Woodchuck hepatitis B virus cDNA and Antigen

WHV produces a core protein that forms the viral capsid, which encapsulates the viral genome. The virus also produces an external core antigen (HBcAg) that circulates in the blood and serves as a marker of viral infection. The major envelope protein of WHV is a large protein that mediates viral entry into host cells and helps the virus evade the immune system.

Reverse transcriptase is a unique enzyme produced by WHV that enables the virus to replicate its DNA through a RNA intermediate. The protein X (HBx) is a regulatory protein that modulates host cell signaling pathways and is implicated in viral pathogenesis.

Woodchuck hepatitis B virus (WHV) is a member of the Hepadnaviridae family and is closely related to the human hepatitis B virus. The virus causes hepatitis in woodchucks and is a valuable model for studying the pathogenesis and treatment of human hepatitis B virus infection.

The WHV genome encodes several proteins that are important for its replication and pathogenesis. The capsid protein forms the viral core, while the large envelope protein is responsible for virus assembly and release. The external core antigen is a component of the viral envelope and can be used as a diagnostic marker for hepatitis B infection. The reverse transcriptase is responsible for converting the viral RNA genome into a DNA intermediate, which can then integrate into the host genome. The protein X (HBx) is a regulatory protein that can modulate the host immune response and contribute to virus-induced liver cancer.

Understanding the functions and interactions of these viral proteins is essential for developing effective antiviral strategies against hepatitis B virus infection.

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.