Interferon - wikipedia Interferon `` IFN '' redirects here. For other uses, see IFN ( disambiguation ). Interferon alpha / beta domain The molecular structure of human interferon - alpha Identifiers Symbol Interferons Pfam PF00143 InterPro IPR000471 PROSITE PDOC00225 SCOP 1au1 SUPERFAMILY 1au1 Available protein structures : Pfam structures PDB RCSB PDB ; PDBe ; PDBj PDBsum structure summary Interferons ( IFNs ) are a group of signaling proteins made and released by host cells in response to the presence of several pathogens, such as viruses, bacteria, parasites, and also tumor cells. In a typical scenario, a virus - infected cell will release interferons causing nearby cells to heighten their anti-viral defenses. IFNs belong to the large class of proteins known as cytokines, molecules used for communication between cells to trigger the protective defenses of the immune system that help eradicate pathogens. Interferons are named for their ability to `` interfere '' with viral replication by protecting cells from virus infections. IFNs also have various other functions : they activate immune cells, such as natural killer cells and macrophages ; they increase host defenses by up - regulating antigen presentation by virtue of increasing the expression of major histocompatibility complex ( MHC ) antigens. Certain symptoms of infections, such as fever, muscle pain and `` flu - like symptoms '', are also caused by the production of IFNs and other cytokines. More than twenty distinct IFN genes and proteins have been identified in animals, including humans. They are typically divided among three classes : Type I IFN, Type II IFN, and Type III IFN. IFNs belonging to all three classes are important for fighting viral infections and for the regulation of the immune system. Contents 1 Types of interferon 2 Function 3 Induction of interferons 4 Downstream signaling 5 Virus resistance to interferons 6 Interferon therapy 6.1 Diseases 6.2 Drug formulations 7 History 8 Human interferons 9 See also 10 References Types of interferon Based on the type of receptor through which they signal, human interferons have been classified into three major types. Interferon type I : All type I IFNs bind to a specific cell surface receptor complex known as the IFN - α / β receptor ( IFNAR ) that consists of IFNAR1 and IFNAR2 chains. The type I interferons present in humans are IFN - α, IFN - β, IFN - ε, IFN - κ and IFN - ω. In general, type I interferons are produced when the body recognizes a virus has invaded it. They are produced by fibroblasts and monocytes. However, the production of type I IFN - α is prohibited by another cytokine known as Interleukin - 10. Once released, type I interferons will activate molecules which prevent the virus from producing and replicating its RNA and DNA. Overall, IFN - α can be used to treat hepatitis B and C infections, while IFN - β can be used to treat multiple sclerosis. Interferon type II ( IFN - γ in humans ) : This is also known as immune interferon and is activated by Interleukin - 12. Furthermore, type II interferons are released by T helper cells, type 1 specifically. However, they block the proliferation of T helper cells type two. The previous results in an inhibition of T 2 immune response and a further induction of T 1 immune response, which leads to the development of debilitating diseases such as multiple sclerosis. IFN type II binds to IFNGR, which consists of IFNGR1 and IFNGR2 chains and has a different receptor than type I IFN. Interferon type III : Signal through a receptor complex consisting of IL10R2 ( also called CRF2 - 4 ) and IFNLR1 ( also called CRF2 - 12 ). Although discovered more recently than type I and type II IFNs, recent information demonstrates the importance of Type III IFNs in some types of virus infections. In general, type I