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interferons can be used to treat all of the following except what

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Signaling proteins released by host cells in response to the presence of pathogens

Interferon blazon I (α/β/δ...)
1RH2 Recombinant Human Interferon-Alpha 2b-01.png

The molecular structure of human interferon-blastoff (PDB: 1RH2​)
Identifiers
Symbol Interferons
Pfam PF00143
InterPro IPR000471
SMART SM00076
PROSITE PDOC00225
CATH 1au0
SCOP2 1au1 / Telescopic / SUPFAM
CDD cd00095
Interferon type II (γ)
1HIG Interferon-Gamma01.png

The three-dimensional structure of human being interferon gamma (PDB: 1HIG​)
Identifiers
Symbol IFN-gamma
Pfam PF00714
InterPro IPR002069
CATH 1d9cA00
SCOP2 d1d9ca_ / Scope / SUPFAM
Interferon type Three (λ)
Identifiers
Symbol IL28A
Pfam PF15177
InterPro IPR029177
CATH 3og6A00

Interferons (IFNs, [1]) are a group of signaling proteins[2] made and released by host cells in response to the presence of several viruses. In a typical scenario, a virus-infected jail cell volition release interferons causing nearby cells to enhance their anti-viral defenses.

IFNs belong to the large class of proteins known as cytokines, molecules used for advice between cells to trigger the protective defenses of the allowed system that help eradicate pathogens.[3] Interferons are named for their ability to "interfere" with viral replication[three] past protecting cells from virus infections. However, virus-encoded genetic elements have the ability to antagonize the IFN response contributing to viral pathogenesis and viral diseases.[4] IFNs too have various other functions: they actuate immune cells, such as natural killer cells and macrophages, and they increment host defenses by up-regulating antigen presentation by virtue of increasing the expression of major histocompatibility circuitous (MHC) antigens. Certain symptoms of infections, such as fever, muscle pain and "flu-similar symptoms", are as well caused past the production of IFNs and other cytokines.

More twenty singled-out IFN genes and proteins accept been identified in animals, including humans. They are typically divided among three classes: Type I IFN, Type Ii IFN, and Type Three IFN. IFNs belonging to all three classes are important for fighting viral infections and for the regulation of the immune system.

Types of interferon [edit]

Based on the blazon of receptor through which they point, man interferons accept been classified into three major types.

  • Interferon type I: All type I IFNs bind to a specific cell surface receptor complex known every bit the IFN-α/β receptor (IFNAR) that consists of IFNAR1 and IFNAR2 chains.[5] The type I interferons present in humans are IFN-α, IFN-β, IFN-ε, IFN-κ and IFN-ω.[six] In general, blazon I interferons are produced when the body recognizes a virus that has invaded it. They are produced by fibroblasts and monocytes. Yet, the production of type I IFN-α is inhibited by some other cytokine known as Interleukin-ten. Once released, type I interferons demark to specific receptors on target cells, which leads to expression of proteins that volition prevent the virus from producing and replicating its RNA and DNA.[7] Overall, IFN-α can exist used to care for hepatitis B and C infections, while IFN-β can be used to treat multiple sclerosis.[3]
  • Interferon type 2 (IFN-γ in humans): This is also known as immune interferon and is activated by Interleukin-12.[3] Type II interferons are as well released past cytotoxic T cells and type-one T helper cells. Withal, they block the proliferation of type-2 T helper cells. The previous results in an inhibition of Thtwo immune response and a farther induction of Thane immune response.[8] IFN type II binds to IFNGR, which consists of IFNGR1 and IFNGR2 chains.[3]
  • Interferon type Three: Point through a receptor complex consisting of IL10R2 (also called CRF2-4) and IFNLR1 (also chosen CRF2-12). Although discovered more than recently than type I and type II IFNs,[9] recent data demonstrates the importance of Type III IFNs in some types of virus or fungal infections.[10] [11] [12]

In full general, blazon I and 2 interferons are responsible for regulating and activating the immune response.[three] Expression of blazon I and III IFNs can be induced in about all cell types upon recognition of viral components, specially nucleic acids, past cytoplasmic and endosomal receptors, whereas blazon 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.

