Feline calicivirus cDNA and Antigen

Feline calicivirus (FCV) is a highly contagious virus that primarily affects cats. It is a member of the Caliciviridae family, which also includes human norovirus and rabbit hemorrhagic disease virus. FCV is transmitted through direct contact with infected cats, contaminated objects, or aerosols. It can cause a range of clinical signs, including respiratory symptoms, fever, and oral ulcers.

The FCV capsid is composed of multiple copies of three structural proteins: VP1, VP2, and VP3. VP1 is the major capsid protein and forms the outer shell of the virus, while VP2 and VP3 are minor capsid proteins that contribute to the structure of the capsid. These proteins play a crucial role in the virus’s ability to infect and replicate within the host cell.

Studies have shown that the major capsid protein, VP1, is the most important structural protein for FCV infection. It contains several functional domains, including the receptor-binding domain and the antigenic regions, which are critical for the virus’s ability to attach to and enter host cells. VP1 also interacts with the host immune system and plays a role in viral replication and assembly.

VP2 and VP3 are minor capsid proteins that are believed to play a role in stabilizing the capsid structure and promoting virus assembly. They have also been shown to be involved in viral entry into the host cell.

Understanding the structure and function of the FCV capsid proteins is important in developing effective treatments for FCV. Researchers are actively exploring the use of antiviral drugs and vaccines to control the spread of the virus. By targeting these proteins, it may be possible to inhibit viral replication and prevent the virus from spreading in the feline population.

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.