Bacteroides fragilis cDNA and Antigen

Bacteroides fragilis is a Gram-negative bacterium that is part of the normal flora of the human gastrointestinal tract. However, in certain conditions, it can cause infections such as peritonitis, abscesses, and bacteremia. Here, we will explore three key components of Bacteroides fragilis that are related to its pathogenicity: Cpn60 groEL protein, Major OmpA, and Surface Antigen.

Cpn60 groEL protein:

The Cpn60 groEL protein is a chaperonin protein that is important for protein folding and stabilization in Bacteroides fragilis. It is a member of the HSP60 family of heat shock proteins and is found in both the cytoplasm and outer membrane of the bacterium. The Cpn60 groEL protein is believed to play a role in the survival of Bacteroides fragilis in the human host.

Major OmpA:

The Major OmpA (Outer membrane protein A) is a surface protein that is involved in the interaction between Bacteroides fragilis and the host. It is known to elicit an immune response in the host, and it is believed to be important for the adhesion of the bacterium to host cells. Additionally, the Major OmpA is also believed to play a role in the resistance of Bacteroides fragilis to antimicrobial agents.

Surface Antigen:

The surface antigen of Bacteroides fragilis is a complex of polysaccharides and glycoproteins that is found on the surface of the bacterium. It is believed to play a role in the adhesion of Bacteroides fragilis to host cells and in the evasion of the host immune system. The surface antigen is highly variable, with different strains of Bacteroides fragilis having different surface antigen profiles.

In conclusion, the Cpn60 groEL protein, Major OmpA, and Surface Antigen of Bacteroides fragilis are important components related to the pathogenicity of this bacterium. Further research is needed to fully understand their roles in the interaction between Bacteroides fragilis and the host, as well as their potential as targets for the development of new treatments for infections caused by this bacterium.

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.