Feline herpesvirus cDNA and Antigen

Feline herpesvirus (FHV) is a highly contagious virus that affects cats. It is a member of the herpesvirus family and can cause a range of clinical signs, including upper respiratory symptoms, eye infections, and even death in severe cases. FHV is transmitted through direct contact with infected cats, contaminated objects, or aerosols.

The FHV genome encodes for numerous proteins, many of which are essential for viral replication, assembly, and host immune evasion. Some of the key FHV proteins include:

Glycoprotein E and M: These proteins are involved in viral entry into host cells. They work together to form a complex that binds to host cell receptors and mediates fusion between the viral envelope and host cell membrane.

Membrane protein UL56: This protein is involved in the formation of the viral envelope and is essential for viral replication and assembly.

Nuclear protein UL55: This protein plays a critical role in viral DNA replication and packaging. It is involved in the formation of viral nucleocapsids and interacts with other viral proteins to promote viral assembly.

Envelope protein UL43: This protein is involved in viral spread and immune evasion. It is thought to play a role in modulating the host immune response and facilitating the release of virions from infected cells.

Capsid scaffold protein: This protein is essential for viral assembly and stabilizes the viral capsid. It interacts with other viral proteins to promote the formation of infectious virions.

Immediate early protein: This protein is one of the first viral proteins to be expressed after infection and plays a critical role in regulating viral gene expression. It helps to activate the expression of other viral genes and promote viral replication.

Glycoprotein D: This protein is involved in viral entry into host cells and is a major target of the host immune response. It is critical for the virus’s ability to infect and replicate within the host cell.

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.