including:

Nucleocapsid protein: The nucleocapsid is a helical ribonucleoprotein complex that encapsidates the viral genome and plays a key role in viral RNA synthesis and replication.

Non-structural protein: The non-structural protein plays a critical role in viral replication, inhibits the host’s innate immune response, and enhances viral pathogenesis.

Glycoprotein G1 and G2: The glycoprotein G1 and G2 are surface proteins that play a key role in viral attachment and entry into host cells.

Understanding the structure and function of these proteins is critical to the development of effective treatments and vaccines for Rift Valley Fever.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.