Gallid herpesvirus cDNA and Antigen

Gallid herpesvirus, also known as avian herpesvirus or chicken herpesvirus, is a virus that infects chickens and other poultry. The virus is responsible for causing various symptoms such as respiratory infections, eye infections, and reproductive disorders. The antigen is a substance that the immune system recognizes as foreign and triggers an immune response. The genome of Gallid herpesvirus is made up of DNA and is used to study the genetic makeup of the virus.

The GaHV virion is composed of a complex structure that includes a nucleocapsid, tegument proteins, and an envelope. Several structural proteins are involved in the formation of the virion, including:

23-kDa nuclear protein – A protein that is involved in the regulation of gene expression in infected cells.

GP57-65 – A group of glycoproteins that are located on the surface of the virion and are involved in attachment and entry into host cells.

Minor capsid scaffold protein-like protein – A protein that is involved in the assembly of the capsid.

38 kDa phosphoprotein – A protein that is involved in the regulation of viral gene expression and the replication of the viral genome.

Envelope glycoprotein L – A glycoprotein that is located on the surface of the virion and is involved in the fusion of the viral envelope with the host cell membrane.

Envelope glycoprotein B – A glycoprotein that is involved in the attachment and entry of the virus into host cells.

Envelope glycoprotein H – A glycoprotein that is involved in the fusion of the viral envelope with the host cell membrane.

The capsid and envelope proteins of GaHV play critical roles in the virus lifecycle, as they mediate viral entry into host cells, protect the viral genome, and facilitate the release of new virus particles from infected cells. The structural proteins are also targets for the host immune system and can elicit strong antibody responses in infected animals.

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.