Ehrlichia chaffeensis cDNA and Antigen

Ehrlichia chaffeensis is a species of bacteria that is a causative agent of human ehrlichiosis, a vector-borne infectious disease. It is transmitted by the Lone star tick (Amblyommaamericanum). It primarily affects white blood cells, and can cause fever, headaches, fatigue, and muscle pains. In severe cases, it can lead to complications such as meningoencephalitis and acute respiratory distress syndrome (ARDS). Treatment typically involves antibiotics such as doxycycline or tetracycline. The bacterium expresses several virulence factors, including outer membrane proteins and surface antigens, that play a critical role in the pathogenesis of the disease.

Here are some of the important Ehrlichia chaffeensis virulence factors:

28 kDa proteins: E. chaffeensis expresses three 28 kDa proteins (gene 14, gene 16, and gene 18) that are thought to be involved in host-pathogen interactions.

60 kDa chaperonin Cpn60: This protein is a member of the chaperonin family and is essential for bacterial survival. It is also recognized by the host immune system and has been shown to induce a strong antibody response.

Immunodominant surface protein gp47: This protein is a major target of the host immune response and is believed to be involved in the adhesion and invasion of host cells.

Major OMP-1A: This is a major outer membrane protein of E. chaffeensis that has been shown to play a critical role in bacterial pathogenesis.

Surface antigen D15: This antigen is an immunodominant surface protein that has been shown to be involved in the adhesion and invasion of host cells.

Surface antigen msp4: This antigen is also an immunodominant surface protein that is thought to play a role in bacterial pathogenesis.

120 kDa immunodominant surface protein: This protein is the most abundant protein in the outer membrane of E. chaffeensis and is a major target of the host immune response.

Understanding the function of these virulence factors is critical for the development of effective therapies and vaccines against E. chaffeensis.

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.

One application of E. chaffeensis cDNA is in the identification of virulence factors. By sequencing and analyzing cDNA libraries, researchers can identify genes that are important for the pathogenesis of the bacterium, providing insights into the mechanisms of infection.

Recombinant antigens derived from E. chaffeensis have been used in the development of diagnostic tests for HME. These tests are based on the detection of antibodies against specific antigens in the patient’s serum. Recombinant antigens have been shown to have improved sensitivity and specificity compared to traditional diagnostic tests, making them useful tools for the rapid and accurate diagnosis of HME.

Another application of recombinant antigens is in the development of a vaccine for Ehrlichia chaffeensis. Several recombinant antigens have been shown to elicit a protective immune response in animal models and are being evaluated in preclinical and clinical trials.