Helicobacter pylori cDNA and Antigen

Helicobacter pylori is a gram-negative bacterium that colonizes the human stomach and can cause chronic gastritis, peptic ulcers, and gastric cancer. Several antigens and proteins of H. pylori have been identified as important targets for the immune response against this bacterium.

The 36 kDa antigen of H. pylori is a surface-exposed protein that has been shown to induce a strong humoral immune response in infected individuals. Antibodies against this protein have been shown to reduce bacterial colonization and inflammation in infected individuals, indicating its potential as a target for vaccine development and immunotherapy.

The cytotoxicity-associated immunodominant antigen (CagA) of H. pylori is a protein that is injected into host cells via a type IV secretion system. CagA has been shown to induce cell signaling pathways that lead to inflammation, cell proliferation, and cancer development. Antibodies against CagA have been shown to reduce the risk of gastric cancer in infected individuals, indicating its potential as a target for immunotherapy and prevention of cancer development.

Protective surface antigen D15 is a protein that is exposed on the surface of H. pylori and has been shown to be involved in bacterial adhesion and colonization. Antibodies against this protein have been shown to reduce bacterial colonization and inflammation in infected individuals, indicating its potential as a target for vaccine development and immunotherapy.

The surface antigen protein with a signal peptide of H. pylori is involved in bacterial adhesion and colonization. This protein has been shown to induce a strong humoral immune response in infected individuals, and antibodies against it have been shown to reduce bacterial colonization and inflammation.

Urease, a protein consisting of subunit alpha and beta, is an immunodominant antigen of H. pylori that is involved in bacterial survival in the acidic environment of the stomach. Urease neutralizes stomach acid by catalyzing the hydrolysis of urea to produce ammonia, which can neutralize acid. Antibodies against urease have been shown to reduce bacterial colonization and inflammation in infected individuals.

The 60 kDa chaperonin of H. pylori is a protein that is involved in bacterial protein folding and has been shown to induce a cellular immune response in infected individuals.

Understanding the roles and functions of these antigens and proteins can aid in the development of novel therapies and vaccines for H. pylori infections. Further research is needed to fully understand their mechanisms of action and optimize their use in therapeutic and diagnostic applications.

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.

Helicobacter pylori cDNA and recombinant antigens can be used in a variety of applications. They can be used in diagnostic tests to detect the presence of H. pylori in a patient’s sample. They can also be used in vaccine development to help stimulate the body’s immune system to recognize the pathogen. Additionally, they can be used in research to better understand the genetic makeup of H. pylori and how it interacts with the human body. Finally, they can be used in drug discovery and development to identify potential new treatments for H. pylori infection.