Mumps virus cDNA and Antigen

Mumps virus is a single-stranded RNA virus that causes an illness characterized by fever, headache, and swollen salivary glands. The virus has several key proteins that are critical to its replication and pathogenicity, including the membrane protein, hemagglutinin-neuraminidase, and nucleoprotein.

The nucleoprotein of the Mumps virus is the most abundant protein in the viral particle and plays a key role in virus replication and transcription. It binds to the viral RNA genome, forming the ribonucleoprotein complex that is responsible for virus replication and transcription.

The membrane protein, also known as the matrix protein, plays an important role in the assembly and budding of the virus. It is responsible for stabilizing the virus envelope and interacting with other viral proteins during viral assembly.

The hemagglutinin-neuraminidase is a glycoprotein that is involved in the binding of the virus to host cells and the cleavage of sialic acid residues. It is also responsible for the fusion of the virus with the host cell membrane, allowing for viral entry and replication.

The nucleoprotein is a highly conserved protein that binds to the viral RNA and plays an important role in the replication and transcription of the virus. It is involved in the formation of the ribonucleoprotein complex, which is essential for viral replication.

Understanding the functions of these important proteins is crucial for the development of effective treatments and vaccines for mumps virus.

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.