Campylobacter concisus cDNA and Antigen

Campylobacter concisus is a Gram-negative, curved, or spiral-shaped, motile bacterium of the Campylobacter genus, which is a member of the family Campylobacteraceae. It is a commensal organism which is found in the mucosal surfaces of humans, including the oral cavity, gastrointestinal tract, and genitourinary tract. It is one of the most identified species in the oral cavity and is associated with periodontal disease and inflammatory bowel disease. C. concisus can cause gastroenteritis in humans, especially in young children, but it is not considered a major pathogen. Treatment typically involves the use of antibiotics, although some strains of C. concisus are resistant to certain antibiotics.

The Campylobacter concisus produces various antigens that play an important role in its pathogenesis. Some of the key antigens produced by Campylobacter concisus, include acid membrane antigen A, invasion antigen B, CjaA, and the 60 kDa chaperonin.

Acid Membrane Antigen A:Acid membrane antigen A (AMA) is a 28 kDa protein that is exposed on the surface of Campylobacter concisus. This antigen is believed to play a crucial role in the pathogenesis of Campylobacter-associated infections. In addition to being a potential vaccine candidate, AMA has also been used as a target in diagnostic tests for Campylobacter infections.

Invasion Antigen B:Invasion antigen B (IAB) is a 42 kDa protein that is involved in the invasion of host cells by Campylobacter concisus. This antigen is believed to be important in the bacterium’s ability to colonize the human gut and cause disease. Studies have shown that antibodies against IAB can protect against Campylobacter infection in animal models, suggesting that this antigen could be a potential target for vaccine development.

CjaA:CjaA is a 37 kDa protein that is expressed on the surface of Campylobacter concisus. This antigen is believed to be involved in the bacterium’s adherence to host cells. Studies have shown that antibodies against CjaA can inhibit the binding of Campylobacter concisus to host cells, suggesting that this antigen could be a target for the development of novel therapeutics.

60 kDa Chaperonin:The 60 kDa chaperonin is a heat shock protein that is involved in protein folding and stability. This protein has been identified as an antigen in Campylobacter concisus infections, and antibodies against it have been detected in patients with the bacterium. However, the role of the 60 kDa chaperonin in the pathogenesis of Campylobacter infections is not well understood.

In conclusion, Campylobacter concisus produces several antigens that play important roles in its pathogenesis. Acid membrane antigen A, invasion antigen B, CjaA, and the 60 kDa chaperonin are some of the key antigens produced by this bacterium. Further research on these antigens could lead to the development of novel therapeutics and vaccines against Campylobacter infections.

Campylobacter concisus is a Gram-negative bacterial species that can cause gastrointestinal illnesses. The cDNA of this species, as well as its recombinant antigens, can be used in a variety of medical applications.

One application is in the diagnosis of Campylobacter infection. The cDNA of the species can be used to detect the presence of the microbe in a sample, enabling the detection of active infections. The recombinant antigens can be used for serological tests, to detect the presence of antibodies that indicate a past or current infection.

cDNA and recombinant antigens can also be used to develop vaccines and other therapeutic interventions. Vaccines based on the cDNA or antigens of Campylobacter concisus could be used to prevent infection, while other therapeutic interventions could be used to treat active infections.

Finally, the cDNA and recombinant antigens of Campylobacter concisus can also be used in research applications. For example, the cDNA can be used to study the genetic makeup of the microbe and its gene expression, while the antigens can be used to study the immune response to the microbe.

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.