Interferons (IFNs) are natural glycoproteins belonging to the cytokine superfamily and are produced by the cells of the immune system of most vertebrates in response to challenges by foreign agents such as viruses, parasites, and tumor cells. Interferon-beta (IFN beta) is an extracellular protein mediator of host defense and homeostasis. IFN beta has well-established direct antiviral, antiproliferative, and immunomodulatory properties. Recombinant IFN beta is approved for the treatment of relapsing-remitting multiple sclerosis. The recombinant IFN beta protein has the theoretical potential to either treat or causes autoimmune neuromuscular disorders by altering the complicated and delicate balances within the immune system networks. It is the most widely prescribed disease-modifying therapy for multiple sclerosis (MS). IFN beta is effective in reducing relapses in secondary progressive MS and may have a modest effect in slowing disability progression. In addition to the common antiviral activity, IFN beta also induces increased production of the p53 gene product which promotes apoptosis and thus has a therapeutic effect against certain cancers. The role of IFN-beta in bone metabolism could warrant its systematic evaluation as a potential adjunct to therapeutic regimens of osteolytic diseases. Furthermore, IFN beta might play a beneficial role in the development of chronic progressive CNS inflammation.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD119 (cluster of differentiation 119), also known as IFNGR1 ( interferon gamma receptor 1), is part of the heterodimeric gamma interferon receptor which consists of IFNGR1 (CD119) and IFNGR2. The IFNGR1 gene encodes the ligand-binding chain (alpha) of the interteron receptor while IFNGR gene encodes the non-ligand binding partner. The ability of the interferon-γ was achieved through binding to the interferon receptor CD119. After binding, the products of activated T-lymphocytes interferon-γ exerts antiviral activity, growth inhibitory effect, and several immune- regulatory activities on a variety of cell types.
Interferon gamma receptor 1(IFNGR1) encoded by the IFNGR1 gene, is a single-pass type 1 membrane protein which belongs to the type II cytokine receptor family. IFNGR1 is phosphorylated at Ser/Thr residues after translation. IFNGR1 is a receptor for interferon gamma, two receptors bind one interferon gama dimer. A genetic variation in IFNGR1 is associated with susceptibility to Helicobacter pylori infection. In addition, defects in IFNGR1 are a cause of mendelian susceptibility to mycobacterial disease, also known as familial disseminated atypical mycobacterial infection.
Interferon omega-1 is also known as Interferon alpha-II-1and IFNW1. It is a Secreted protein that in humans is encoded by the IFNW1 gene. IFNW1 belongs to the alpha/beta interferon family. Type I IFNs consist of IFN α, β, τ, and ω and bind to the type I IFN receptor, whereas IFN-γ is the only type II IFN and is specific for the type II IFN receptor. IFNW1 is a recently discovered protein structurally related to IFN-alpha and –beta. It has been shown that IFN-omega 1 similar to that of other human class I IFNs; potent antiviral activity was also observed on cells of bovine and ovine but not of equine or murine origin.
At least 23 different variants of IFN-α are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-α subtypes differ in their sequences by only one or two positions. Naturally occurring variants also include proteins that are truncated by 10 amino acids at the carboxyl-terminal end.
At least 23 different variants of IFN-α are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-α subtypes only differ in their sequences by one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.
Interferon-alpha 2 (IFN alpha-2) is one of 14 subtypes with anin the IFN-alpha class of Type I Interferons. The members of the IFN-alpha class, also known as alpha leukocyte interferons, encompass a group of distinct but closely related proteins which share approximately 80% amino acid (aa) sequence identity and have a similar globular structure composed of five alpha-helices. IFN-alpha class members signal through a common cell surface receptor complex composed of IFN-alpha R2 and IFN-alpha R1 subunits. As the first highly active IFN to be cloned and produced, IFN alpha-2 has become the prototypic IFN for academic and pharmaceutical research. The mature extracellular domain (ECD) of mouse IFN alpha-2 shares 60% and 83% aa sequence identity with an human and rat, respectively. Murine IFN-alpha 2 can eliminate cardiac viral load and protect cardiomyocytes from injury in animals infected with an coxsackievirus B3 (CVB3). IFN alpha-2 derived mutants with an reduced IFNR2 binding inhibited HIV replication and mutants with an more IFNAR1 binding potentiated antiviral activity.
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