and II interferons are responsible for regulating and activating the immune response. Expression of type I and III IFNs can be induced in virtually all cell types upon recognition of viral components, especially nucleic acids, by cytoplasmic and endosomal receptors, whereas type II interferon is induced by cytokines such as IL - 12, and its expression is restricted to immune cells such as T cells and NK cells. Function All interferons share several common effects : they are antiviral agents and they modulate functions of the immune system. Administration of Type I IFN has been shown experimentally to inhibit tumor growth in animals, but the beneficial action in human tumors has not been widely documented. A virus - infected cell releases viral particles that can infect nearby cells. However, the infected cell can prepare neighboring cells against a potential infection by the virus by releasing interferons. In response to interferon, cells produce large amounts of an enzyme known as protein kinase R ( PKR ). This enzyme phosphorylates a protein known as eIF - 2 in response to new viral infections ; the phosphorylated eIF - 2 forms an inactive complex with another protein, called eIF2B, to reduce protein synthesis within the cell. Another cellular enzyme, RNAse L -- also induced by interferon action -- destroys RNA within the cells to further reduce protein synthesis of both viral and host genes. Inhibited protein synthesis destroys both the virus and infected host cells. In addition, interferons induce production of hundreds of other proteins -- known collectively as interferon - stimulated genes ( ISGs ) -- that have roles in combating viruses and other actions produced by interferon. They also limit viral spread by increasing p53 activity, which kills virus - infected cells by promoting apoptosis. The effect of IFN on p53 is also linked to its protective role against certain cancers. Another function of interferons is to upregulate major histocompatibility complex molecules, MHC I and MHC II, and increase immunoproteasome activity. Higher MHC I expression increases presentation of viral peptides to cytotoxic T cells, while the immunoproteasome processes viral peptides for loading onto the MHC I molecule, thereby increasing the recognition and killing of infected cells. Higher MHC II expression increases presentation of viral peptides to helper T cells ; these cells release cytokines ( such as more interferons and interleukins, among others ) that signal to and co-ordinate the activity of other immune cells. Interferons, such as interferon gamma, directly activate other immune cells, such as macrophages and natural killer cells. Induction of interferons Production of interferons occurs mainly in response to microbes, such as viruses and bacteria, and their products. Binding of molecules uniquely found in microbes -- viral glycoproteins, viral RNA, bacterial endotoxin ( lipopolysaccharide ), bacterial flagella, CpG motifs -- by pattern recognition receptors, such as membrane bound Toll like receptors or the cytoplasmic receptors RIG - I or MDA5, can trigger release of IFNs. Toll Like Receptor 3 ( TLR3 ) is important for inducing interferons in response to the presence of double - stranded RNA viruses ; the ligand for this receptor is double - stranded RNA ( dsRNA ). After binding dsRNA, this receptor activates the transcription factors IRF3 and NF - κB, which are important for initiating synthesis of many inflammatory proteins. RNA interference technology tools such as siRNA or vector - based reagents can either silence or stimulate interferon pathways. Release of IFN from cells ( specifically IFN - γ in lymphoid cells ) is also induced by mitogens. Other cytokines, such as interleukin 1, interleukin 2, interleukin - 12, tumor necrosis factor and colony - stimulating