Human calicivirus cDNA and Antigen

HuCV is highly contagious and can be transmitted from person to person through contaminated food and water, as well as through close contact with an infected individual. Outbreaks of HuCV infections are common, particularly in crowded and unsanitary conditions, and the virus is a significant public health concern worldwide.

The human calicivirus antigen refers to a specific protein or combination of proteins present on the surface of the virus that can be used to identify and detect the presence of the virus in a sample. The antigen is recognized by the immune system and is the target of the host’s immune response to infection.

The use of human calicivirus antigens in diagnostic tests, such as ELISA or immunoassays, is important for accurately identifying infections with the virus. The development of recombinant antigens, made using genetic engineering techniques, has increased the sensitivity and specificity of these tests, allowing for earlier and more accurate diagnosis of HuCV infections.

Human calicivirus is a single-stranded RNA virus that causes acute gastroenteritis in humans. The virus is known for its unique structural and molecular features, which are governed by several key viral proteins, including the nucleocapsid protein, capsid protein, minor structural protein, major capsid protein VP1, and RNA polymerase.

The nucleocapsid protein is a structural protein that plays a role in protecting the viral genome and facilitating viral assembly. The capsid protein forms the outer shell of the virus and is critical for viral attachment and entry into host cells.

The minor structural protein is a small protein that is thought to play a role in regulating the assembly and disassembly of viral particles. The major capsid protein VP1 is the most abundant protein in the virus and is responsible for the characteristic morphology of calicivirus particles.

The RNA polymerase is an enzyme that is responsible for replicating the viral genome, making it an important target for antiviral therapies. Research is ongoing to develop drugs that can inhibit RNA polymerase activity and effectively treat calicivirus infections.

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.