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.
Interferon-alpha 2 (IFN alpha-2) is one of 14 subtypes within 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 Human and rat, respectively. Murine IFN-alpha 2 can eliminate cardiac viral load and protect cardiomyocytes from injury in animals infected with coxsackievirus B3 (CVB3). IFN alpha-2 derived mutants with reduced IFNR2 binding inhibited HIV replication and mutants with more IFNAR1 binding potentiated antiviral activity.
Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. They are typically divided among three IFN classes: Type I, Type II and Type III. IFNA4 is a secreted protein and produced by macrophages. Two variants of IFNA4 (IFNA4a and IFNA4b) are known, which differ from each other by changes in their coding regions at nucleotide positions 220 and 410 .
Interferon-alpha/beta receptor alpha chain (IFNAR1) is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulates Janus protein kinases; which in turn phosphorylate several proteins; including STAT1 and STAT2. The encoded protein also functions as an antiviral factor. Tyk2 slows down IFNAR1 degradation and that this is due; at least in part; to inhibition of IFNAR1 endocytosis. Mutant versions of IFNAR1; in which Tyr466 is changed to phenylalanine; can act in a dominant negative manner to inhibit phosphorylation of STAT2. These observations are consistent with a model in which IFNAR1 mediates the interaction between JAK kinases and the STAT transcription factors.
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