Rinderpest virus cDNA and Antigen

Rinderpest virus, also known as cattle plague virus, is a highly contagious viral disease that affects cattle and other ruminants. The virus is known for causing devastating epidemics in the past but has now been eradicated through a successful global vaccination campaign. The virus is composed of several proteins, including:

Nucleoprotein (N): This protein forms the helical nucleocapsid that contains the viral RNA.

Hemagglutinin: A surface glycoprotein that mediates the attachment of the virus to host cells.

Protein C: A non-structural protein that is involved in viral replication and assembly.

Hemagglutinin glycoprotein: A type II transmembrane protein that forms spikes on the viral surface.

Matrix protein: A structural protein that lines the inner surface of the viral envelope and plays a role in virus assembly and budding.

Non-structural protein V: A viral protein that is involved in suppressing host immune responses.

Fusion glycoprotein F0: A viral surface glycoprotein that is responsible for mediating fusion between the viral envelope and host cell membranes.

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.