San Miguel Sea Lion Virus cDNA and Antigen

San Miguel sea lion virus (SMSV) is a calicivirus that primarily infects sea lions. The virus has several important proteins that play a critical role in viral replication and pathogenesis.

Capsid is the outer shell of the virus that protects the viral genome during transmission. It is composed of many copies of a single protein, Capsid protein VP1, which is responsible for the structural integrity of the capsid.

Protein p16, p30, and p32 are non-structural proteins of SMSV that are involved in the regulation of viral gene expression and replication. These proteins play critical roles in the early stages of viral infection and are required for the virus to successfully replicate in host cells.

SMSV-1 Viral genome-linked protein is a viral protein that is covalently linked to the viral RNA genome. This protein is involved in viral RNA replication and plays a crucial role in the viral life cycle.

Protein VP22 is another non-structural protein of SMSV that is involved in the regulation of viral gene expression. It is produced during the late stages of viral infection and is required for the efficient assembly of new virus particles.

In summary, San Miguel sea lion virus has several important proteins, including Capsid, Protein p16, Protein p30, Protein p32, SMSV-1 Viral genome-linked protein, Protein VP22, and Capsid protein VP1, that play crucial roles in viral replication and pathogenesis. These proteins are potential targets for antiviral drug development and could help to control the spread of the virus in sea lion populations.

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.