Echinococcus granulosus is a tapeworm that can infect canids and livestock, leading to the development of hydatid cysts in the liver, lungs, and other organs. These cysts can cause significant health problems and may even be fatal if left untreated.

Several key antigens of E. granulosus have been identified as potential targets for the development of diagnostic tests and vaccines against hydatidosis. These include EG19, EG18, and EG13, which are all located in the parasite’s tegument, or outer layer.

EG19 and EG18 are believed to play a role in the immune evasion of E. granulosus, by interfering with host immune responses and promoting parasite survival. The EG13 antigen, on the other hand, is thought to be involved in the attachment of the worm to host tissues.

In addition to these surface antigens, the EG95 vaccine antigen has shown promise as a potential target for vaccine development against hydatidosis. This antigen is involved in the development of the hydatid cyst and has been shown to confer host-protective immunity in vaccinated animals.

Ongoing research into the immunology and pathogenesis of E. granulosus infection will be crucial for the development of effective diagnostic tests and vaccines against hydatidosis. By targeting these key antigens, it may be possible to develop new tools to combat this important zoonotic disease and improve the health of both animals and humans.

The cDNA (complementary DNA) and recombinant antigens of Echinococcus granulosus have several potential applications, including:
Diagnosis: The recombinant antigen of Echinococcus granulosus can be used to detect the presence of specific antibodies in the host, which indicates an active or past infection. Serological tests, such as ELISA and Western blotting, can be used to detect the antibodies. Additionally, PCR (polymerase chain reaction) can be used to detect the parasite’s DNA in tissue samples.

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.