Interferon
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"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
[show]Available protein structures:
Pfam
structures
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Interferons (IFNs) are a group of signaling proteins[1] 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.[2] Interferons are named for their ability to "interfere" with viral replication[2] 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
[hide]
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[edit]
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.[3] The type I interferons present in humans are IFN-α, IFN-β, IFN-ε, IFN-κ and IFN-ω.[4] 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.[2]
Interferon type II (IFN-γ in humans): This is also known as immune interferon and is activated by Interleukin-12.[2] 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 Th2 immune response and a further induction of Th1 immune response, which leads to the development of debilitating diseases such as multiple sclerosis.[5] IFN type II binds to IFNGR, which consists of IFNGR1 and IFNGR2 chains and has a different receptor than type I IFN.[2]
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,[6] recent information demonstrates the importance of Type III IFNs in some types of virus infections.[7][8]
In general, type I and II interferons are responsible for regulating and activating the immune response.[2] 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[edit]
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.[9][10] They also limit viral spread by increasing p53 activity, which kills virus-infected cells by promoting apoptosis.[11][12] The effect of IFN on p53 is also linked to its protective role against certain cancers.[11]
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[edit]
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.[13] 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.[14]
Downstream signaling[edit]
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.[15]
STAT activation initiates the most well-defined cell signaling pathway for all IFNs, the classical Janus kinase-STAT (JAK-STAT) signaling pathway.[15] 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.[15] A collection of known ISGs is available on Interferome, a curated online database of ISGs (www.interferome.org);[16] 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.[15] 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.[15]
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.[15] Type I IFNs further activate p38 mitogen-activated protein kinase (MAP kinase) to induce gene transcription.[15] 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.[15]
Virus resistance to interferons[edit]
Many viruses have evolved mechanisms to resist interferon activity.[17] 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.[18] 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).[18][19] 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.[19][20] 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).[18] 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.[20] 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.[21][22][23] 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 [18] 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.[24]
Interferon therapy[edit]
Three vials filled with human leukocyte interferon
Diseases[edit]
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.[25]
Interferon therapy is used (in combination with chemotherapy and radiation) as a treatment for some cancers.[26] 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.[26] Patients with recurrent melanomas receive recombinant IFN-α2b.[27] Both hepatitis B and hepatitis C are treated with IFN-α, often in combination with other antiviral drugs.[28][29] 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.[30] 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.[31]
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.[32] 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.[32] Low-quality evidence suggests that the combination of interferon and an antiviral agent may speed the healing process compared to antiviral therapy alone.[32]
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.[33]
Drug formulations[edit]
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.[34] 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).[35][36][37] Interferon-containing regimens may also include protease inhibitors such as boceprevir and telaprevir.
History[edit]
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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;[38][39][40] 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.[39] The findings of Isaacs and Lindenmann have been widely confirmed and corroborated in the literature.[41]
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.[42] 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).[43] 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.[44][45][46] 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.[47][48] Tan's laboratory isolated sufficient amounts of human beta interferon to perform the first amino acid, sugar composition and N-terminal analyses.[49] 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.[49][50][51][52] 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.[40] By the early 1980s, genes for these interferons had been cloned, adding further definitive proof that interferons were responsible for interfering with viral replication.[53][54] Gene cloning also confirmed that IFN-α was encoded by a family of many related genes.[55] The type II IFN (IFN-γ) gene was also isolated around this time.[56]
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[57] or derived from yeasts. Interferon can also be produced by recombinant mammalian cells.[58] 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.[59] Large amounts of human beta interferon were made by superinducing the beta interferon gene in human fibroblast cells.[60][61]
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[edit]
IFNA1
IFNA2
IFNA4
IFNA5
IFNA6
IFNA7
IFNA8
IFNA10
IFNA13
IFNA14
IFNA16
IFNA17
IFNA21
IFNB1
IFNW
IFNE1
IFNK
[4][62]
See also[edit]
ATC code L03#L03AB Interferons
Immunosuppression
Immunosuppressive drug
Immunotherapy
Interferon Consensus Sequence-binding protein
References[edit]
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Jump up ^ Ho, M, and Enders, JF, An inhibitor of viral activity appearing in infected cell cultures. PNAS 45, 385-389, 1959
Jump up ^ Tan YH, Tischfield J, Ruddle FH (1973). "The linkage of genes for the human interferon-induced antiviral protein and indophenol oxidase-B traits to chromosome G-21". J. Exp. Med. 137 (2): 317–30. PMC 2139494  . PMID 4346649. doi:10.1084/jem.137.2.317.
