Babesia canis is a tick-borne parasitic protozoan that infects dogs and is one of the most important causative agents of canine babesiosis worldwide. This parasite is composed of several subspecies, including B. caniscanis, B. canisrossi, and B. canisvogeli, all of which cause slightly different clinical presentations of the disease.

Heat Shock Protein 70 (HSP70) is a well-known protein associated with B. canis that is involved in protein folding and is essential for parasite survival. There are three types of HSP70 proteins associated with B. canis: Canis HSP70, Rossi HSP70, and Vogeli HSP70. Each of these proteins plays a different role in the parasite’s life cycle and host-parasite interactions.

Canis HSP70 is a major surface protein expressed by the parasite, and it is involved in host cell invasion and immune evasion. Rossi HSP70 is a cytosolic protein that is involved in parasite growth and development, while Vogeli HSP70 is an apicoplast-targeted protein that plays a role in parasite metabolism.

Understanding the functions and structures of these HSP70 proteins is essential for developing effective strategies to prevent and treat B. canis 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 HSP70 proteins, there are other proteins and antigens associated with B. canis that are being studied for their potential roles in disease pathogenesis and immunity. These include surface antigens, such as merozoite surface antigen 1 and 2, and metabolic enzymes, such as pyruvate kinase and enolase.

Overall, understanding the complex interplay between B. canis and its host is critical for developing effective strategies to prevent and treat babesiosis in dogs. 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.

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.