Babesia caballi is a tick-borne protozoan parasite that infects horses and causes babesiosis, a disease that can be severe and sometimes fatal. Like Babesia bovis, B. caballi has a complex life cycle that involves multiple stages, and it interacts with a variety of host proteins to establish and maintain infection.

One of the most well-known proteins associated with B. caballi is the 48kDa merozoite antigen, which is a major surface protein expressed during the blood stage of infection. This antigen plays a critical role in host-parasite interactions, and it is being studied as a potential target for vaccines and therapeutics.

Another important protein associated with B. caballi is Heat Shock Protein 70, or HSP70, which is involved in protein folding and is essential for parasite survival. This protein is expressed at high levels during the blood stage of infection, and it is being evaluated as a potential drug target for babesiosis.

Understanding the functions and structures of these proteins is essential for developing effective strategies to prevent and treat B. caballi infection. Ongoing research is focused on identifying new targets for vaccines and therapies, as well as improving our understanding of the basic biology of this important parasite.

In addition to the 48kDa merozoite antigen and HSP70, there are other proteins and antigens associated with B. caballi that are being studied for their potential roles in disease pathogenesis and immunity. These include surface antigens, such as RAP-1 and Rhoptry-associated protein 2, as well as enzymes involved in metabolism, such as pyruvate kinase and enolase.

Overall, understanding the complex interplay between B. caballi and its host is critical for developing effective strategies to prevent and treat babesiosis. Ongoing research into the different proteins and antigens associated with this parasite will likely lead to the development of new diagnostics, vaccines, and therapies to combat this important disease in horses.

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.