Equine infectious anemia virus cDNA and Antigen

Equine infectious anemia (EIA) virus, also known as swamp fever, is a retrovirus that infects horses, donkeys, and mules. The virus is primarily spread through the bite of infected horse flies but can also be spread through other blood-sucking insects, as well as through contaminated needles, instruments, and equipment. Once infected, the virus replicates in the horse’s red blood cells and causes a chronic, debilitating disease. EIA can lead to fever, weight loss, anemia, and edema (swelling). Some horses may also develop neurological signs.

The Equine infectious anemia (EIA) virus genome is the complete set of genetic instructions that the virus uses to replicate and cause disease. Like all retroviruses, the EIA virus genome consists of two copies of single-stranded RNA enclosed in a viral envelope. The RNA genome codes for several viral proteins, including the viral reverse transcriptase, protease, and integrase enzymes, as well as the viral envelope protein (gp90) that is important for diagnostic tests and vaccine development.

The EIA virus genome is relatively small, around 9.7 kilobases in size, which is significantly smaller than the genomes of other retroviruses such as HIV. The genome of EIA virus is divided into three regions: long terminal repeats (LTRs), gag, and env.

Equine infectious anemia (EIA) virus antigen refers to the specific proteins found on the surface of the virus that can be recognized by the host’s immune system. These proteins, known as viral envelope proteins, can be used to create diagnostic tests for EIA, as well as vaccines to protect horses from the disease.

The EIAV virion is composed of several structural proteins, including:

Envelope protein – a glycosylated protein that forms the outer layer of the virion and mediates viral entry into host cells.

Gag polyprotein – a precursor protein that is cleaved into several smaller proteins, including the capsid protein, which forms the core of the virion.

Gp45 – a membrane glycoprotein that is involved in viral assembly and maturation.

GP90 – a larger glycoprotein that is also involved in viral assembly and maturation.

Envelope glycoprotein – another glycosylated protein that is involved in viral entry into host cells.

These structural proteins work together to allow the virus to infect and replicate within host cells. The viral envelope glycoproteins are particularly important for the virus to evade the immune system, as they can rapidly mutate and change their antigenic structure. The complex structure of the EIAV virion and the variability of its structural proteins make it a challenging target for the development of effective vaccines and 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.