Montana myotis leukoencephalitis virus cDNA and Antigen

Montana myotis leukoencephalitis virus (MMLV) is a virus that belongs to the Flaviviridae family. The virus has a positive-sense single-stranded RNA genome and is primarily transmitted to bats by the bite of infected insects such as mosquitoes and ticks. The virus has been known to cause leukoencephalitis in bats.

The MMLV genome encodes for several proteins, including the capsid protein, envelope protein, and nonstructural proteins (1, 4A, 4B, and 2B). The capsid protein is involved in the packaging of the viral genome, while the envelope protein is responsible for the attachment and entry of the virus into host cells. The nonstructural proteins play a variety of roles in the replication and assembly of the virus. Nonstructural protein 1, for example, is involved in viral replication and pathogenesis, while nonstructural protein 4A has been shown to inhibit host cell protein synthesis. Nonstructural protein 4B is involved in the formation of viral replication complexes, and nonstructural protein 2B is involved in the rearrangement of intracellular membranes during viral replication.

Overall, understanding the various proteins encoded by the MMLV genome is important for developing strategies to control the spread of this virus and for developing treatments for associated diseases.

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.