The EBI3 gene is linked to the Epstein-Barr virus-induced gene 3; which is also known by the names interleukin-27 subunit beta or IL27, it is a protein. EBI3 is produced in E.Coli, which is a single, non-glycosylated, polypeptide chain, which contains 209 amino acids and has a molecular weight of 23.3. EBI3 is purified using proprietary chromatographic techniques, ensuring it is safe to be used medically.
An immunosuppressive protein, EBI3 / IL27, can be used to treat a range of autoimmune diseases, such as inflammatory bowel disease. How this works is that by specifically targeting a localized area of the intestine, EBI3 was actively synthesized, and so was able to reduce the impact of IBD on mice, which means that there is potential for success when treating humans.
The structure of EBI3, which is typical for soluble cytokine receptors, is made up of a double pair of modified FNIII domains. This surface tends to contain two cysteine residues, which are forming bridges and have a WSXWS motif, the signature of this binding. In the EBI3 protein, the sequence of WSXWS is located in between the F and G strands, which is LSDWS, the amino acid positions 214 - 218. Among the IL family members, EBI3 is unique, because it lacks N-terminal immunoglobulin. Studies have shown that the EBI3 / IL27 interface is made up of two areas that have hydrophobic and polar properties. Both EBI3 / IL27 come from an aromatic hydrophobic cluster, which is surrounded by a polar area. There is no crystal structure of EBI3 / IL27; the structure adopts a four-helix bundle fold, the combination contains a stretch of consecutive glutamic amino acid residues which is unique to the IL12 family cytokines and may contribute to the activity of these cytokines.
Identified by the induction of its expression in B lymphocytes by the Epstein-Barr viruses infection. This protein is a type of glycoprotein, which is also a member of the hematopoietin receptor family and is related to p40 subunit of interleukin 12. This gene helps to regulate cell-mediated immune responses. It is a subunit of two heterodimeric cytokines: interleukin-27 and interleukin-35. The link occurs because IL27 is made up of p28 and EBI3. What makes IL27 special is the fact that it can trigger signalling in T cells, B cells, and myeloid cells. It has also been suggested that IL27 may be one of the genes that is differentially expressed by septicemic patients and healthy controls. It has been shown that levels of serum in patients with sepsis are elevated, and the same applies to animals.
The protein that this gene is encoded with is one of the subunits of a heterodimeric cytokine complex. Related to the interleukin 12A protein, this protein interacts with the Epstein-Barr virus-induced gene EBI3 because it is similar to interleukin 12B, known as IL12B. This then forms a complex that forms a vast expansion of naive CD4 T cells. This combination can always connect with interleukin 12, triggering interferon gamma production of naive CD4 T cells.