Anisakis simplex is a parasitic nematode that is commonly found in marine fish and mammals, including whales, dolphins, and seals. Humans can become infected with A. simplex when they consume raw or undercooked seafood that is infected with the parasite, and the resulting infection can cause a variety of symptoms, including abdominal pain, nausea, and vomiting.

A. simplex is known to produce several proteins that are important for its survival and virulence. Elongation factor 1-alpha is a protein that is involved in protein synthesis and has been shown to have immunomodulatory effects on the host, allowing the parasite to evade the host’s immune system. SXP-RAL-2 is another protein produced by A. simplex that has been shown to induce a strong immune response in the host and may be a potential target for vaccine development. Enolase is a metabolic enzyme that is involved in glycolysis and has been shown to have adhesive properties that help the parasite attach to host tissue.

Paramyosin-allergen Ani s 2 is a protein that is produced by A. simplex and is a major allergen in humans. Exposure to Ani s 2 can lead to allergic reactions, ranging from mild symptoms such as hives and itching, to more severe symptoms such as anaphylaxis. Other proteins produced by A. simplex include the 29-kDa protein and the 42 kDa antigenic protein, which have been studied for their potential as diagnostic markers for Anisakis infections.

The study of Anisakis simplex and its associated proteins is important for understanding the mechanisms behind the parasite’s virulence and for developing new treatments and prevention strategies for Anisakis infections. Efforts to control the spread of Anisakis infections and to educate the public about the risks of consuming raw or undercooked seafood are ongoing, and the development of new vaccines and other immunotherapies may provide important new tools in the fight against this important human 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.