Office [edit]

All interferons share several common effects: they are antiviral agents and they attune functions of the immune system. Assistants of Type I IFN has been shown experimentally to inhibit tumor growth in animals, but the benign action in human being tumors has not been widely documented. A virus-infected jail cell releases viral particles that can infect nearby cells. However, the infected cell tin can protect neighboring cells against a potential infection of 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 Fifty—besides induced by interferon action—destroys RNA within the cells to further reduce poly peptide synthesis of both viral and host genes. Inhibited poly peptide synthesis impairs both virus replication and infected host cells. In add-on, interferons induce product of hundreds of other proteins—known collectively every bit interferon-stimulated genes (ISGs)—that have roles in combating viruses and other actions produced by interferon.[13] [14] They also limit viral spread by increasing p53 activity, which kills virus-infected cells by promoting apoptosis.[15] [sixteen] The effect of IFN on p53 is as well linked to its protective part against certain cancers.[fifteen]

Some other role of interferons is to upwards-regulate major histocompatibility circuitous molecules, MHC I and MHC II, and increment immunoproteasome activity. All interferons significantly enhance the presentation of MHC I dependent antigens. Interferon gamma (IFN-gamma) likewise significantly stimulates the MHC 2-dependent presentation of antigens. Higher MHC I expression increases presentation of viral and abnormal peptides from cancer cells to cytotoxic T cells, while the immunoproteasome processes these peptides for loading onto the MHC I molecule, thereby increasing the recognition and killing of infected or malignant cells. Higher MHC II expression increases presentation of these peptides to helper T cells; these cells release cytokines (such as more interferons and interleukins, among others) that betoken to and co-ordinate the activity of other immune cells.[17] [18] [19]

Interferons can likewise suppress angiogenesis past down regulation of angiogenic stimuli deriving from tumor cells. They also suppress the proliferation of endothelial cells. Such suppression causes a decrease in tumor angiogenesis, a decrease in its vascularization and subsequent growth inhibition. Interferons, such as interferon gamma, directly activate other immune cells, such as macrophages and natural killer cells.[17] [18] [19]

Induction of interferons [edit]

Production of interferons occurs mainly in response to microbes, such every bit 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 design recognition receptors, such as membrane bound toll like receptors or the cytoplasmic receptors RIG-I or MDA5, can trigger release of IFNs. Toll Similar 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). Later on 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 every bit siRNA or vector-based reagents can either silence or stimulate interferon pathways.[20] Release of IFN from cells (specifically IFN-γ in lymphoid cells) is also induced by mitogens. Other cytokines, such as interleukin 1, interleukin two, interleukin-12, tumor necrosis factor and colony-stimulating cistron, can too enhance interferon production.[21]

Downstream signaling [edit]

By interacting with their specific receptors, IFNs actuate point transducer and activator of transcription (STAT) complexes; STATs are a family of transcription factors that regulate the expression of certain allowed system genes. Some STATs are activated by both blazon I and type 2 IFNs. However each IFN type can likewise activate unique STATs.[22]

STAT activation initiates the most well-defined cell signaling pathway for all IFNs, the classical Janus kinase-STAT (JAK-STAT) signaling pathway.[22] In this pathway, JAKs acquaintance with IFN receptors and, post-obit receptor engagement with IFN, phosphorylate both STAT1 and STAT2. As a event, an IFN-stimulated cistron 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.[22] A drove of known ISGs is available on Interferome, a curated online database of ISGs (www.interferome.org);[23] Additionally, STAT homodimers or heterodimers form from different combinations of STAT-i, -three, -4, -5, or -half-dozen during IFN signaling; these dimers initiate gene transcription by binding to IFN-activated site (GAS) elements in gene promoters.[22] Blazon I IFNs tin can induce expression of genes with either ISRE or GAS elements, only factor induction by type Ii IFN can occur only in the presence of a GAS chemical element.[22]

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 chosen CRKL, a nuclear adaptor for STAT5 that also regulates signaling through the C3G/Rap1 pathway.[22] Blazon I IFNs further actuate p38 mitogen-activated protein kinase (MAP kinase) to induce cistron transcription.[22] Antiviral and antiproliferative furnishings specific to type I IFNs result from p38 MAP kinase signaling. The phosphatidylinositol 3-kinase (PI3K) signaling pathway is also regulated past both type I and blazon II IFNs. PI3K activates P70-S6 Kinase one, an enzyme that increases protein synthesis and jail cell proliferation; phosphorylates ribosomal protein s6, which is involved in protein synthesis; and phosphorylates a translational repressor protein called eukaryotic translation-initiation gene 4E-binding poly peptide 1 (EIF4EBP1) in guild to deactivate it.[22]

Interferons tin disrupt signaling by other stimuli. For example, Interferon alpha induces RIG-Thousand, which disrupts the CSN5-containing COP9 signalosome (CSN), a highly conserved multiprotein complex implicated in protein deneddylation, deubiquitination, and phosphorylation.[24] RIG-Chiliad has shown the capacity to inhibit NF-κB and STAT3 signaling in lung cancer cells, which demonstrates the potential of type I IFNs.[ commendation needed ]

Virus resistance to interferons [edit]

