Zaire ebolavirus cDNA and Antigen

Zaire ebolavirus is a species of Ebolavirus and is the most virulent of the known ebolaviruses. It is named after the Democratic Republic of the Congo (formerly Zaire), where it was first identified in 1976. The virus is responsible for the majority of the outbreaks of the disease known as Ebola virus disease, which is a severe, often fatal illness in humans and other primates. The virus is spread through contact with the bodily fluids of infected individuals and is most commonly transmitted through contact with infected animals such as bats, monkeys, and gorillas. The mortality rate of Zaire ebolavirus is typically between 50-90%, although the 2014-2016 West African outbreak had a mortality rate of around 70%. Treatment is limited to supportive care, and there are no specific vaccines or drugs approved for the treatment of Zaire ebolavirus.

The Zaire ebolavirus antigen is a glycoprotein found on the surface of the Zaire ebolavirus that is responsible for initiating the infection process. This antigen binds to specific receptors on the host cell and initiates the endocytic process that leads to the introduction of the virus into the cell. It is also responsible for triggering the immune response in the host, which results in the production of antibodies against the virus. The antigen is made up of a single polypeptide chain that is cleaved into two subunits, GP1 and GP2, which are linked by a disulfide bridge. GP1 is responsible for binding to specific cell receptors, while GP2 is responsible for triggering the immune response.

The Zaire ebolavirus antigen genome consists of seven genes that encode structural and nonstructural proteins. These genes include VP35, VP40, GP, VP30, VP24, L, and NP. VP35 is a nonstructural protein that helps to regulate transcription and replication of the virus. VP40 is a structural protein that is found in the viral envelope and is involved in the assembly and budding of the virus from the host cell. GP is the glycoprotein that is involved in attachment and entry of the virus into the host cell. VP30 is a transcription factor that helps to control the expression of viral genes. VP24 is a structural protein that is found in the viral envelope and is involved in assembly and budding of the virus. L is the polymerase protein which helps to replicate the viral genome. Finally, NP is the nucleoprotein which helps to package the viral genome.

One of the key proteins of EBOV is the nucleoprotein, which is responsible for encapsulating the viral RNA genome and forming the ribonucleoprotein complex. Matrix protein VP40 plays a role in the formation and release of viral particles, and the envelope glycoprotein is responsible for viral attachment and entry into host cells.

Another important protein is the membrane-associated protein VP24, which plays a role in the regulation of host immune responses and viral replication. VP24 is known to inhibit the host interferon response and is believed to contribute to the pathogenesis of the virus.

Targeting these viral proteins is a promising approach for the development of antiviral therapies and vaccines against EBOV. Several drugs that target EBOV proteins are currently under investigation, including those that inhibit the activity of the nucleoprotein, matrix protein VP40, and envelope glycoprotein.

In conclusion, understanding the functions of EBOV proteins is critical for the development of effective treatments and vaccines against this deadly virus. The nucleoprotein, matrix protein VP40, envelope glycoprotein, and membrane-associated protein VP24 all play important roles in the virus life cycle and pathogenesis and may serve as potential targets for the development of antiviral therapies.

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.