Jump up ^ Tan YH (1976). "Chromosome 21 and the cell growth inhibitory effect of human interferon preparations". Nature. 260 (5547): 141–3. PMID 176593. doi:10.1038/260141a0.
Jump up ^ Meager A, Graves H, Burke DC, Swallow DM (1979). "Involvement of a gene on chromosome 9 in human fibroblast interferon production". Nature. 280 (5722): 493–5. PMID 460428. doi:10.1038/280493a0.
Jump up ^ Berthold W, Tan C, Tan YH (1978). "Chemical modifications of tyrosyl residue(s) and action of human-fibroblast interferon". Eur. J. 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: a b 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". Biochemistry. 19 (16): 3831–5. PMID 6157401. doi:10.1021/bi00557a028.
Jump up ^ Knight E, Hunkapiller MW, Korant BD, Hardy RW, Hood LE (1980). "Human fibroblast interferon: amino acid analysis and amino terminal amino acid sequence". Science. 207 (4430): 525–6. PMID 7352259. doi:10.1126/science.7352259.
Jump up ^ Weissenbach J, Chernajovsky Y, Zeevi M, Shulman L, Soreq H, Nir U, Wallach D, Perricaudet M, Tiollais P, Revel M (December 1980). "Two interferon mRNAs in human fibroblasts: in vitro translation and Escherichia coli cloning studies". Proc. Natl. Acad. Sci. U.S.A. 77 (12): 7152–6. Bibcode:1980PNAS...77.7152W. PMC 350459  . PMID 6164058. doi:10.1073/pnas.77.12.7152.
Jump up ^ Taniguchi T, Fujii-Kuriyama Y, Muramatsu M (July 1980). "Molecular cloning of human interferon cDNA". Proc. Natl. Acad. Sci. U.S.A. 77 (7): 4003–6. Bibcode:1980PNAS...77.4003T. PMC 349756  . PMID 6159625. doi:10.1073/pnas.77.7.4003.
Jump up ^ Nagata S, Mantei N, Weissmann C (October 1980). "The structure of one of the eight or more distinct chromosomal genes for human interferon-alpha". Nature. 287 (5781): 401–8. Bibcode:1980Natur.287..401N. PMID 6159536. doi:10.1038/287401a0.
Jump up ^ Gray PW, Goeddel DV (August 1982). "Structure of the human immune interferon gene". Nature. 298 (5877): 859–63. Bibcode:1982Natur.298..859G. PMID 6180322. doi:10.1038/298859a0.
Jump up ^ Nagata S, Taira H, Hall A, Johnsrud L, Streuli M, Ecsödi J, Boll W, Cantell K, Weissmann C (March 1980). "Synthesis in E. coli of a polypeptide with human leukocyte interferon activity". Nature. 284 (5754): 316–20. Bibcode:1980Natur.284..316N. PMID 6987533. doi:10.1038/284316a0.
Jump up ^ US patent 6207146, Tan YH, Hong WJ, "Gene expression in mammalian cells.", issued 2001
Jump up ^ Cantell K (1998). The story of interferon: the ups and downs in the life of a scientis. 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.
[show]
v
t
e
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
[show]
v
t
e
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
I
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
Th1
IFNγ
TNFβ
Th2
IL4
IL5
IL6
IL10
IL13
[show]
v
t
e
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
Authority control
NDL: 00564172
Retrieved from "https://en.wikipedia.org/w/index.php?title=Interferon&oldid=800575871"
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ul
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html
local
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b
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li
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href title
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html
local
li
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/wiki/Alpha-taxilin Alpha-taxilin
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/wiki/Interleukin_32 Interleukin 32
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/wiki/Interleukin_34 Interleukin 34
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/wiki/Type_II_cytokine_receptor Type II cytokine receptor
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/wiki/Interleukin_26 Interleukin 26
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/wiki/Interferon_type_III Interferon type III
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/wiki/Interleukin_28 Interleukin 28
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/wiki/Interleukin_29 Interleukin 29
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/wiki/Interferon_type_I Interferon type I
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/wiki/IFNA2 IFNA2
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/wiki/IFNA8 IFNA8
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/wiki/IFNA10 IFNA10
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/wiki/IFNA13 IFNA13
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/wiki/IFNA14 IFNA14
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/wiki/IFNA16 IFNA16
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/wiki/IFNA17 IFNA17
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/wiki/IFNA21 IFNA21
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/wiki/IFNB1 IFNB1
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/wiki/IFNK IFNK
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/wiki/IFNW1 IFNW1
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/wiki/Interferon_type_II Interferon type II
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scope class style
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/wiki/Interferon_gamma Interferon gamma
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padding:0em 0.25em
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/wiki/Immunoglobulin_superfamily Immunoglobulin superfamily
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/wiki/IL1A IL1A
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li
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href title
/wiki/Interleukin_1_beta Interleukin 1 beta
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/wiki/Interleukin_1_receptor_antagonist Interleukin 1 receptor antagonist
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/wiki/IL1F5 mw-redirect IL1F5
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/wiki/IL36A IL36A
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/wiki/IL1F7 mw-redirect IL1F7
