Theileria ovis is a protozoan parasite that infects sheep and goats worldwide, causing ovine theileriosis. The disease is transmitted by ticks, and it can result in significant economic losses in the livestock industry. Theileria ovis is known to cause anemia, weight loss, and decreased milk production in infected animals.

To survive within the host, Theileria ovis has evolved various strategies to evade the host’s immune system. One of these strategies is the production of heat shock proteins (HSPs). Heat shock proteins are molecular chaperones that play a critical role in the folding and stabilization of other proteins. They are produced by cells in response to stressful conditions, such as heat, radiation, and infection.

Heat shock protein 70 (HSP70) is a highly conserved protein that is present in all living organisms. It is a key player in the survival of many parasites, including Theileria ovis.

The Role of Heat Shock Protein 70 in Theileria ovis:

Heat shock protein 70 has been identified in Theileria ovis and has been shown to play a crucial role in the survival of the parasite within its host. The protein is involved in many cellular processes, including protein folding, protein trafficking, and antigen presentation.

Studies have shown that Theileria ovis can induce the production of HSP70 in infected sheep. This induction is thought to be a mechanism for the parasite to evade the host’s immune system by interfering with the host’s immune response.

Moreover, it has been shown that HSP70 is present on the surface of Theileria ovis merozoites, the invasive form of the parasite. This suggests that the protein may also play a role in the invasion of host cells by the parasite.

The application of Theileria ovis cDNA and recombinant antigen may help to improve the diagnosis, treatment, and control of this parasite. By using cDNA and recombinant antigen, researchers can develop more specific and sensitive diagnostic tests for Theileria ovis, as well as vaccines and treatments that target the parasite more effectively. In addition, researchers can also use cDNA and recombinant antigen to study the genetics and biology of Theileria ovis, which can improve our understanding of this parasite and its effects on livestock.

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.