Amoebophrya karlodinium is a parasitic dinoflagellate that infects Karlodiniumveneficum, a toxic algal species that causes harmful algal blooms (HABs) in marine ecosystems. The parasite is known to infect and kill K. veneficum cells, but the mechanisms behind this process are not well understood.

One protein that has been identified in Amoebophrya karlodinium is the blood stage antigen 41-3-like protein, which is similar to a protein found in the blood stage of the malaria parasite. While the function of this protein in the parasite-host interaction is not fully known, it has been suggested that it may play a role in the recognition and attachment of the parasite to the host cell.

The relationship between Amoebophrya karlodinium and Karlodiniumveneficum has important implications for marine ecosystems, as harmful algal blooms can have negative effects on water quality, marine life, and human health. Understanding the interactions between these two organisms can help us develop strategies to mitigate the effects of HABs and protect the health of marine ecosystems.

Additionally, the blood stage antigen 41-3-like protein found in Amoebophrya karlodinium is of interest for its potential as a diagnostic or therapeutic target in malaria research. While the protein’s exact function in the parasite-host interaction is still being studied, its similarity to the malaria protein suggests that it may have similar functions in the malaria parasite as well. Further research on this protein could lead to the development of new treatments and prevention strategies for malaria, a disease that affects millions of people worldwide.

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.