factor, can also enhance interferon production. Downstream signaling By interacting with their specific receptors, IFNs activate signal transducer and activator of transcription ( STAT ) complexes ; STATs are a family of transcription factors that regulate the expression of certain immune system genes. Some STATs are activated by both type I and type II IFNs. However each IFN type can also activate unique STATs. STAT activation initiates the most well - defined cell signaling pathway for all IFNs, the classical Janus kinase - STAT ( JAK - STAT ) signaling pathway. In this pathway, JAKs associate with IFN receptors and, following receptor engagement with IFN, phosphorylate both STAT1 and STAT2. As a result, an IFN - stimulated gene factor 3 ( ISGF3 ) complex forms -- this contains STAT1, STAT2 and a third transcription factor called IRF9 -- and moves into the cell nucleus. Inside the nucleus, the ISGF3 complex binds to specific nucleotide sequences called IFN - stimulated response elements ( ISREs ) in the promoters of certain genes, known as IFN stimulated genes ISGs. Binding of ISGF3 and other transcriptional complexes activated by IFN signaling to these specific regulatory elements induces transcription of those genes. A collection of known ISGs is available on Interferome, a curated online database of ISGs ( www.interferome.org ) ; Additionally, STAT homodimers or heterodimers form from different combinations of STAT - 1, - 3, - 4, - 5, or - 6 during IFN signaling ; these dimers initiate gene transcription by binding to IFN - activated site ( GAS ) elements in gene promoters. Type I IFNs can induce expression of genes with either ISRE or GAS elements, but gene induction by type II IFN can occur only in the presence of a GAS element. In addition to the JAK - STAT pathway, IFNs can activate several other signaling cascades. For instance, both type I and type II IFNs activate a member of the CRK family of adaptor proteins called CRKL, a nuclear adaptor for STAT5 that also regulates signaling through the C3G / Rap1 pathway. Type I IFNs further activate p38 mitogen - activated protein kinase ( MAP kinase ) to induce gene transcription. Antiviral and antiproliferative effects specific to type I IFNs result from p38 MAP kinase signaling. The phosphatidylinositol 3 - kinase ( PI3K ) signaling pathway is also regulated by both type I and type II IFNs. PI3K activates P70 - S6 Kinase 1, an enzyme that increases protein synthesis and cell proliferation ; phosphorylates of ribosomal protein s6, which is involved in protein synthesis ; and phosphorylates a translational repressor protein called eukaryotic translation - initiation factor 4E - binding protein 1 ( EIF4EBP1 ) in order to deactivate it. Virus resistance to interferons Many viruses have evolved mechanisms to resist interferon activity. They circumvent the IFN response by blocking downstream signaling events that occur after the cytokine binds to its receptor, by preventing further IFN production, and by inhibiting the functions of proteins that are induced by IFN. Viruses that inhibit IFN signaling include Japanese Encephalitis Virus ( JEV ), dengue type 2 virus ( DEN - 2 ) and viruses of the herpesvirus family, such as human cytomegalovirus ( HCMV ) and Kaposi 's sarcoma - associated herpesvirus ( KSHV or HHV8 ). Viral proteins proven to affect IFN signaling include EBV nuclear antigen 1 ( EBNA1 ) and EBV nuclear antigen 2 ( EBNA - 2 ) from Epstein - Barr virus, the large T antigen of Polyomavirus, the E7 protein of Human papillomavirus ( HPV ), and the B18R protein of vaccinia virus. Reducing IFN - α activity may prevent signaling via STAT1, STAT2, or IRF9 ( as with JEV infection ) or through the JAK - STAT pathway ( as with DEN - 2 infection ). Several poxviruses encode soluble IFN receptor homologs -- like the