Anaplasma marginale cDNA and recombinant antigen

Anaplasma marginale is a bacterium that can cause anaplasmosis, a serious disease that affects cattle. Understanding the role of specific proteins in the pathogenesis of this disease is critical to developing effective treatments and prevention strategies. In this article, we will explore the function and importance of several key proteins, including 60 kDa chaperonin, Ana29, Major Surface Antigen 4 (MSA-4), Major Surface Protein 1 beta 2 (MSP1b2), Surface Antigen AmI95, AmV70, and msp1 beta chain.

60 kDa chaperonin

60 kDa chaperonin is a protein that helps Anaplasma marginale survive and thrive within the host’s bloodstream. This protein acts as a molecular chaperone, assisting in the folding and assembly of other proteins necessary for the bacterium’s survival.

Ana29

Ana29 is another protein produced by Anaplasma marginale. This protein is a surface-exposed protein that plays a key role in the bacterium’s ability to infect host cells. Studies have shown that antibodies against Ana29 can provide partial protection against anaplasmosis, making it an important target for vaccine development.

MSA-4

MSA-4 is a major surface antigen produced by Anaplasma marginale. This protein is involved in the bacterium’s ability to evade the host’s immune system. MSA-4 interacts with host cells, allowing the bacterium to remain undetected and continue to proliferate within the host’s bloodstream.

MSP1b2

MSP1b2 is another major surface protein produced by Anaplasma marginale. This protein is involved in the bacterium’s ability to adhere to host cells, allowing it to establish infection and evade the host’s immune system.

Surface Antigen AmI95 and AmV70

Surface Antigen AmI95 and AmV70 are two additional surface-exposed proteins produced by Anaplasma marginale. These proteins play important roles in the bacterium’s ability to adhere to and invade host cells, leading to the development of anaplasmosis.

msp1 beta chain

msp1 beta chain is a protein that is critical to the survival and replication of Anaplasma marginale. This protein is involved in the synthesis of heme, an important molecule for the bacterium’s survival within the host’s bloodstream.

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. Codon-optimized cDNA is cloned into E. coli expression vector with 6x His-tag at N-terminus and ready-to-use for recombinant protein production.