Vaccinia virus cDNA and Antigen

Vaccinia virus is a type of virus that is used in the creation of vaccines to protect against smallpox. It is a large, complex virus that has a double-stranded DNA genome and contains more than 200 genes. Vaccinia virus is closely related to the viruses that cause smallpox and cowpox, and it is used as a vaccine in humans and animals to protect them against these other viruses. Vaccinia virus is administered in a form of a weakened, live virus, and it generally produces a mild, localized infection that stimulates the body’s immune system to produce protective antibodies against smallpox.

Vaccinia virus antigen is a type of protein found on the surface of the vaccinia virus, which is a member of the poxvirus family. The antigen is composed of several viral proteins, including the major outer membrane protein and viral envelope proteins. These proteins play a role in viral attachment and entry into host cells. Vaccinia virus antigen is used in the manufacture of vaccines, which can help protect people from diseases caused by the virus, such as smallpox.

Vaccinia virus is a large, complex, double-stranded DNA virus that belongs to the poxvirus family. Its genome is composed of a linear double-stranded DNA molecule of approximately 200 kb, which is the largest among the poxviruses. The genome is divided into three major components: the core region, the left-hand region, and the right-hand region. The core region contains the essential genes required for virus replication and contains the origins of replication, which are required for efficient genome replication. The left-hand and right-hand regions contain additional genes, which are involved in the production of proteins necessary for virus assembly and the formation of a protective outer envelope.Some of the key proteins of Vaccinia virus are CD47 antigen/integrin-associated protein, 16.1K protein, IMV heparin binding surface protein, major envelope proteins, surface antigen S, and several others.

CD47 antigen/integrin-associated protein is a host protein that is hijacked by the virus to aid in its entry into host cells. This protein is exploited by Vaccinia virus to attach to and enter host cells via integrin receptors, leading to virus entry and subsequent infection.

The 16.1K protein is an early viral protein that is involved in virus replication and transcription. It interacts with other viral proteins to form a complex that is critical for the expression of other viral genes.

The IMV heparin binding surface protein is a structural protein that is present on the surface of the infectious mature virus (IMV) and is involved in the attachment of the virus to host cells. This protein interacts with heparin sulfate proteoglycans on the host cell surface, leading to virus entry.

The major envelope proteins of Vaccinia virus include surface antigen S, major envelope protein p37K, and the immunodominant envelope protein p35. These proteins are involved in virus assembly, budding, and release. The surface antigen S is also involved in virus entry into host cells and is a target of the host immune response. The immunodominant envelope protein p35 is a major target of the host immune response, and its presence in a vaccine may contribute to the elicitation of an immune response against Vaccinia virus.

The protein H5 of Vaccinia virus encompasses several proteins, including serine proteinase inhibitor 3, host range protein 1, protein K4, protein K5, and protein K7. These proteins are involved in virus replication, transcription, and immune evasion. The serine proteinase inhibitor 3 inhibits the host immune response by interfering with the host complement system. Host range protein 1 plays a role in determining the host range of the virus, while protein K4, K5, and K7 are involved in virus replication and transcription.

Overall, understanding the roles and functions of these key proteins is crucial for developing effective vaccines and antiviral therapies against Vaccinia virus, which is still used today in some areas of the world as a smallpox vaccine and has the potential to be used as a vector for other vaccines.

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.