Aeromonas hydrophila cDNA and Antigen

Aeromonas hydrophila is a gram-negative bacterium that can cause various infections in both humans and animals. The antigens are specific proteins or molecules present on the surface of the bacterium and can be used to identify or diagnose infections caused by this bacterium.

The 17 kDa antigen and 27 kDa antigen are two specific proteins that are present in the outer membrane of Aeromonas hydrophila. These antigens have been shown to be immunogenic and can elicit an immune response in infected individuals. The 17 kDa antigen has been suggested to be a potential diagnostic marker for Aeromonas hydrophila infections.

OPRM (Outer membrane protein R) is another protein present in the outer membrane of Aeromonas hydrophila. This protein has been shown to be involved in the adherence and colonization of the bacterium in host cells.

The surface antigen is a general term used to refer to any antigenic molecule present on the surface of the bacterium. In the case of Aeromonas hydrophila, there are several surface antigens that have been identified and characterized, including the O-antigen and the H-antigen. These surface antigens can also be used for diagnostic purposes.

Aeromonas hydrophila cDNA and recombinant antigen are important tools for the investigation of the pathogenicity, virulence, and immunogenicity of this organism. cDNA allows for the study of gene expression, while recombinant antigens can be used to identify, study, and quantify specific proteins. This description focuses on the use of these tools to explore the molecular basis of Aeromonas hydrophila pathogenesis, enabling researchers to better understand the mechanisms of this organism and develop novel treatments.

The antigen of A. hydrophila is a bacterial protein or polysaccharide which is recognized by the host’s immune system, triggering an immune response. Antigens from A. hydrophila can be used in vaccines, diagnostics, and for research purposes. The antigenic structure of the bacterium includes lipopolysaccharides, flagellar proteins, and outer membrane proteins. These antigens can be extracted from the bacterium or synthesized in the laboratory.

The use of recombinant proteins/cDNA in academic research and diagnostic 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.