Trichinella britovi is a parasitic roundworm that is found in animals such as pigs, bears, and wild boars. This species of Trichinella is particularly common in Europe and is known to cause a zoonotic disease in humans called trichinellosis. Trichinella britovi can infect humans who consume undercooked or raw meat from infected animals, leading to symptoms such as diarrhea, abdominal pain, and muscle pain.

One of the key components of Trichinella britovi’s pathogenesis is the secretion of specific antigens that allow the parasite to evade the host’s immune system and establish infection. These antigens are proteins that are secreted by the parasite and can interact with host cells to modulate the immune response. One such antigen is the secretory antigen of Trichinella britovi, which has been identified as a potential target for diagnostic and therapeutic interventions.

Research has shown that the secretory antigen of Trichinella britovi can be detected in serum samples from infected animals and humans, making it a promising candidate for diagnostic tests. Additionally, studies have suggested that targeting this antigen with antibodies or other therapeutic agents may be an effective strategy for treating trichinellosis.

In order to better understand the pathogenesis of Trichinella britovi and develop effective treatments, researchers are continuing to study the parasite’s secreted antigens and their interactions with host cells. By identifying key targets for diagnostic and therapeutic interventions, we can work towards reducing the burden of trichinellosis and other parasitic infections around the world.

Trichinella britovi cDNA and recombinant antigen can be used in the diagnosis of trichinellosis. These molecules can be used as targets in PCR-based assays or as antigens in enzyme-linked immunosorbent assays (ELISAs). PCR-based assays are highly sensitive and specific, but they require specialized equipment and expertise. ELISAs are less sensitive but simpler to use and do not require specialized equipment. Both techniques are used to detect the presence of Trichinella britovi in a sample.

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.