Vesicular stomatitis Indiana virus cDNA and Antigen

Vesicular stomatitis Indiana virus (VSIV) is a virus that causes a contagious disease primarily affecting livestock, including horses, cattle, sheep, goats, and swine. It is an arthropod-borne virus belonging to the family Rhabdoviridae, and can be spread by biting midges, black flies, and mosquitoes. The virus is endemic to the United States and occurs sporadically in other parts of North and South America. Infected animals may show signs of fever, oral lesions, and lameness. In rare cases, humans may become infected and experience flu-like symptoms; however, this is very rare. Currently, there is no vaccine or specific treatment for VSIV, and the best way to protect livestock is to reduce exposure to biting insects.

Vesicular stomatitis Indiana virus (VSI) is a member of the family Rhabdoviridae and is the etiological agent of vesicular stomatitis, a disease that primarily affects cattle, horses, and swine. VSI antigen is a protein found in the virus that can be used in laboratory diagnosis of the virus. It is also used in the development of vaccines and other treatments. The antigen can be extracted from the virus itself or produced in a lab using recombinant technologies.

Vesicular stomatitis Indiana virus (VSIV) is a single-stranded, negative-sense, non-segmented RNA virus in the Rhabdoviridae family. The VSIV genome is approximately 11,000 nucleotides in length and contains five genes that encode for the viral proteins. These genes are the nucleocapsid (N) gene, phosphoprotein (P) gene, matrix (M) gene, glycoprotein (G) gene, and the large (L) gene. These genes are arranged in the following order: N-P-M-G-L. The VSIV genome also contains several non-coding intergenic regions and a polyadenylation signal at the 3’ end of the genome.

The M protein of VSIV is a viral structural protein that forms a helical structure around the viral RNA genome. It plays a critical role in the assembly and budding of new virus particles from the host cell membrane. The glycoprotein of VSIV is essential for viral entry and is involved in the fusion of the virus envelope with the host cell membrane. The glycoprotein is also a target for the host immune response and plays a crucial role in the virulence of the virus.

The phosphoprotein of VSIV is an essential component of the viral RNA polymerase complex and is involved in regulating the transcription and replication of the viral RNA genome. It also plays a critical role in counteracting the host antiviral response, allowing the virus to replicate and spread.

Understanding the structure and function of the M protein, glycoprotein, and phosphoprotein of VSIV is essential for developing effective antiviral treatments and vaccines against the virus. Studies of these viral proteins have also provided insights into the replication mechanisms of other related viruses, leading to the development of new antiviral therapies for a range of viral infections.

Overall, the M protein, glycoprotein, and phosphoprotein of VSIV are all critical components of the virus replication cycle and are essential targets for developing antiviral therapies against the 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.