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/wiki/IL36B IL36B
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/wiki/IL1F9 mw-redirect IL1F9
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/wiki/IL1F10 IL1F10
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/wiki/Interleukin_33 Interleukin 33
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/wiki/Interleukin_18 Interleukin 18
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/wiki/IL17_family mw-redirect IL17 family
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/wiki/Interleukin_17 Interleukin 17
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/wiki/Interleukin_25 Interleukin 25
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/wiki/IL17A IL17A
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/wiki/Hematopoietic mw-redirect Hematopoietic
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/wiki/Stem_cell_factor Stem cell factor
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/wiki/Colony-stimulating_factor Colony-stimulating factor
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ul
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href title
/wiki/Osteopontin Osteopontin
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/wiki/Macrophage_migration_inhibitory_factor Macrophage migration inhibitory factor
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padding:0em 0.25em
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display: none;
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br
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scope class style
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href title
/wiki/Proinflammatory_cytokine Proinflammatory cytokine
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i
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/wiki/Interleukin_1 mw-redirect Interleukin 1
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li
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/wiki/Tumor_necrosis_factor_alpha Tumor necrosis factor alpha
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/wiki/Monokine Monokine
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/wiki/Lymphokine Lymphokine
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sub
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/wiki/Interferon_gamma Interferon gamma
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sub
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/wiki/Interleukin_4 Interleukin 4
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/wiki/Interleukin_5 Interleukin 5
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/wiki/Interleukin_6 Interleukin 6
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/wiki/Interleukin_10 Interleukin 10
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/wiki/Interleukin_13 Interleukin 13
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role class aria-labelledby style
navigation navbox Cell_signaling:_cytokines padding:3px
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id href
collapseButton3 #
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collapseButton
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abbr
title style
View this template ;;background:none transparent;border:none;-moz-box-shadow:none;-webkit-box-shadow:none;box-shadow:none;
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href title
/wiki/Template:Cytokine_receptor_modulators Template:Cytokine receptor modulators
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class
nv-view
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title style
Discuss this template ;;background:none transparent;border:none;-moz-box-shadow:none;-webkit-box-shadow:none;box-shadow:none;
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/wiki/Template_talk:Cytokine_receptor_modulators Template talk:Cytokine receptor modulators
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nv-talk
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Edit this template ;;background:none transparent;border:none;-moz-box-shadow:none;-webkit-box-shadow:none;box-shadow:none;
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external text //en.wikipedia.org/w/index.php?title=Template:Cytokine_receptor_modulators&action=edit
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plainlinks hlist navbar mini
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Cytokine_receptor_modulators font-size:114%;margin:0 4em
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/wiki/Template:Chemokine_receptor_modulators Template:Chemokine receptor modulators
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href title
/wiki/Erythropoietin_receptor Erythropoietin receptor
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row navbox-group width:1%;text-align:center;
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/w/index.php?title=ARA-290&action=edit&redlink=1 new ARA-290 (page does not exist)
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/w/index.php?title=Asialo_erythropoietin&action=edit&redlink=1 new Asialo erythropoietin (page does not exist)
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/w/index.php?title=Carbamylated_erythropoietin&action=edit&redlink=1 new Carbamylated erythropoietin (page does not exist)
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href class title
/w/index.php?title=CNTO-530&action=edit&redlink=1 new CNTO-530 (page does not exist)
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/wiki/Darbepoetin_alfa Darbepoetin alfa
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/wiki/Epoetin_alfa Epoetin alfa
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/wiki/Epoetin_beta Epoetin beta
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/w/index.php?title=Epoetin_kappa&action=edit&redlink=1 new Epoetin kappa (page does not exist)
