Paragonimus westermani is a species of lung fluke which is the causative agent of paragonimiasis, a type of parasitic disease. The antigen associated with this organism is a glycoprotein, which is secreted by the fluke and recognized by the host’s immune system. The primary antigenic proteins are the surface proteins, which are expressed on the tegument and cilia of the fluke and play a role in the evasion of host immunity. These proteins are responsible for the recognition of the fluke by the host’s immune system and the generation of an immune response. Other antigens associated with the fluke are enzymes, such as catalase and esterase, which are involved in the digestion of host cells.

Paragonimus westermani egg antigen is an important component used in the diagnosis of paragonimiasis, a parasitic lung infection caused by the lung fluke P. westermani. This immunodominant glycoprotein is found in the eggs of the parasite and is released into the host’s body during infection.

Serological tests that detect antibodies to P. westermani egg antigen are commonly used to diagnose paragonimiasis. The test is based on the principle that the host’s immune system produces antibodies to the parasite’s antigens, including the egg antigen. The presence of these antibodies in a patient’s blood or other bodily fluids can confirm a diagnosis of paragonimiasis.

This parasitic flatworm. Paragonimus westermani cDNA and recombinant antigens can be used to develop diagnostic tests for the detection of the parasite and its antigens in the human body. These diagnostic tests can help to diagnose the infection and allow for more targeted and effective treatments.The cDNA and recombinant antigens can also be used for the development of vaccines against the disease. The antigens can be used to create vaccines that can induce immunity against the parasite and prevent the development of the disease. Vaccines can also be used to reduce the spread of the parasite.

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.