Many viruses have evolved mechanisms to resist interferon activity.[25] 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.[26] Viruses that inhibit IFN signaling include Japanese Encephalitis Virus (JEV), dengue type 2 virus (DEN-2), and viruses of the herpesvirus family, such equally human cytomegalovirus (HCMV) and Kaposi'due south sarcoma-associated herpesvirus (KSHV or HHV8).[26] [27] 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 Man papillomavirus (HPV), and the B18R protein of vaccinia virus.[27] [28] Reducing IFN-α action may prevent signaling via STAT1, STAT2, or IRF9 (as with JEV infection) or through the JAK-STAT pathway (as with DEN-2 infection).[26] Several poxviruses encode soluble IFN receptor homologs—like the B18R protein of the vaccinia virus—that demark to and prevent IFN interacting with its cellular receptor, impeding advice between this cytokine and its target cells.[28] 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 iii (σ3) protein, and vaccinia virus employs using the gene product of its E3L gene, p25.[29] [xxx] [31] The ability of interferon to induce protein production from interferon stimulated genes (ISGs) can also be affected. Production of poly peptide kinase R, for example, can exist disrupted in cells infected with JEV.[26] Some viruses escape the anti-viral activities of interferons by cistron (and thus protein) mutation. The H5N1 flu virus, likewise known every bit bird flu, has resistance to interferon and other anti-viral cytokines that is attributed to a unmarried amino acid change in its Non-Structural Protein one (NS1), although the precise mechanism of how this confers amnesty is unclear.[32]

Coronavirus response [edit]

Coronaviruses evade innate immunity during the kickoff ten days of viral infection.[33] In the early on stages of infection, SARS-CoV-2 induces an even lower interferon type I (IFN-I) response than SARS-CoV, which itself is a weak IFN-I inducer in human cells.[33] SARS-CoV-2 limits the IFN-3 response besides.[34] Reduced numbers of plasmacytoid dendritic cells with age is associated with increased COVID-nineteen severity, perchance because these cells are substantial interferon producers.[35]

10 percentage of patients with life-threatening COVID-xix have autoantibodies against blazon I interferon.[35]

Delayed IFN-I response contributes to the pathogenic inflammation (cytokine storm) seen in subsequently stages of COVID-19 disease.[36] Application of IFN-I prior to (or in the very early stages of) viral infection can be protective,[33] which should be validated in randomized clinical trials.[36]

Interferon therapy [edit]

Three vials filled with human leukocyte interferon

Diseases [edit]

Interferon beta-1a and interferon beta-1b are used to care for and command multiple sclerosis, an autoimmune disorder. This treatment may help in reducing attacks in relapsing-remitting multiple sclerosis[37] and slowing disease progression and activeness in secondary progressive multiple sclerosis.[38]

Interferon therapy is used (in combination with chemotherapy and radiations) as a treatment for some cancers.[39] This treatment can be used in hematological malignancy, such as in leukemia and lymphomas including hairy cell leukemia, chronic myeloid leukemia, nodular lymphoma, and cutaneous T-cell lymphoma.[39] Patients with recurrent melanomas receive recombinant IFN-α2b.[forty] Both hepatitis B and hepatitis C are treated with IFN-α, often in combination with other antiviral drugs.[41] [42] 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—tin can be treated with a threescore-fourscore% success rate with the current standard-of-intendance 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.[43] Biopsies of patients given the treatment show reductions in liver damage and cirrhosis. Some testify shows giving interferon immediately following infection can prevent chronic hepatitis C, although diagnosis early in infection is hard since concrete symptoms are thin in early on hepatitis C infection. Command of chronic hepatitis C by IFN is associated with reduced hepatocellular carcinoma.[44]

Unconfirmed results suggested that interferon middle drops may be an effective treatment for people who accept herpes simplex virus epithelial keratitis, a type of centre infection.[45] In that location is no articulate prove to suggest that removing the infected tissue (debridement) followed past interferon drops is an effective treatment approach for these types of middle infections.[45] Unconfirmed results suggested that the combination of interferon and an antiviral agent may speed the healing process compared to antiviral therapy alone.[45]

When used in 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 torso temperature, feeling ill, fatigue, headache, muscle pain, convulsion, dizziness, hair thinning, and depression. Erythema, pain, and hardness at the site of injection are also oft observed. IFN therapy causes immunosuppression, in item through neutropenia and tin result in some infections manifesting in unusual means.[46]

Drug formulations [edit]

Pharmaceutical forms of interferons
Generic name Brand name
Interferon alfa Multiferon
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 blastoff 2a (Egypt) Reiferon Retard
PEGylated interferon alpha 2b PegIntron
Ropeginterferon alfa-2b Besremi
PEGylated interferon alpha 2b plus ribavirin (Canada) Pegetron