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/w/index.php?title=Epoetin_theta&action=edit&redlink=1 new Epoetin theta (page does not exist)
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/wiki/Epoetin_zeta mw-redirect Epoetin zeta
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/wiki/Erythropoietin Erythropoietin
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/w/index.php?title=Erythropoietin-Fc&action=edit&redlink=1 new Erythropoietin-Fc (page does not exist)
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/wiki/Methoxy_polyethylene_glycol-epoetin_beta Methoxy polyethylene glycol-epoetin beta
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/wiki/Peginesatide Peginesatide
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href title
/wiki/Granulocyte_colony-stimulating_factor_receptor Granulocyte colony-stimulating factor receptor
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/wiki/Filgrastim Filgrastim
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/wiki/Granulocyte_colony-stimulating_factor Granulocyte colony-stimulating factor
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/wiki/Lenograstim Lenograstim
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href class title
/w/index.php?title=Leridistim&action=edit&redlink=1 new Leridistim (page does not exist)
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href class title
/w/index.php?title=Lipegfilgrastim&action=edit&redlink=1 new Lipegfilgrastim (page does not exist)
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href class title
/w/index.php?title=Nartograstim&action=edit&redlink=1 new Nartograstim (page does not exist)
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/wiki/Pegfilgrastim Pegfilgrastim
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/w/index.php?title=Pegnartograstim&action=edit&redlink=1 new Pegnartograstim (page does not exist)
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row navbox-group width:1%;text-align:center;
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/w/index.php?title=Ecogramostim&action=edit&redlink=1 new Ecogramostim (page does not exist)
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/wiki/Granulocyte_macrophage_colony-stimulating_factor mw-redirect Granulocyte macrophage colony-stimulating factor
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/w/index.php?title=Milodistim&action=edit&redlink=1 new Milodistim (page does not exist)
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/wiki/Molgramostim Molgramostim
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/w/index.php?title=Regramostim&action=edit&redlink=1 new Regramostim (page does not exist)
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/wiki/Sargramostim Sargramostim
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/wiki/Mavrilimumab Mavrilimumab
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/w/index.php?title=MOR103&action=edit&redlink=1 new MOR103 (page does not exist)
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/wiki/Namilumab Namilumab
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href class title
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row navbox-group width:1%;text-align:center;
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/w/index.php?title=Cilmostim&action=edit&redlink=1 new Cilmostim (page does not exist)
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/wiki/Interleukin-34 mw-redirect Interleukin-34
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/w/index.php?title=Lanimostim&action=edit&redlink=1 new Lanimostim (page does not exist)
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/w/index.php?title=Interferon&oldid=800575871 Permanent link to this revision of the page
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/w/index.php?title=Interferon&action=info More information about this page
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https://ja.wikipedia.org/wiki/%E3%82%A4%E3%83%B3%E3%82%BF%E3%83%BC%E3%83%95%E3%82%A7%E3%83%AD%E3%83%B3 インターフェロン – Japanese ja ja interlanguage-link-target
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https://uk.wikipedia.org/wiki/%D0%86%D0%BD%D1%82%D0%B5%D1%80%D1%84%D0%B5%D1%80%D0%BE%D0%BD%D0%B8 Інтерферони – Ukrainian uk uk interlanguage-link-target
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img
src srcset width height alt
/static/images/wikimedia-button.png /static/images/wikimedia-button-1.5x.png 1.5x, /static/images/wikimedia-button-2x.png 2x 88 31 Wikimedia Foundation
html
local
a
href
https://wikimediafoundation.org/
html
local
li
id
footer-copyrightico
html
local
img
src alt srcset width height
/static/images/poweredby_mediawiki_88x31.png Powered by MediaWiki /static/images/poweredby_mediawiki_132x47.png 1.5x, /static/images/poweredby_mediawiki_176x62.png 2x 88 31
html
local
a
href
//www.mediawiki.org/
html
local
li
id
footer-poweredbyico
html
local
ul
id class
footer-icons noprint
html
local
div
style
clear:both
html
local
div
id role
footer contentinfo
html
local
div
class
suggestions-results
html
local
div
class
suggestions-special
html
local
div
class style
suggestions display: none; font-size: 13px;
html
local
polygon
points
0 8, 10 8, 18 0, 26 8, 1000 8, 1000 1000, 0 1000
html
local
clippath
id
mwe-popups-mask
html
local
polygon
points
0 8, 274 8, 282 0, 290 8, 1000 8, 1000 1000, 0 1000
html
local
clippath
id
mwe-popups-mask-flip
html
local
polygon
points
0 8, 174 8, 182 0, 190 8, 1000 8, 1000 1000, 0 1000
html
local
clippath
id
mwe-popups-landscape-mask
html
local
polygon
points
0 0, 1000 0, 1000 242, 190 242, 182 250, 174 242, 0 242
html
local
clippath
id
mwe-popups-landscape-mask-flip
html
local
defs
html
local
svg
width height
0 0
html
local
div
id
mwe-popups-svg
html
local
body
class
mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject page-Interferon rootpage-Interferon vector-experimental-print-styles vector-nav-directionality skin-vector action-view
html
local