Trypanosoma cruzi is a parasitic protozoan that causes Chagas disease, a potentially life-threatening illness that affects millions of people worldwide. The disease is primarily found in Latin America, where it is transmitted to humans through the bite of an infected triatomine bug, also known as the “kissing bug.” While there is currently no effective vaccine for Chagas disease, efforts are underway to develop new treatments based on understanding the biology of T. cruzi and its antigens.

T. cruzi is known to express a wide variety of antigens that are involved in different stages of the parasite’s life cycle and in host-parasite interactions. Some of the most important antigens of T. cruzi include:

A13 and 38: These two antigens are expressed on the surface of the parasite and have been shown to elicit a strong immune response in infected individuals. They are being studied as potential targets for vaccines and diagnostic tests.

Tc40: This antigen is found in the cytoplasm of T. cruzi and is thought to be involved in the parasite’s ability to invade host cells. It is being studied as a potential target for drug development.

Sialidase-Neuraminidase: This antigen is involved in the parasite’s ability to modify host cell surfaces, which helps the parasite to evade the host immune system. It is being studied as a potential target for vaccines and drug development.

PHGST 5: This antigen is expressed on the surface of the parasite and has been shown to elicit a strong immune response in infected individuals. It is being studied as a potential target for vaccines and diagnostic tests.

Amastigote cytoplasmic antigen: This antigen is expressed during the intracellular stage of the parasite’s life cycle and is involved in the replication of the parasite within host cells. It is being studied as a potential target for drug development.

Surface antigen: This antigen is expressed on the surface of the parasite and has been shown to elicit a strong immune response in infected individuals. It is being studied as a potential target for vaccines and diagnostic tests.

Insect stage-specific antigen: This antigen is expressed during the insect stage of the parasite’s life cycle and is involved in the parasite’s interaction with the insect vector. It is being studied as a potential target for drug development.

24 kDa antigen-ALC-1 antigen: This antigen is involved in the attachment of the parasite to host cells and is being studied as a potential target for drug development.

P21 antigen protein: This antigen is expressed on the surface of the parasite and has been shown to elicit a strong immune response in infected individuals. It is being studied as a potential target for vaccines and diagnostic tests.

Major 85 kDa surface antigen: This antigen is expressed on the surface of the parasite and has been shown to elicit a strong immune response in infected individuals. It is being studied as a potential target for vaccines and diagnostic tests.

Sialidase Major surface antigen: This antigen is involved in the parasite’s ability to modify host cell surfaces and is being studied as a potential target for vaccines and drug development.

Application of Trypanosoma cruzi cDNA and recombinant antigen in the diagnosis of Chagas’ disease. The cDNA and antigen can be used to detect the presence of the parasite in a sample, and to identify its genetic variability. This can help to improve the accuracy of the diagnosis, and to
improve the management of the disease. Furthermore, the use of these techniques can also be used to monitor the spread of the disease, and to
monitor the efficacy of treatments.

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.