Ixodes scapularis, commonly known as the Deer tick, is a species of hard-bodied tick that is found in North America. This tick is known to carry and transmit several pathogens, including Borrelia burgdorferi, which is responsible for causing Lyme disease.

Ixodes scapularis also produces several salivary gland proteins that play a critical role in its feeding process. One of these proteins is the protective antigen 4D8, also known as subolesin, which is involved in tick development and reproduction.

In addition to 4D8, Ixodes scapularis produces several other salivary gland proteins, including 15 kDa and 14 kDa proteins, as well as 17 kDa, 20 kDa, 25 kDa, and 26 kDa proteins. These proteins are involved in various functions, such as regulating host immune response, binding to histamine, and scavenging reactive oxygen species.

Furthermore, Ixodes scapularis also produces glutathione peroxidase, which helps to protect the tick against oxidative stress, and salp10, which has been shown to inhibit the activity of platelet-derived growth factor.

Another notable salivary gland protein produced by Ixodes scapularis is the histamine binding protein, which binds to histamine and other biogenic amines. This protein is thought to play a role in the tick’s feeding process by preventing host inflammation and itching.

Lastly, Ixodes scapularis produces thrombospondin, a glycoprotein that has been shown to inhibit angiogenesis and induce apoptosis in various cell types. This protein is involved in the tick’s feeding process by promoting wound healing and preventing host immune response.

Overall, the salivary gland proteins produced by Ixodes scapularis play a critical role in the tick’s feeding process and survival. Understanding these proteins and their functions may help in the development of new strategies for controlling tick-borne diseases.

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.

The cDNA (complementary DNA) of Ixodes scapularis can be used to produce recombinant antigens that have several applications, including:

Diagnosis of tick-borne diseases: Recombinant antigens derived from Ixodes scapularis cDNA can be used as diagnostic markers for the detection of tick-borne diseases. These antigens can be used in diagnostic tests, such as ELISA, to detect antibodies produced by the host against the tick-borne pathogen.

Vaccine development: Recombinant antigens from Ixodes scapularis cDNA can also be used to develop vaccines against tick-borne diseases. These antigens can be used to stimulate the immune system to produce a protective response against the tick, thereby preventing transmission of the disease.