Several different types of interferons are approved for use in humans. One was showtime approved for medical use in 1986.[47] For example, in January 2001, the Food and Drug Administration (FDA) canonical the utilize of PEGylated interferon-alpha in the U.s.a.; in this conception, PEGylated interferon-alpha-2b (Pegintron), polyethylene glycol is linked to the interferon molecule to make the interferon final longer in the body. Blessing for PEGylated interferon-alpha-2a (Pegasys) followed in October 2002. These PEGylated drugs are injected once weekly, rather than administering two or iii times per calendar 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 to the lowest degree 75% of people with hepatitis C genotypes 2 or three do good from interferon treatment, although this is effective in less than fifty% of people infected with genotype 1 (the more common grade of hepatitis C virus in both the U.S. and Western Europe).[48] [49] [50] Interferon-containing regimens may likewise include protease inhibitors such equally boceprevir and telaprevir.

There are also interferon-inducing drugs, notably tilorone[51] that is shown to be effective confronting Ebola virus.[52]

History [edit]

Interferons were first described in 1957 past Alick Isaacs and Jean Lindenmann at the National Found for Medical Research in London;[53] [54] [55] 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 flu virus in chicken embryo chorioallantoic membranes by heat-inactivated influenza virus. Their experiments revealed that this interference was mediated by a poly peptide 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.[54] The findings of Isaacs and Lindenmann take been widely confirmed and corroborated in the literature.[56]

Furthermore, others may have fabricated observations on interferons before the 1957 publication of Isaacs and Lindenmann. For example, during research to produce a more than efficient vaccine for smallpox, Yasu-ichi Nagano and Yasuhiko Kojima—ii Japanese virologists working at the Constitute for Infectious Diseases at the University of Tokyo—noticed inhibition of viral growth in an expanse 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 cistron from tissue homogenates.[57] Independently, Monto Ho, in John Enders'south 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 cistron viral inhibitory factor (VIF).[58] It took another fifteen to twenty years, using somatic prison cell genetics, to show that the interferon activeness factor and interferon gene reside in different human chromosomes.[59] [60] [61] The purification of homo beta interferon did non occur until 1977. Y.H. Tan and his co-workers purified and produced biologically active, radio-labeled human beta interferon past superinducing the interferon factor in fibroblast cells, and they showed its active site contains tyrosine residues.[62] [63] Tan'southward laboratory isolated sufficient amounts of human beta interferon to perform the first amino acrid, carbohydrate limerick and North-terminal analyses.[64] They showed that homo beta interferon was an unusually hydrophobic glycoprotein. This explained the large loss of interferon activity when preparations were transferred from test tube to examination tube or from vessel to vessel during purification. The analyses showed the reality of interferon activeness by chemical verification.[64] [65] [66] [67] The purification of human alpha interferon was not reported until 1978. A series of publications from the laboratories of Sidney Pestka and Alan Waldman betwixt 1978 and 1981, draw the purification of the type I interferons IFN-α and IFN-β.[55] By the early on 1980s, genes for these interferons had been cloned, adding farther definitive proof that interferons were responsible for interfering with viral replication.[68] [69] Cistron cloning likewise confirmed that IFN-α was encoded by a family of many related genes.[70] The type Ii IFN (IFN-γ) gene was also isolated around this fourth dimension.[71]

Interferon was first synthesized manually at Rockefeller Academy in the lab of Dr. Bruce Merrifield, using solid phase peptide synthesis, 1 amino acid at a time. He after won the Nobel Prize in chemistry. Interferon was deficient and expensive until 1980, when the interferon factor was inserted into bacteria using recombinant Deoxyribonucleic acid technology, allowing mass tillage and purification from bacterial cultures[72] or derived from yeasts. Interferon can also be produced past recombinant mammalian cells.[73] Before the early 1970s, large scale production of human interferon had been pioneered past Kari Cantell. He produced big amounts of human being alpha interferon from large quantities of homo white blood cells collected by the Finnish Blood Depository financial institution.[74] Large amounts of homo beta interferon were fabricated past superinducing the beta interferon gene in human fibroblast cells.[75] [76]

Cantell's and Tan's methods of making large amounts of natural interferon were critical for chemic characterisation, clinical trials and the grooming of small amounts of interferon messenger RNA to clone the human being 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 adult equally 'betaseron' and approved for the treatment of MS. Superinduction of the homo beta interferon gene was too 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

[6] [77]

Teleost fish interferons [edit]

  • IFNa
  • IFNb
  • IFNc
  • IFNd
  • IFNe
  • IFNf
  • IFNg (gamma)
  • IFNh

[78] [79]

References [edit]

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  • Media related to Interferons at Wikimedia Commons

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Source: https://en.wikipedia.org/wiki/Interferon

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