B18R protein of the vaccinia virus -- that bind to and prevent IFN interacting with its cellular receptor, impeding communication between this cytokine and its target cells. Some viruses can encode proteins that bind to double - stranded RNA ( dsRNA ) to prevent the activity of RNA - dependent protein kinases ; this is the mechanism reovirus adopts using its sigma 3 ( σ3 ) protein, and vaccinia virus employs using the gene product of its E3L gene, p25. The ability of interferon to induce protein production from interferon stimulated genes ( ISGs ) can also be affected. Production of protein kinase R, for example, can be disrupted in cells infected with JEV Some viruses escape the anti-viral activities of interferons by gene ( and thus protein ) mutation. The H5N1 influenza virus, also known as bird flu, has resistance to interferon and other anti-viral cytokines that is attributed to a single amino acid change in its Non-Structural Protein 1 ( NS1 ), although the precise mechanism of how this confers immunity is unclear. Interferon therapy Three vials filled with human leukocyte interferon Diseases Interferon beta - 1a and interferon beta - 1b are used to treat and control multiple sclerosis, an autoimmune disorder. This treatment is effective for reducing attacks in relapsing - remitting multiple sclerosis and slowing disease progression and activity in secondary progressive multiple sclerosis. Interferon therapy is used ( in combination with chemotherapy and radiation ) as a treatment for some cancers. This treatment can be used in hematological malignancy ; leukemia and lymphomas including hairy cell leukemia, chronic myeloid leukemia, nodular lymphoma, and cutaneous T - cell lymphoma. Patients with recurrent melanomas receive recombinant IFN - α2b. Both hepatitis B and hepatitis C are treated with IFN - α, often in combination with other antiviral drugs. Some of those treated with interferon have a sustained virological response and can eliminate hepatitis virus. The most harmful strain -- hepatitis C genotype I virus -- can be treated with a 60 - 80 % success rate with the current standard - of - care treatment of interferon - α, ribavirin and recently approved protease inhibitors such as Telaprevir ( Incivek ) May 2011, Boceprevir ( Victrelis ) May 2011 or the nucleotide analog polymerase inhibitor Sofosbuvir ( Sovaldi ) December 2013. Biopsies of patients given the treatment show reductions in liver damage and cirrhosis. Some evidence shows giving interferon immediately following infection can prevent chronic hepatitis C, although diagnosis early in infection is difficult since physical symptoms are sparse in early hepatitis C infection. Control of chronic hepatitis C by IFN is associated with reduced hepatocellular carcinoma. There is low - quality evidence suggesting that interferon eye drops may be an effective treatment for people who have herpes simplex virus epithelial keratitis, a type of eye infection. There is no clear evidence to suggest that removing the infected tissue ( debridement ) followed by interferon drops is an effective treatment approach for these types of eye infections. Low - quality evidence suggests that the combination of interferon and an antiviral agent may speed the healing process compared to antiviral therapy alone. When used in the systemic therapy, IFNs are mostly administered by an intramuscular injection. The injection of IFNs in the muscle or under the skin is generally well tolerated. The most frequent adverse effects are flu - like symptoms : increased body temperature, feeling ill, fatigue, headache, muscle pain, convulsion, dizziness, hair thinning, and depression. Erythema, pain, and hardness on the spot of injection are also frequently observed. IFN therapy causes immunosuppression, in particular through neutropenia