Rhipicephalus sanguineus is a species of tick found in tropical and temperate regions worldwide. It is commonly referred to as the brown dog tick and is an important vector of diseases to humans, dogs, and other animals. R. sanguineus is a hard-bodied tick with a wide, blunt head and long mouthparts that it uses to attach to its host and feed on their blood. In the adult stage, it is reddish-brown in color and can grow up to 8 mm in length. Females are larger than the males. R. sanguineus has a three-host life cycle, meaning that it feeds on different hosts at different stages of its life. The larvae and nymph stages feed on small mammals, such as mice and rats, while the adult stage feeds on larger mammals such as dogs and humans. R. sanguineus is a vector for several diseases in humans, such as Rocky Mountain spotted fever, babesiosis, and ehrlichiosis.

Cement-like Antigen is a significant component of this cement substance. Researchers are interested in understanding the role of this antigen in the tick’s ability to attach to its host and feed for long periods. Additionally, the antigen is being investigated as a potential target for developing novel tick control strategies.

Rhipicephalus sanguineus cDNA and recombinant antigens can be used to develop a variety of diagnostic, therapeutic, and preventive strategies. Diagnostic strategies include the use of cDNA- and antigen-based immunoassays to detect the presence of R. sanguineus antigens in samples and to diagnose tick-borne diseases. Therapeutic strategies can be developed using the recombinant antigens as vaccines to protect against R. sanguineus infection. Finally, preventive strategies can be developed using the cDNA and antigen sequences to develop insecticides and repellents that target R. sanguineus specifically.

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.