Spring viremia of carp virus cDNA and Antigen

Spring viremia of carp virus (SVCV) is a negative-sense RNA virus that is a major pathogen of fish, causing significant economic losses in the aquaculture industry. The virus encodes several important proteins, including:

Glycoprotein: A membrane-bound protein that is involved in virus attachment and entry into host cells.

Matrix: A protein that forms a layer beneath the viral envelope and plays a role in virus assembly and budding.

Nucleocapsid protein: A structural protein that binds to the viral RNA genome and forms the viral nucleocapsid.

Phosphoprotein: A regulatory protein that is involved in the replication and transcription of the viral genome.

Nucleoprotein: A structural protein that binds to the viral RNA genome and plays a role in the formation of the viral nucleocapsid.

These proteins are essential for the replication and pathogenesis of SVCV. Their study is important for understanding the mechanisms of viral infection and for the development of effective treatments for fish diseases caused by SVCV.

In addition to the above-mentioned proteins, SVCV encodes other important proteins, such as the viral RNA polymerase, which is responsible for replicating and transcribing the viral genome. The viral RNA polymerase is an attractive target for antiviral drug development, as it is essential for the viral life cycle.

The glycoprotein of SVCV is particularly important for viral pathogenesis, as it is involved in the attachment and entry of the virus into host cells. The glycoprotein is also a major target of the host immune response, and the study of its structure and function is important for the development of effective vaccines against SVCV.

The nucleocapsid protein of SVCV plays a critical role in viral genome packaging and virion assembly. It is also involved in the regulation of viral gene expression and the evasion of host immune responses. The study of the nucleocapsid protein can provide important insights into the mechanisms of viral replication and pathogenesis.

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.