Reston ebolavirus cDNA and Antigen

Reston ebolavirus (RESTV) is an ebolavirus species that was first identified in 1989, in macaque monkeys imported from the Philippines to a Reston, Virginia research facility. This species is distinct from other species of ebolavirus, as it does not appear to cause illness in humans or other non-human primates. RESTV can, however, cause disease in pigs. RESTV is spread through contact with infected animal tissue or body fluids, such as saliva, urine, or feces. It is believed that the virus is spread through contact with infected animals, either through direct contact with their body fluids or through contact with surfaces that have been contaminated with the virus. RESTV can also be spread through aerosols, which is why it is important to take precautions when working with infected animals. There is currently no vaccine or treatment available for RESTV infection, so prevention methods are the most effective way to protect oneself from this virus. These methods include avoiding contact with infected animals and their body fluids, wearing protective clothing and masks when working with animals, and washing hands thoroughly after meeting an animal. It is also important to practice good hygiene and sanitation in animal facilities.

Reston ebolavirus antigen is a protein found on the surface of the Reston ebolavirus, which is a subtype of the Ebola virus. The antigen is responsible for stimulating an immune response against the virus, which helps the body to fight off infection. The antigen can be used to develop vaccines to protect against the Reston ebolavirus, as well as diagnostics tests to detect the virus in infected individuals.

The Reston ebolavirus is an ebolavirus that was first discovered in 1989, in Reston, Virginia. It is related to the Zaire ebolavirus and is the only ebolavirus known to not cause disease in humans. The Reston ebolavirus is a negative-sense, single-stranded RNA virus with a genome of approximately 19 kilobases in length. It contains seven genes that encode for structural and non-structural proteins, with two additional open reading frames (ORFs) of unknown function. The Reston ebolavirus genome encodes for two glycoproteins, GP1 and GP2, which are responsible for attaching to and entering target cells, as well as for causing haemorrhagic fever. It also encodes for the NP, VP35, VP40, VP30, and L proteins, which are responsible for the virus’s replication and assembly. The Reston ebolavirus also contains two non-structural proteins, VP24 and VP25, which play a role in viral replication and transcription.

The virus has several proteins associated with its structure and replication, including the nucleoprotein, envelope glycoprotein, membrane-associated protein VP24, and matrix protein VP40.

The nucleoprotein is a major component of the virus’s ribonucleoprotein complex, which is critical for viral replication and transcription. The envelope glycoprotein plays a key role in viral entry and is a major target for vaccine development. The membrane-associated protein VP24 is important for viral assembly and budding, while the matrix protein VP40 is involved in viral assembly and release.

Understanding the functions of these proteins is crucial for developing effective treatments and vaccines for Reston ebolavirus.

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.