Foot-and-mouth disease virus cDNA and recombinant antigen

Foot-and-mouth disease virus (FMDV) is a highly contagious viral disease that affects cloven-hoofed animals such as cattle, pigs, sheep, and goats. FMDV is characterized by the formation of blisters in the mouth and on the hooves, leading to fever, lameness, and reduced milk production. FMDV can cause significant economic losses in the livestock industry due to decreased production and trade restrictions on affected countries.

The Capsid proteins P88, VP1, type C VP4 protein, and type C VP3 protein are critical components of the FMDV virion. The Capsid proteins play a crucial role in the viral lifecycle by protecting the viral genome and facilitating the virus’s entry into host cells. They are also important targets for the immune system, and changes in the Capsid protein sequence can lead to the emergence of new FMDV strains.

The P88 protein is involved in the initial steps of FMDV assembly, while the VP1 protein is responsible for binding to host cell receptors and inducing an immune response. The type C VP4 protein and type C VP3 protein are involved in capsid formation and stability.

FMDV is primarily transmitted via direct contact with infected animals, contaminated equipment or surfaces, and through the air over short distances. There are no specific antiviral treatments for FMDV, and vaccination is the primary method for controlling the spread of the disease. Vaccines containing inactivated or attenuated FMDV are widely used in endemic areas and are an important component of outbreak control strategies.

Understanding the structure and function of the FMDV Capsid proteins is critical for the development of effective vaccines and diagnostic tests for this important animal disease. Ongoing research into the molecular mechanisms of FMDV pathogenesis and transmission is essential for the continued control and eradication of FMDV in livestock populations worldwide.

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.