Murray Valley encephalitis virus cDNA and Antigen

Murray Valley encephalitis virus (MVEV) is a flavivirus that is found in Australia and Papua New Guinea. It is transmitted to humans through the bite of infected mosquitoes and can cause severe neurological disease, including encephalitis.

The envelope protein is a key component of the MVEV virion and is responsible for facilitating the virus’s entry into host cells. It is also a target for the immune system’s response to the virus.

Protein C is a non-structural protein that plays a role in viral replication by inhibiting host cell translation and promoting viral protein synthesis. It also interacts with host proteins to modulate the immune response.

The envelope protein E is another key component of the MVEV virion and is involved in viral entry and fusion with host cell membranes. It is also a target for the immune system’s response to the virus.

Non-structural protein 1 (NS1) and 2a (NS2a) are involved in viral replication and the formation of the viral replication complex. NS1 also plays a role in immune evasion by inhibiting the complement pathway.

Serine protease subunit NS2B is part of the viral replication complex and is essential for the proteolytic processing of viral polyproteins. It is a target for antiviral drug development.

Research on MVEV and its key components, including the envelope protein, protein C, envelope protein E, non-structural protein 1 and 2a, and serine protease subunit NS2B, is ongoing. While there is currently no specific treatment for MVEV infection, understanding the mechanisms of viral replication and immune evasion may help in the development of antiviral therapies and vaccines.

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.