Enterocytozoon bieneusi is a unicellular eukaryotic parasite that belongs to the phylum Microsporidia. It is a common cause of intestinal infection in humans and animals, particularly in immunocompromised individuals. One of the significant proteins expressed by E. bieneusi is Proliferating Cell Nucleolar Antigen p120, which plays an essential role in the life cycle of the parasite.

Proliferating Cell Nucleolar Antigen p120 is a 120 kDa protein, which is present in the cytoplasm and nucleolus of E. bieneusi cells. The protein contains several conserved domains, including an RNA binding domain, a ribosomal RNA processing domain, and an RNA helicase domain. These domains are essential for the protein’s function in ribosome biogenesis and mRNA processing.

The Proliferating Cell Nucleolar Antigen p120 is an essential component of the nucleolus, which is the site of ribosome biogenesis. The protein is involved in ribosomal RNA processing, and it plays a crucial role in the assembly of the small subunit of the ribosome. It has also been shown to be involved in mRNA processing and export.

Recent studies have suggested that Proliferating Cell Nucleolar Antigen p120 may be a potential drug target for treating E. bieneusi infections. Inhibition of the protein’s function could prevent the growth and proliferation of the parasite, leading to the clearance of the infection.

Enterocytozoon bieneusi Proliferating Cell Nucleolar Antigen p120 is a crucial protein in the biology and pathogenesis of microsporidia infections. Its involvement in ribosome biogenesis and mRNA processing makes it a potential drug target for treating E. bieneusi infections.

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.

The cDNA and recombinant antigens derived from E. bieneusi can be used in the development of such tests. cDNA and recombinant antigens can be used in various applications, including PCR-based detection assays, ELISAs, and immunoblotting. PCR-based detection assays allow for the rapid and sensitive detection of E. bieneusi infection. ELISAs are useful for the semi-quantitative detection of E. bieneusi-specific antibodies in serum and other body fluids. Immunoblotting is useful for the qualitative detection of E. bieneusi-specific antibodies in serum and other body fluids. cDNA and recombinant antigens can also be used in the development of vaccines and immunotherapeutic agents to prevent and treat E. bieneusi infection.