Ascaris lumbricoides, commonly known as the common roundworm, is a parasitic nematode that infects the intestines of humans and other mammals. A. lumbricoides infections are common in areas with poor sanitation, and can lead to a range of symptoms, including abdominal pain, diarrhea, and weight loss. In severe cases, the parasite can even cause intestinal blockages, which can be life-threatening.

One of the major allergens produced by A. lumbricoides is ABA-1, a protein that has been shown to induce a strong immune response in infected individuals. Exposure to ABA-1 can cause a range of symptoms, including itching, hives, and even anaphylaxis in some cases. ABA-1 has also been implicated in the development of asthma in infected individuals and may play a role in the high rates of asthma in areas with high rates of A. lumbricoides infections.

Efforts to control A. lumbricoides infections have focused on improving sanitation and hygiene practices in areas where the parasite is endemic. In addition, researchers are working to develop new treatments and prevention strategies for A. lumbricoides infections, including the development of new vaccines and immunotherapies that target the parasite’s unique biology.

Studying A. lumbricoides and the ABA-1 allergen is important for understanding the mechanisms behind the parasite’s virulence and for developing new treatments and prevention strategies for this important human parasite. Continued research in this area may provide important new insights into the biology of A. lumbricoides infections and may lead to new therapies and prevention strategies that can help to control the spread of this common roundworm.

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.