Yersinia enterocolitica cDNA and recombinant antigen

Yersinia enterocolitica is a Gram-negative, rod-shaped bacterium that is part of the family Enterobacteriaceae. It is a human pathogen that can cause gastroenteritis, sepsis, and lymphadenitis. In humans, the main symptoms are abdominal pain, diarrhea, and fever. Other symptoms may include nausea, vomiting, and bloody stools. The bacteria are spread through contaminated food, water, and contact with infected individuals. Treatment includes antibiotics, such as tetracyclines, aminoglycosides, and cephalosporins. Vaccines are available for animals, but not for humans. It produces several key antigens including:

One of the key proteins associated with Yersinia enterocolitica is the 60 kDa chaperonin Cpn60. This protein plays a vital role in the folding and stabilization of other proteins within the bacterium. It is also thought to play a role in the virulence of Yersinia enterocolitica, helping the bacterium to evade the immune system of the host.

Another important protein associated with Yersinia enterocolitica is the V antigen. This protein is located on the surface of the bacterium and is involved in the inhibition of the host’s immune response. It is also thought to play a role in the bacterium’s ability to invade host cells.

The pH 6 antigen is another key protein associated with Yersinia enterocolitica. This protein is thought to play a role in the bacterium’s survival within the host’s acidic stomach environment. It is also involved in the bacterium’s ability to adhere to host cells, allowing it to colonize the gastrointestinal tract.

Finally, the Adhesin 4 protein is another important component of Yersinia enterocolitica. This protein is involved in the bacterium’s ability to adhere to host cells, allowing it to colonize the host’s gastrointestinal tract. It is also thought to play a role in the formation of biofilms, which can protect the bacterium from antibiotics and the host’s immune system.

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.

For diagnostic purposes, cDNA and recombinant antigens can be used to detect the presence of Yersinia enterocolitica in clinical samples. A sandwich enzyme-linked immunosorbent assay (ELISA) can be used to detect the presence of the bacteria in a sample. The ELISA utilizes two different antibodies, one of which is specific to Yersinia enterocolitica and the other to a known antigen of the bacteria. The presence of the bacteria in the sample can then be detected by measuring the levels of the antigen in the sample.

In vaccine development, cDNA and recombinant antigens can be used to develop a vaccine that provides immunity against Yersinia enterocolitica. This can be done by generating a recombinant protein from the cDNA sequence of the bacteria, which can be used to generate an immune response against the bacteria. The recombinant protein may be used as a subunit vaccine.