Neospora hughesi is an apicomplexan parasite that infects horses and causes neuromuscular disease. The parasite is closely related to Toxoplasma gondii, a well-known human and animal pathogen. Neospora hughesi has a complex life cycle, involving both intermediate and definitive hosts, and it expresses a variety of surface and secreted antigens that are involved in host-pathogen interactions.

One of the important antigens expressed by Neospora hughesi is SAG1-related sequence 2 (SRS2), which is a member of the SAG1-related sequence family of surface antigens. SRS2 is involved in host cell invasion and is a potential target for vaccine development. Another important antigen is Antigen N54, which is expressed on the surface of the parasite’s tachyzoite stage and is recognized by the host immune system.

Neospora hughesi cDNA and recombinant antigen can be used to develop diagnostic tests for neosporosis, an infectious disease caused by the protozoan parasite Neospora hughesi. Recombinant antigens can be used to detect the presence of antibodies in the serum of infected animals, while cDNA can be used to develop a PCR-based test to detect the presence of the parasite in samples. Both methods are used to diagnose neosporosis in animals. Additionally, the cDNA can also be used to identify new potential vaccine candidates or to develop novel therapeutic strategies for treating the 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.