Leishmania chagasi is a parasitic protozoan that causes visceral leishmaniasis, a severe and potentially fatal disease in humans. It is transmitted to humans through the bites of infected sandflies. The disease is prevalent in many parts of the world, including India, Bangladesh, Nepal, Sudan, and Brazil. The treatment for this disease is challenging, and there is no vaccine available to prevent it. However, researchers have identified various surface proteins that could help in the development of an effective vaccine.

Guanine Nucleotide-binding Protein Subunit Beta-like Protein:
Guanine nucleotide-binding protein subunit beta-like protein is a protein found on the surface of Leishmania chagasi. It plays a crucial role in the parasite’s survival and virulence. Studies have shown that Guanine nucleotide-binding protein subunit beta-like protein could be a potential vaccine candidate against visceral leishmaniasis.

Major Surface Protein Associated Protein:
Major surface protein associated protein is another protein found on the surface of Leishmania chagasi. It is essential for the survival and growth of the parasite. Researchers have identified Major surface protein associated protein as a potential vaccine candidate against visceral leishmaniasis.

Leishmania chagasi cDNA and recombinant antigens have been used for the diagnosis of canine visceral leishmaniasis. The cDNA and recombinant antigens are used in various serological tests to detect antibodies and antigens of the Leishmania species in the patient’s serum. These tests include the indirect immunofluorescence assay (IFA), enzyme-linked immunosorbent assay (ELISA), and Western blot. The cDNA and recombinant antigens are also used in direct tests, such as the direct agglutination test (DAT), which detects Leishmania antigens in the patient’s serum. The cDNA and recombinant antigens can also be used in polymerase chain reaction (PCR) to detect Leishmania DNA in the patient’s serum. These tests can be used to accurately diagnose canine visceral leishmaniasis in a timely manner.

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.