and can result in some infections manifesting in unusual ways. Drug formulations Pharmaceutical forms of interferons Generic name Trade name Interferon alpha 2a Roferon A Interferon alpha 2b Intron A / Reliferon / Uniferon Human leukocyte Interferon - alpha ( HuIFN - alpha - Le ) Multiferon Interferon beta 1a, liquid form Rebif Interferon beta 1a, lyophilized Avonex Interferon beta 1a, biogeneric ( Iran ) Cinnovex Interferon beta 1b Betaseron / Betaferon Interferon gamma 1b Actimmune PEGylated interferon alpha 2a Pegasys PEGylated interferon alpha 2a ( Egypt ) Reiferon Retard PEGylated interferon alpha 2b PegIntron PEGylated interferon alpha 2b plus ribavirin ( Canada ) Pegetron Several different types of interferons are approved for use in humans. One was first approved for medical use in 1986. For example, in January 2001, the Food and Drug Administration ( FDA ) approved the use of PEGylated interferon - alpha in the USA ; in this formulation, PEGylated interferon - alpha - 2b ( Pegintron ), polyethylene glycol is linked to the interferon molecule to make the interferon last longer in the body. Approval for PEGylated interferon - alpha - 2a ( Pegasys ) followed in October 2002. These PEGylated drugs are injected once weekly, rather than administering two or three times per week, as is necessary for conventional interferon - alpha. When used with the antiviral drug ribavirin, PEGylated interferon is effective in treatment of hepatitis C ; at least 75 % of people with hepatitis C genotypes 2 or 3 benefit from interferon treatment, although this is effective in less than 50 % of people infected with genotype 1 ( the more common form of hepatitis C virus in both the U.S. and Western Europe ). Interferon - containing regimens may also include protease inhibitors such as boceprevir and telaprevir. History This article relies too much on references to primary sources. Please improve this by adding secondary or tertiary sources. ( July 2014 ) Sidney Pestka of Rutgers University, seen here receiving the National Medal of Technology. Interferons were first described in 1957 by Alick Isaacs and Jean Lindenmann at the National Institute for Medical Research in London ; the discovery was a result of their studies of viral interference. Viral interference refers to the inhibition of virus growth caused by previous exposure of cells to an active or a heat - inactivated virus. Isaacs and Lindenmann were working with a system that involved the inhibition of the growth of live influenza virus in chicken embryo chorioallantoic membranes by heat - inactivated influenza virus. Their experiments revealed that this interference was mediated by a protein released by cells in the heat - inactivated influenza virus - treated membranes. They published their results in 1957 naming the antiviral factor they had discovered interferon. The findings of Isaacs and Lindenmann have been widely confirmed and corroborated in the literature. Furthermore, others may have made observations on interferons before the 1957 publication of Isaacs and Lindenmann. For example, during research to produce a more efficient vaccine for smallpox, Yasu - ichi Nagano and Yasuhiko Kojima -- two Japanese virologists working at the Institute for Infectious Diseases at the University of Tokyo -- noticed inhibition of viral growth in an area of rabbit - skin or testis previously inoculated with UV - inactivated virus. They hypothesised that some `` viral inhibitory factor '' was present in the tissues infected with virus and attempted to isolate and characterize this factor from tissue homogenates. Independently, Monto Ho, in John Enders 's lab, observed in 1957 that attenuated poliovirus conferred a species specific anti-viral effect in human amniotic cell cultures. They described these observations in a 1959 publication, naming