Dirofilaria immitis is a parasitic nematode that infects dogs, and occasionally other mammals, through mosquito bites. Once inside the host, the worms mature and mate, with the female releasing microfilariae that circulate in the bloodstream. These microfilariae can then be taken up by mosquitoes and transmitted to other animals, completing the parasite’s life cycle.

One of the major challenges in diagnosing and treating D. immitis infection is the presence of numerous immunodominant antigens that can trigger an immune response in the host. These antigens include the Venom allergen antigen 5-like protein, which has been shown to be an important mediator of inflammation and immune activation in dogs with heartworm disease.

Other important antigens include the D34 immunodominant antigen, which is believed to play a key role in the development of protective immunity against the parasite, and the Immunodominant antigen homologue, which has been shown to be a potent stimulator of the immune response in dogs with heartworm disease.

Additionally, the Cuticular antigen, Filarial common antigen protein, Polyprotein antigen, and Cuticular antigen tandem repeats are all key antigens that have been identified as potential targets for immunodiagnostic assays and vaccine development against D. immitis.

Despite the challenges posed by these numerous and complex antigens, significant progress has been made in the development of effective diagnostic tests and treatments for D. immitis infection. Ongoing research into the immunology of the parasite and its interactions with the host immune system will be crucial for the development of new tools to combat this important canine health threat.

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.