Ascaris suum, also known as the Pig Roundworm, is a parasitic nematode that infects pigs and can be transmitted to humans through contact with contaminated soil or infected pork products. In pigs, A. suum infections can cause a range of symptoms, including weight loss, diarrhea, and respiratory problems. In humans, the parasite can cause a condition known as visceral larva migrans, which can lead to fever, abdominal pain, and other symptoms.

One of the unique proteins produced by A. suum is the immunosuppressive ovarian message protein (IM), which has been shown to have immunomodulatory effects on host immune cells. IM may play a role in the parasite’s ability to evade host immune responses and establish chronic infections in the host. Another unique protein produced by A. suum is the major sperm protein (MSP), which is involved in the development of sperm in the male parasite.

Research on A. suum and its unique proteins has important implications for animal and human health. Understanding the mechanisms by which A. suum evades host immune responses could lead to the development of new treatments and prevention strategies for both animal and human infections. Additionally, the MSP protein produced by A. suum has been used as a model for studying the structure and function of similar proteins in other organisms, including humans.

Studying A. suum and its unique proteins is important for understanding the biology of this important parasite and for developing new strategies for controlling and preventing infections in both animals and humans. Continued research in this area may lead to important new insights into the biology of parasitic nematodes and may provide new targets for the development of novel therapies and prevention strategies.

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.