the responsible factor viral inhibitory factor ( VIF ). It took another fifteen to twenty years, using somatic cell genetics, to show that the interferon action gene and interferon gene reside in different human chromosomes. The purification of human beta interferon did not occur until 1977. Chris Y.H. Tan and his co-workers purified and produced biologically active, radio - labeled human beta interferon by superinducing the interferon gene in fibroblast cells, and they showed its active site contains tyrosine residues. Tan 's laboratory isolated sufficient amounts of human beta interferon to perform the first amino acid, sugar composition and N - terminal analyses. They showed that human beta interferon was an unusually hydrophobic glycoprotein. This explained the large loss of interferon activity when preparations were transferred from test tube to test tube or from vessel to vessel during purification. The analyses showed the reality of interferon activity by chemical verification. The purification of human alpha interferon was not reported until 1978. A series of publications from the laboratories of Sidney Pestka and Alan Waldman between 1978 and 1981, describe the purification of the type I interferons IFN - α and IFN - β. By the early 1980s, genes for these interferons had been cloned, adding further definitive proof that interferons were responsible for interfering with viral replication. Gene cloning also confirmed that IFN - α was encoded by a family of many related genes. The type II IFN ( IFN - γ ) gene was also isolated around this time. Interferon was scarce and expensive until 1980, when the interferon gene was inserted into bacteria using recombinant DNA technology, allowing mass cultivation and purification from bacterial cultures or derived from yeasts. Interferon can also be produced by recombinant mammalian cells. Before the early 1970s, large scale production of human interferon had been pioneered by Kari Cantell. He produced large amounts of human alpha interferon from large quantities of human white blood cells collected by the Finnish Blood Bank. Large amounts of human beta interferon were made by superinducing the beta interferon gene in human fibroblast cells. Cantell 's and Tan 's methods of making large amounts of natural interferon were critical for chemical characterisation, clinical trials and the preparation of small amounts of interferon messenger RNA to clone the human alpha and beta interferon genes. The superinduced human beta interferon messenger RNA was prepared by Tan 's lab for Cetus corp. to clone the human beta interferon gene in bacteria and the recombinant interferon was developed as ' betaseron ' and approved for the treatment of MS. Superinduction of the human beta interferon gene was also used by Israeli scientists to manufacture human beta interferon. Human interferons IFNA1 IFNA2 IFNA4 IFNA5 IFNA6 IFNA7 IFNA8 IFNA10 IFNA13 IFNA14 IFNA16 IFNA17 IFNA21 IFNB1 IFNW IFNE1 IFNK See also ATC code L03 # L03AB Interferons Immunosuppression Immunosuppressive drug Immunotherapy Interferon Consensus Sequence - binding protein References Jump up ^ De Andrea, M ; Gariglio, M ; Gioia, D ; Landolfo, S ; Ravera, R ( 2002 ). `` The interferon system : an overview ''. Eur J Paediatr Neurol. 6 Suppl A ( 6 ) : A41 -- 58. PMID 12365360. ^ Jump up to : Cohen, B ; Parkin, J ( 2001 ). `` An overview of the immune system ''. Lancet. 357 ( 9270 ) : 1777 -- 89. 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Biochem. 