Hepatitis A virus cDNA and Antigen

Hepatitis A virus (HAV) is a type of virus that causes inflammation of the liver (hepatitis). HAV is primarily spread through contaminated food or water and can cause symptoms such as fatigue, abdominal pain, jaundice (yellowing of the skin and eyes), and nausea. The symptoms of HAV infection typically resolve on their own within a few weeks, although severe cases can lead to liver failure. There is a vaccine available to prevent HAV infection, and good hygiene practices, such as washing hands regularly, can also reduce the risk of transmission.

Hepatitis A virus (HAV) antigen refers to a substance (protein) present on the surface of HAV that triggers an immune response. Antigens are recognized by the body’s immune system and help it identify pathogens, such as HAV. In the context of HAV, the antigen can be used as a tool for developing diagnostic tests to detect HAV infection. Additionally, the antigen may be used in vaccine development to help protect individuals from HAV infection. The use of HAV antigen in these applications is important for controlling the spread of HAV and reducing the impact of HAV-associated liver disease.

Hepatitis A virus (HAV) viral protein 1, also known as VP1, is a structural protein that plays an important role in the assembly and function of the HAV virion. It is one of the four structural proteins that make up the HAV capsid, which surrounds the viral genome and protects it from the host immune system.

VP1 is a relatively small protein, with a molecular weight of approximately 35 kDa. It is composed of three distinct domains, each of which plays a specific role in the structure and function of the protein. The N-terminal domain is responsible for anchoring VP1 to the inner surface of the viral capsid, while the central domain forms a shell that encloses the viral genome. The C-terminal domain is thought to be involved in interactions with host cell receptors and may play a role in the entry of the virus into host cells.

In addition to its role in virion assembly and host cell entry, VP1 is also an important target of the host immune response. Antibodies to VP1 are commonly produced during HAV infection and can be used as a marker of acute infection in clinical settings.

Understanding the structure and function of VP1 is therefore important for developing new treatment options and control measures for HAV. For example, drugs that target specific interactions between VP1 and host cells may be effective in blocking viral entry and replication. Furthermore, research on VP1 can also provide insights into the evolution and diversity of HAV and related viruses, which can inform efforts to control the spread of these pathogens.

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.