Viral hemorrhagic septicemia virus cDNA and Antigen

Viral hemorrhagic septicemia virus (VHSV) is a highly contagious fish virus that can cause severe disease in many species of fresh and marine fish. The virus is believed to be spread by water currents and by infected fish and is capable of quickly spreading throughout a fish population. Symptoms of VHSV infection vary depending on the species of fish, but can include bloody streaks on the body, fin and tail rotor erosion, ulcers, bulging eyes, and death. Treatment is not available for VHSV, so prevention and containment are the most effective ways to manage the virus. This includes limiting the spread of the virus by preventing the transfer of fish or water from one place to another, and by using proper sanitation and disinfection protocols for equipment and facilities.

Viral hemorrhagic septicemia virus antigen (VHSV-Ag) is a viral antigen derived from the viral hemorrhagic septicemia virus, which is a type of fish-infecting rhabdovirus. VHSV-Ag is used in laboratory tests to detect the presence of the virus in fish. It can be used to diagnose the infection in both live and dead fish. VHSV-Ag can also be used to rapidly detect the virus in fish farms and hatcheries. The antigen is used in combination with other tests such as histopathology, fluorescent antibody tests, and PCR tests to confirm the presence of the virus.

Viral hemorrhagic septicemia virus (VHSV) is an aquatic respiratory pathogen of the genus Novirhabdovirus in the family Rhabdoviridae. It is composed of a single-stranded, negative-sense RNA genome of approximately 11,000 nucleotides in length, organized into five genes. These genes encode for the following proteins: Nucleoprotein (N), Phosphoprotein (P), Matrix protein (M), Glycoprotein (G) and the non-structural protein (NS).

The glycoprotein (G) is the major surface protein of VHSV and is responsible for virus attachment and entry into host cells. The G protein is heavily glycosylated and contains multiple antigenic sites, making it a prime target for neutralizing antibodies. The G protein is also involved in VHSV pathogenesis, as it has been shown to induce cell death and inflammation in fish cells.

The envelope spike protein (E) is another important component of VHSV and is responsible for membrane fusion during viral entry into host cells. The E protein interacts with the G protein and the matrix protein M1 to mediate fusion between the viral envelope and the host cell membrane.

The matrix proteins, M1 and M2, are essential for viral assembly and release. The M1 protein plays a key role in virus assembly by interacting with the RNP and the G protein to form the viral particle. The M2 protein is a phosphorylated protein that is involved in the budding and release of VHSV from infected cells.

Understanding the structure and function of these VHSV proteins is essential for the development of effective vaccines and antiviral therapies. By targeting key viral proteins such as the N, G, and E proteins, it may be possible to inhibit VHSV replication and reduce the severity of the disease.

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.