87 ( 2 ) : 367 -- 70. PMID 678325. doi : 10.1111 / j. 1432 - 1033.1978. tb12385. x. Jump up ^ Berthold W, Tan C, Tan YH ( 1978 ). `` Purification and in vitro labeling of interferon from a human fibroblastoid cell line ''. J. Biol. Chem. 253 ( 14 ) : 5206 -- 12. PMID 670186. ^ Jump up to : Tan YH, Barakat F, Berthold W, Smith - Johannsen H, Tan C ( 1979 ). `` The isolation and amino acid / sugar composition of human fibroblastoid interferon ''. J. Biol. Chem. 254 ( 16 ) : 8067 -- 73. PMID 468807. Jump up ^ Zoon KC, Smith ME, Bridgen PJ, Anfinsen CB, Hunkapiller MW, Hood LE ( 1980 ). `` Amino terminal sequence of the major component of human lymphoblastoid interferon ''. Science. 207 ( 4430 ) : 527 -- 8. PMID 7352260. doi : 10.1126 / science. 7352260. Jump up ^ Okamura H, Berthold W, Hood L, Hunkapiller M, Inoue M, Smith - Johannsen H, Tan YH ( 1980 ). `` Human fibroblastoid interferon : immunosorbent column chromatography and N - terminal amino acid sequence ''. 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Singapore ; New York : World Scientific. ISBN 978 - 981 - 02 - 3148 - 4. Jump up ^ Tan YH, Armstrong JA, Ke YH, Ho M ( 1970 ). `` Regulation of cellular interferon production : enhancement by antimetabolites ''. Proc. Natl. Acad. Sci. U.S.A. 67 ( 1 ) : 464 -- 71. PMC 283227. PMID 5272327. doi : 10.1073 / pnas. 67.1. 464. Jump up ^ US patent 3773924, Ho M, Armstrong JA, Ke YH, Tan YH, `` Interferon Production '', issued 1973 Jump up ^ Bekisz, J ; Goldman, ND ; Hernandez, J ; Schmeisser, H ; Zoon, KC ( 2004 ). `` Mini Review Human Interferons Alpha, Beta and Omega ''. Growth Factors. 22 ( 4 ) : 243 -- 51. PMID 15621727. doi : 10.1080 / 08977190400000833. DNA virus antivirals ( primarily J05, also S01AD and D06BB ) Baltimore I Herpesvirus DNA - synthesis inhibitor TK activated Purine analogue guanine ( Aciclovir / Valaciclovir Ganciclovir / Valganciclovir Penciclovir / Famciclovir ) adenine ( Vidarabine ) Pyrimidine analogue uridine ( Idoxuridine Trifluridine ( + tipiracil ) Edoxudine ) thymine Brivudine Sorivudine cytosine ( Cytarabine ) Not TK activated Foscarnet Other Docosanol early protein ( Fomivirsen ) Tromantadine HPV / MC Imiquimod / Resiquimod Podophyllotoxin Vaccinia assembly : Rifampicin Poxviridae Methisazone Hepatitis B ( VII ) Nucleoside analogues / NARTIs : Entecavir Lamivudine Telbivudine Clevudine Nucleotide analogues / NtRTIs : Adefovir Tenofovir disoproxil Tenofovir alafenamide Multiple / general Nucleic acid inhibitors Cidofovir Interferon Interferon alfa 2b Peginterferon alfa - 2a Multiple / unknown Ribavirin / Taribavirin Moroxydine WHO - EM Withdrawn from market Clinical trials : Phase III Never to phase III Cell signaling : cytokines By family Chemokine CCL CCL1 CCL2 / MCP1 CCL3 / MIP1α CCL4 / MIP1β CCL5 / RANTES CCL6 CCL7 CCL8 CCL9 CCL11 CCL12 CCL13 CCL14 CCL15 CCL16 CCL17 CCL18 / PARC / DCCK1 / AMAC1 / MIP4 CCL19 CCL20 CCL21 CCL22 CCL23 CCL24 CCL25 CCL26 CCL27 CCL28 CXCL CXCL1 / KC CXCL2 CXCL3 CXCL4 CXCL5 CXCL6 CXCL7 CXCL8 / IL8 CXCL9 CXCL10 CXCL11 CXCL12 CXCL13 CXCL14 CXCL15 CXCL16 CXCL17 CX3CL CX3CL1 XCL XCL1 XCL2 TNF TNFA Lymphotoxin TNFB / LTA TNFC / LTB TNFSF4 TNFSF5 / CD40LG TNFSF6 TNFSF7 TNFSF8 TNFSF9 TNFSF10 TNFSF11 TNFSF13 TNFSF13B EDA Interleukin Type I ( grouped by receptor subunit ) γ chain IL2 / IL15 IL4 / IL13 IL7 IL9 IL21 β chain IL3 IL5 GMCSF IL6 like / gp130 IL6 IL11 IL27 IL30 IL31 + non IL OSM LIF CNTF CTF1 IL12 family / IL12RB1 IL12 IL23 IL27 IL35 Other IL14 IL16 IL32 IL34 Type II IL10 family IL10 / IL22 IL19 IL20 IL24 IL26 Interferon type III IL28 / IFNL2 + 3 IL29 / IFNL1 Interferon IFNA1 IFNA2 IFNA4 IFNA5 IFNA6 IFNA7 IFNA8 IFNA10 IFNA13 IFNA14 IFNA16 IFNA17 IFNA21 IFNB1 IFNK IFNW1 II IFNG Ig superfamily IL1 family : IL1A / IL1F1 IL1B / IL1F2 1Ra / IL1F3 IL1F5 IL1F6 IL1F7 IL1F8 IL1F9 IL1F10 33 / IL1F11 18 / IL1G IL17 family IL17 / IL25 ( IL17A ) Other Hematopoietic KITLG Colony - stimulating factor SPP1 MIF By function / cell proinflammatory cytokine IL1 TNFA Monokine Lymphokine IFNγ TNFβ IL4 IL5 IL6 IL10 IL13 Cytokine receptor modulators Chemokine See here instead. CSF Erythropoietin Agonists : ARA - 290 Asialo erythropoietin