Theileria lestoquardi is a protozoan parasite that infects small ruminants such as sheep and goats and is transmitted by the tick Hyalomma anatolicum. The parasite causes a severe disease known as malignant theileriosis, which is characterized by high fever, anemia, and death. It is an economically important disease in many parts of the world, particularly in the Middle East, North Africa, and Central Asia, where it is endemic.

The immunodominant merozoite and piroplasm antigen of T. lestoquardi play a crucial role in the survival and pathogenesis of the parasite. Merozoites are the invasive form of the parasite that invade and multiply within red blood cells (RBCs), leading to their destruction and the development of anemia. Piroplasms, on the other hand, are the form of the parasite that circulate freely in the bloodstream of the host.

The immunodominant merozoite antigen of T. lestoquardi is a 29-kDa protein that is involved in the invasion of RBCs. Studies have shown that the antigen is highly conserved among different strains of the parasite and is recognized by the host immune system during infection. Therefore, it is considered a promising target for vaccine development against malignant theileriosis.

The piroplasm antigen of T. lestoquardi is a 33-kDa protein that is expressed on the surface of the parasite. It is involved in the attachment of the parasite to the surface of RBCs, which is an important step in the invasion process. The antigen is also recognized by the host immune system and is believed to play a role in the pathogenesis of the disease.

The cDNA and recombinant antigen derived from this organism can be used to develop diagnostic tests for the infection. This would enable veterinarians to detect the parasite in animals and treat them accordingly. Additionally, it could be used to create vaccines that could protect animals from becoming infected. These applications could help to reduce the economic losses associated with this parasite, and improve the welfare of 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.