Onchocerca gibsoni is a parasitic nematode that infects cattle and is a major cause of bovine onchocerciasis, also known as river blindness. One of the key proteins produced by O. gibsoni is the repetitive antigen protein (RAG-1), which is a major target for the host immune response.

The RAG-1 protein is a highly repetitive and antigenic protein that is expressed on the surface of the parasite. It is involved in the attachment of the parasite to host tissue and plays a crucial role in the establishment and maintenance of the infection. The RAG-1 protein is also important in inducing a protective immune response in the host.

The identification and characterization of RAG-1 as a major antigenic protein of O. gibsoni have led to the development of new diagnostic tests and potential vaccine candidates. The RAG-1 protein has been shown to be highly specific and sensitive in detecting the presence of O. gibsoni in infected cattle.

Onchocerca gibsoni cDNA and recombinant antigen can be used for a variety of applications in medical research. For example, the cDNA can be used for gene expression studies, helping to identify the gene products involved in the life cycle of this parasitic nematode. This can help to understand the biology of this organism and potentially identify targets for new treatments. The recombinant antigen can be used to develop serological assays that can be used to diagnose and monitor infections with this parasite. Vaccines can also be developed using the recombinant antigen. Finally, the cDNA can be used to develop molecular diagnostic tests that can be used to identify and differentiate Onchocerca gibsoni infections from other nematodes.

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.