Rickettsia peacockii is a Gram-negative bacterium that belongs to the spotted fever group (SFG) Rickettsiae. It is commonly found in various tick species and is known to cause mild to no symptoms in humans. However, the bacterium’s role as an endosymbiont in ticks and its interactions with other tick-borne pathogens make it an interesting subject for study.

One of the significant features of Rickettsia peacockii is its 17 kDa surface antigen. This protein is a major component of the bacterium’s outer membrane and plays an essential role in its interactions with the tick host. The antigen has been found to be highly conserved across different strains of Rickettsia peacockii, indicating its importance in the bacterium’s life cycle.

Studies have shown that the 17 kDa surface antigen is involved in the attachment of Rickettsia peacockii to the tick host’s gut epithelium. This process is crucial for the bacterium’s colonization of the tick’s midgut and subsequent transmission to the next host. The antigen is also thought to be involved in the bacterium’s ability to evade the tick’s immune system, allowing it to establish a persistent infection in the tick.

Furthermore, the 17 kDa surface antigen has been identified as a potential target for the development of vaccines against tick-borne diseases. This is because the antigen is highly specific to Rickettsia peacockii and does not cross-react with other tick-borne pathogens. Vaccines that target the antigen could potentially reduce the incidence of tick-borne diseases by interfering with the bacterium’s life cycle and preventing its transmission to humans.

It is important to detect antibodies in dogs that have been exposed to this pathogen in order to diagnose the infection and to determine the severity of the disease. To do this, cDNA and recombinant antigen from Rickettsia peacockii can be used to detect antibodies in dogs. The cDNA can be used to create a recombinant antigen that can be used in an ELISA assay to detect antibodies in dogs. The ELISA assay involves coating the antigen onto a plate, then adding a serum sample from a dog. If the dog has been exposed to Rickettsia peacockii, there will be an antibody response, which will be detected by a secondary antibody bound to a detectable label. The presence of the detectable label can then be quantified to determine the concentration of antibodies in the sample. This method can be used to accurately diagnose canine ehrlichiosis and to determine the severity of the disease.

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.