Feline parvovirus cDNA and Antigen

Feline parvovirus (FPV) is a highly contagious virus that affects domestic cats and wild felids. It is a member of the Parvoviridae family, which includes other viruses that infect animals such as canine parvovirus and mink enteritis virus. FPV primarily causes a severe, highly contagious enteritis (inflammation of the small intestine) in cats but can also cause other clinical signs such as myocarditis (inflammation of the heart muscle) and panleukopenia (a severe reduction in the number of white blood cells). Symptoms of FPV infection include vomiting, diarrhea, loss of appetite, and dehydration. The virus is spread through contact with infected feces, vomit, or nasal discharge, and can survive for long periods of time in the environment. Vaccination is the most effective means of preventing infection.

The genome of feline parvovirus (FPV) is a single-stranded DNA that is about 5 kb in length. The genome encodes for two non-structural proteins (NS1 and NS2) and two structural proteins (VP2 and VP3). The VP2 protein is the primary capsid protein and VP3 is a minor component of the virus. The NS1 and NS2 proteins play roles in viral replication and pathogenesis. The genome of FPV is highly stable, which makes the virus difficult to eradicate.

Feline parvovirus antigen refers to a protein or component of the feline parvovirus that can be used as a marker for detection or diagnostic purposes. Antigens can be used in tests such as ELISA or Western blot to identify the presence of the virus in a sample. Recombinant antigens can be produced using genetic engineering techniques to generate large quantities of the antigen for use in tests and vaccines.
Feline parvovirus (FPV) is a small, non-enveloped, single-stranded DNA virus that can cause a highly contagious and often fatal disease in cats called feline panleukopenia.

The FPV virion is composed of a single structural protein, the capsid protein, which forms the outer shell of the virus particle. The capsid protein is made up of multiple copies of a single polypeptide chain and is arranged in a characteristic icosahedral structure.

The capsid protein plays several important roles in the FPV lifecycle, including protecting the viral genome from degradation, facilitating viral entry into host cells, and promoting the release of new virus particles from infected cells. The capsid protein is also a major target for the host immune system and can elicit strong antibody responses in infected animals.

Due to the essential role of the capsid protein in the FPV lifecycle, it is a key target for the development of vaccines and antiviral therapies. Several types of FPV vaccines, including inactivated and subunit vaccines, have been developed that are based on the capsid protein. These vaccines have been shown to be highly effective at preventing FPV infection and reducing the severity of disease in infected animals.

Understanding the structure and function of the FPV Capsid protein is essential for developing effective prevention and treatment strategies for this important feline disease.

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.