Plasmodium malariae is a species of malaria parasite that primarily affects humans. Although it is not as common as Plasmodium falciparum or Plasmodium vivax, it can still cause significant illness and even death in some cases.

One of the key proteins in P. malariae is dihydrofolate reductase-thymidylate synthase. This protein plays a crucial role in the parasite’s ability to synthesize DNA. Specifically, it catalyzes the conversion of dihydrofolate to tetrahydrofolate, which is necessary for the synthesis of thymidine, a key component of DNA.

Another important protein in P. malariae is the circumsporozoite protein. This protein is present on the surface of the parasite’s sporozoite stage, which is the form of the parasite that is transmitted to humans by the bite of an infected mosquito. The circumsporozoite protein plays a critical role in the parasite’s ability to invade and infect human liver cells.

Lactate dehydrogenase (LDH) is yet another key protein in P. malariae. This enzyme is involved in the parasite’s energy metabolism, specifically in the conversion of pyruvate to lactate. LDH is also used as a diagnostic marker for malaria, as it is released by the parasite into the bloodstream during infection.

Understanding the roles of these proteins in P. malariae is important for the development of effective treatments and preventative measures against this malaria species. Ongoing research into the parasite’s biology and molecular mechanisms could lead to new therapies and strategies for combating malaria infections.

The application of Plasmodium malariae cDNA and recombinant antigen can be in several areas, including:
Diagnosis: cDNA and recombinant antigen can be used to develop diagnostic tests for malaria. For example, specific genes from the parasite can be cloned and used as probes in polymerase chain reaction (PCR) assays to detect the presence of the parasite in blood samples. Similarly, recombinant antigens can be used in serological tests to detect antibodies against the parasite.
Vaccine development: cDNA and recombinant antigen can be used to develop vaccines against malaria. The genes that encode important surface proteins or other antigens of the parasite can be cloned and expressed as recombinant antigens to induce an immune response against the parasite. Similarly, cDNA can be used to identify genes that are important for parasite survival, and these genes can be targeted to develop new vaccine candidates.

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.