Leishmania major is the causative agent of cutaneous leishmaniasis, a disease that affects the skin and mucous membranes. The parasite has developed several mechanisms to evade the host immune system, including the expression of various surface antigens that can modulate the immune response.

One of the key surface antigens of Leishmania major is Hydrophilic surface protein 1 and 2 (HSP1/2), which are highly expressed during the promastigote stage of the parasite’s life cycle. HSP1/2 are believed to play a role in the binding and internalization of the parasite into host cells, as well as in modulating the host immune response.

Another important surface antigen of Leishmania major is 40S ribosomal protein S3a (RPS3a), which has been shown to induce a strong T-cell response in infected individuals. This antigen is also conserved among different Leishmania species and has shown potential as a vaccine target.

In addition to HSP1/2 and RPS3a, Leishmania major also expresses several other surface antigens, including Surface antigen protein, Proliferating cell nuclear antigen (PCNA), Thiol-specific antioxidant antigen (TSA), Possible surface antigen, Viscerotropic leishmaniasis antigen, and the strain Friedlin p21 antigen protein. Each of these antigens has been studied for their potential as vaccine targets or diagnostic markers for leishmaniasis.

Leishmania major cDNA and recombinant antigens can be used in a variety of applications, including diagnosis and vaccine development. In diagnosis, the Leishmania major cDNA or recombinant antigens can be used to detect the presence of Leishmania major in a sample. This can be done through PCR or ELISA techniques. The cDNA or recombinant antigens can also be used to develop vaccines that can induce an immune response against the parasite. This could be used to prevent or even cure leishmaniasis. Additionally, the cDNA can be used to study the genetic makeup of the parasite and further our understanding 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.