Nosema bombycis is a microsporidian parasite that infects silkworms and is an emerging pathogen that poses a significant threat to the silk industry. The infection process involves a surface-antigen protein, P30.4, which plays a critical role in host-parasite interaction. Recent research has shed light on the molecular mechanisms underlying the interaction between Nosema bombycis and its host, revealing potential avenues for controlling the disease.

The infection process involves a surface-antigen protein, P30.4, which mediates host-parasite interaction. P30.4 binds to host intestinal epithelium, leading to invasion and proliferation 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.