Plasmodium Berghei is a protozoan parasite that is responsible for causing malaria in rodents. The parasite is closely related to Plasmodium falciparum, which is responsible for causing malaria in humans. Plasmodium Berghei is commonly used as a model organism for studying the pathology and treatment of malaria.

Plasmodium berghei antigens are proteins, lipids and carbohydrates found on the surface of the parasite that plays a role in its ability to cause malaria. These antigens can be used for diagnostic and vaccine development purposes. Examples of Plasmodium berghei antigens include merozoite surface proteins, circumsporozoite proteins, and glutamate-rich protein.

MatureCircumsporozoite Protein (CS) is a protein that is produced by the Plasmodium Berghei parasite during the sporozoite stage of its life cycle. This protein is essential for the invasion of the parasite into the host’s liver cells, where it can multiply and cause further damage.

Erythrocyte-binding-like Protein is a group of proteins that are produced by the Plasmodium Berghei parasite during the blood stage of its life cycle. These proteins play a critical role in the invasion of the parasite into the host’s red blood cells, where it can cause the characteristic symptoms of malaria, such as fever and chills.

Recent studies have shown that Plasmodium Berghei can have a significant impact on the production of both MatureCircumsporozoite Protein (CS) and Erythrocyte-binding-like Protein. These proteins are essential for the survival of the parasite and its ability to cause disease in the host.

In particular, MatureCircumsporozoite Protein (CS) has been found to be a promising target for the development of new malaria vaccines. By targeting this protein, researchers hope to be able to prevent the parasite from invading the host’s liver cells and multiplying.

Similarly, Erythrocyte-binding-like Protein has been identified as a potential target for the development of new antimalarial drugs. By targeting this protein, researchers hope to be able to prevent the parasite from invading the host’s red blood cells and causing the characteristic symptoms of malaria.

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.