Carbamylated erythropoietin CNTO - 530 Darbepoetin alfa Epoetin alfa Epoetin beta Epoetin delta Epoetin epsilon Epoetin gamma Epoetin kappa Epoetin omega Epoetin theta Epoetin zeta Erythropoietin ( EPO ) Erythropoietin - Fc Methoxy polyethylene glycol - epoetin beta ( CERA / Mircera ) Peginesatide Pegol sihematide ( EPO - 018B ) G - CSF ( CSF3 ) Agonists : Filgrastim Granulocyte colony - stimulating factor Lenograstim Leridistim Lipegfilgrastim Nartograstim Pegfilgrastim Pegnartograstim GM - CSF ( CSF2 ) Agonists : Ecogramostim Granulocyte macrophage colony - stimulating factor Milodistim Molgramostim Regramostim Sargramostim Antibodies : Mavrilimumab MOR103 Namilumab M - CSF ( CSF1 ) Agonists : Cilmostim Interleukin - 34 Lanimostim Macrophage colony - stimulating factor Mirimostim Kinase inhibitors : Agerafenib SCF ( c - Kit ) See here instead. Thrombopoietin Agonists : Eltrombopag Pegacaristim Promegapoietin Romiplostim Thrombopoietin ( THPO, MGDF ) Interferon IFNAR ( α / β, I ) Agonists : Albinterferon Interferon alpha ( interferon alfa, IFN - α ) Interferon alfa ( IFNA1, IFNA2, IFNA4, IFNA5, IFNA6, IFNA7, IFNA8, IFNA10, IFNA13, IFNA14, IFNA16, IFNA17, IFNA21 ) Interferon alfa 2a Interferon alfa 2b Interferon alfa n1 Interferon alfacon - 1 Interferon alpha - n3 Interferon beta ( IFN - β ) ( IFNB1, IFNB3 ) Interferon beta 1a Interferon beta 1b Interferon kappa ( IFN - ε / κ / τ / ζ, IFNK ) Interferon omega ( IFN - ω, IFNW1 ) Peginterferon alfa - 2a Peginterferon alfa - 2b Antibodies : Anifrolumab Faralimomab MEDI - 545 Rontalizumab Sifalimumab Decoy receptors : Bifarcept IFNGR ( γ, II ) Agonists : Interferon gamma ( IFN - γ ) Interferon gamma 1b Antibodies : Emapalumab Fontolizumab IFNLR ( λ, III ) See IL - 28R ( IFNLR ) here instead. Interleukin See here instead. TGFβ See here instead. TNF See here instead. Others JAK ( inhibitors ) JAK1 Baricitinib Filgotinib Momelotinib Oclacitinib Ruxolitinib Tofacitinib ( tasocitinib, CP - 690550 ) Upadacitinib JAK2 AG - 490 Atiprimod AZD - 1480 Baricitinib CHZ868 Cucurbitacin I ( elatericin B, JSI - 124 ) CYT387 Lestaurtinib NSC - 7908 NSC - 33994 Pacritinib Ruxolitinib SD - 1008 Tofacitinib ( tasocitinib, CP - 690550 ) JAK3 AG - 490 Cercosporamide TCS - 21311 Tofacitinib ( tasocitinib, CP - 690550 ) WHI - P 154 ZM - 39923 ZM - 449829 Others Additional cytokines : Cardiotrophin 1 ( CT - 1 ) FMS - like tyrosine kinase 3 ligand ( FLT3L ) Leukemia / leukocyte inhibitory factor ( LIF ) Oncostatin M ( OSM ) Thymic stromal lymphopoietin ( TSLP ) Additional cytokine receptor modulators : Emfilermin Lestaurtinib Midostaurin Quizartinib Sorafenib Sunitinib See also Receptor / signaling modulators Signaling peptide / protein receptor modulators Growth factor receptor modulators NDL : 00564172 Retrieved from `` https://en.wikipedia.org/w/index.php?title=Interferon&oldid=800575871 '' Categories : Cytokines Antivirals Hidden categories : CS1 French - language sources ( fr ) Articles lacking reliable references from July 2014 All articles lacking reliable references Talk Contents About Wikipedia Azərbaycanca বাংলা Беларуская Bosanski Català Čeština Deutsch Eesti Ελληνικά Español Euskara فارسی Français Gaeilge Galego 한국어 Հայերեն Hrvatski Bahasa Indonesia Italiano עברית Basa Jawa ಕನ್ನಡ ქართული Қазақша Kreyòl ayisyen Кыргызча Magyar Nederlands 日本 語 Oʻzbekcha / ўзбекча Polski Português Română Русский Scots Simple English Slovenščina کوردی Српски / srpski Srpskohrvatski / српскохрватски Suomi Svenska தமிழ் ไทย Türkçe Українська Tiếng Việt 中文 Edit links This page was last edited on 14 September 2017, at 11 : 38. 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Question: interferons alpha and beta are effective against viruses
Answer: IFN-α can be used to treat hepatitis B and C infections, while IFN-β can be used to treat multiple sclerosis