Babesia divergens is a tick-borne parasitic protozoan that infects cattle and is a major cause of bovine babesiosis. This disease can be severe, leading to anemia, fever, and death in some cases. To better understand this important parasite, researchers are studying the surface proteins associated with B. divergens.

One of the most well-known surface proteins associated with B. divergens is the apical membrane antigen 1 (AMA1). This protein plays a key role in host cell invasion, and it is also a target for antibodies produced by the host’s immune system. Studying the structure and function of AMA1 could lead to the development of new vaccines and therapies to prevent and treat babesiosis.

In addition to AMA1, there are other surface proteins associated with B. divergens that are being studied for their potential roles in the parasite’s life cycle and pathogenesis. These include surface proteins such as the variable merozoite surface antigen (VMSA) and the RAP1-like protein (RLP). Understanding the roles of these proteins in host-parasite interactions could provide insights into new targets for vaccines and therapies.

Despite ongoing research, much remains to be learned about the complex interplay between B. divergens and its host. By studying the different surface proteins associated with this parasite, researchers are gaining a better understanding of how it infects and interacts with its host. This knowledge could lead to the development of new strategies to prevent and treat babesiosis in cattle.

Overall, understanding the roles and functions of surface proteins such as AMA1, VMSA, and RLP is critical for developing effective strategies to combat B. divergens and other tick-borne parasites that pose a threat to both animal and human health. Ongoing research into these proteins and other aspects of the parasite’s biology will continue to shed light on this important disease and provide new avenues for treatment and prevention.

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.