Fasciola hepatica, commonly known as the liver fluke, is a parasitic flatworm that infects various mammals, including humans. This trematode worm resides in the bile ducts of the liver and causes a disease known as fascioliasis. The pathogenicity of this parasite is attributed to its ability to secrete several virulence factors, including the Cathepsin L 2 and L1 proteins. In this article, we will discuss the roles and significance of these proteins in the pathogenicity of F. hepatica.

The Cathepsin L 2 and L1 proteins are cysteine proteases that are secreted by the liver fluke during its migration and feeding processes. These proteins are crucial for the survival and pathogenicity of F. hepatica. The Cathepsin L 2 is primarily expressed during the acute phase of the infection, whereas the Cathepsin L1 is expressed throughout the chronic phase of the disease.

The Cathepsin L 2 and L1 proteins are involved in several physiological and pathological processes, including host tissue invasion, nutrient acquisition, and immune evasion. These proteins facilitate the digestion of host tissues by breaking down extracellular matrix proteins, such as collagen and elastin, and host immunoglobulins, such as IgG and IgA. This allows the parasite to invade host tissues and evade the host’s immune response.

Moreover, the Cathepsin L 2 and L1 proteins are capable of modulating the host’s immune response by suppressing T-cell proliferation and cytokine production. This immunomodulatory effect helps the parasite to evade the host’s immune response and establish a chronic infection.

The Cathepsin L 2 and L1 proteins play a crucial role in the pathogenicity of F. hepatica. These proteins facilitate the invasion of host tissues and modulate the host’s immune response, thereby allowing the parasite to establish a chronic infection. Understanding the roles and significance of these proteins may provide insights into the development of novel therapeutic strategies for the treatment of fascioliasis.

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.

Fasciola hepatica cDNA and recombinant antigens can be used for the development of diagnostic assays for the detection of fasciolosis, a food-borne trematode infection. These assays can be used to identify infected individuals and to determine the presence of the parasite in food and water sources. Recombinant antigens can also be used to develop vaccines to provide protection against fasciolosis.