Eimeria acervulina is a type of Coccidian parasite that is known to infect chickens, causing economic losses in the poultry industry. The parasite has been extensively studied due to its high prevalence and the significant impact it has on poultry production. In this article, we will explore the role of Eimeria Acervulina’s antigen, lactate dehydrogenase, profilin, and merozoite surface protein CMZ-8 in understanding and combating this parasite.

Antigen:
Eimeria Acervulina’s antigen is a key player in the host-parasite interaction. The parasite’s antigen triggers an immune response in the host, leading to the production of antibodies that recognize and eliminate the parasite. Researchers have identified several antigenic proteins in Eimeria Acervulina, including lactate dehydrogenase, profilin, and merozoite surface protein CMZ-8.

Lactate Dehydrogenase:
Lactate dehydrogenase is an enzyme that plays a crucial role in the energy metabolism of Eimeria Acervulina. The parasite relies on lactate dehydrogenase to convert pyruvate into lactate, which is then used as an energy source. Researchers have found that lactate dehydrogenase is a promising target for developing drugs that can interfere with the parasite’s energy metabolism and prevent its growth and proliferation.

Profilin:
Profilin is a cytoskeletal protein that is involved in the motility and invasion of Eimeria Acervulina. The parasite uses profilin to move and penetrate the host’s intestinal epithelial cells, allowing it to establish infection. Researchers have found that profilin is a promising target for developing vaccines that can prevent the parasite from invading the host’s cells.

Merozoite Surface Protein CMZ-8:
Merozoite surface protein CMZ-8 is a protein that is expressed on the surface of Eimeria Acervulina’s merozoite stage. The merozoite is the stage of the parasite that is responsible for invading and replicating inside the host’s intestinal epithelial cells. Researchers have found that merozoite surface protein CMZ-8 is a promising target for developing vaccines that can prevent the parasite from invading the host’s cells.

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.

Eimeria acervulina cDNA and recombinant antigen can be used to develop immunodiagnostic tests for the detection of Eimeria acervulina infection in chickens. The cDNA and recombinant antigen can be used to develop ELISA-based tests to detect the presence of Eimeria acervulina-specific antibodies in chicken serum and egg yolk. The cDNA and recombinant antigen can also be used to develop PCR-based tests to detect Eimeria acervulina DNA in chicken samples. These tests can be used to diagnose Eimeria acervulina infection in chickens and to monitor the efficacy of therapeutic and preventive treatments.