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How Do Viruses Act Agains Interferons

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

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

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

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

Interferons (IFNsouth, [1]) are a grouping 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 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 advice betwixt cells to trigger the protective defenses of the immune system that help eradicate pathogens.[3] Interferons are named for their ability to "interfere" with viral replication[iii] past protecting cells from virus infections. However, virus-encoded genetic elements take the power to antagonize the IFN response contributing to viral pathogenesis and viral diseases.[4] IFNs also have various other functions: they actuate immune cells, such every bit natural killer cells and macrophages, and they increment host defenses by up-regulating antigen presentation past virtue of increasing the expression of major histocompatibility circuitous (MHC) antigens. Certain symptoms of infections, such every bit fever, muscle hurting and "flu-similar symptoms", are as well caused past the production of IFNs and other cytokines.

More than 20 distinct IFN genes and proteins take been identified in animals, including humans. They are typically divided amongst three classes: Type I IFN, Type II IFN, and Blazon Three IFN. IFNs belonging to all 3 classes are important for fighting viral infections and for the regulation of the immune arrangement.

Types of interferon [edit]

Based on the type of receptor through which they betoken, human interferons accept been classified into three major types.

  • Interferon type I: All blazon I IFNs demark to a specific cell surface receptor complex known as 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.[6] In general, type I interferons are produced when the trunk recognizes a virus that has invaded it. They are produced past fibroblasts and monocytes. However, the production of type I IFN-α is inhibited by another cytokine known as Interleukin-10. Once released, blazon I interferons bind to specific receptors on target cells, which leads to expression of proteins that will prevent the virus from producing and replicating its RNA and DNA.[7] Overall, IFN-α tin be used to treat hepatitis B and C infections, while IFN-β tin can be used to treat multiple sclerosis.[3]
  • Interferon type II (IFN-γ in humans): This is as well known equally allowed interferon and is activated past Interleukin-12.[3] Type Two interferons are likewise released past cytotoxic T cells and type-i T helper cells. However, they block the proliferation of type-ii T helper cells. The previous results in an inhibition of Th2 immune response and a farther induction of Th1 immune response.[8] IFN type II binds to IFNGR, which consists of IFNGR1 and IFNGR2 chains.[three]
  • Interferon type Three: Signal through a receptor complex consisting of IL10R2 (also chosen CRF2-4) and IFNLR1 (too called CRF2-12). Although discovered more recently than type I and type Ii IFNs,[ix] recent information demonstrates the importance of Type Three IFNs in some types of virus or fungal infections.[10] [11] [12]

In general, blazon I and 2 interferons are responsible for regulating and activating the allowed response.[3] Expression of type I and III IFNs can be induced in virtually all cell types upon recognition of viral components, particularly 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 allowed 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, simply the benign activity in human tumors has not been widely documented. A virus-infected cell releases viral particles that tin can infect nearby cells. Even so, the infected jail cell 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 poly peptide 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 poly peptide, called eIF2B, to reduce protein synthesis within the cell. Some other cellular enzyme, RNAse L—also induced by interferon action—destroys RNA inside the cells to further reduce poly peptide synthesis of both viral and host genes. Inhibited protein synthesis impairs both virus replication and infected host cells. In addition, interferons induce production of hundreds of other proteins—known collectively equally interferon-stimulated genes (ISGs)—that have roles in combating viruses and other actions produced by interferon.[13] [14] They besides limit viral spread past increasing p53 activity, which kills virus-infected cells by promoting apoptosis.[15] [16] The effect of IFN on p53 is as well linked to its protective function against certain cancers.[15]

Another office of interferons is to up-regulate major histocompatibility complex molecules, MHC I and MHC Two, and increase immunoproteasome activity. All interferons significantly enhance the presentation of MHC I dependent antigens. Interferon gamma (IFN-gamma) also significantly stimulates the MHC Ii-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, amongst others) that indicate to and co-ordinate the activity of other immune cells.[17] [18] [xix]

Interferons can also suppress angiogenesis by downwardly regulation of angiogenic stimuli deriving from tumor cells. They besides suppress the proliferation of endothelial cells. Such suppression causes a decrease in tumor angiogenesis, a subtract 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] [xix]

Induction of interferons [edit]

Product 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—past blueprint 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 three (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 tin can either silence or stimulate interferon pathways.[20] Release of IFN from cells (specifically IFN-γ in lymphoid cells) is too induced by mitogens. Other cytokines, such equally interleukin ane, interleukin 2, interleukin-12, tumor necrosis factor and colony-stimulating factor, tin can likewise raise interferon product.[21]

Downstream signaling [edit]

By interacting with their specific receptors, IFNs activate bespeak transducer and activator of transcription (STAT) complexes; STATs are a family of transcription factors that regulate the expression of certain immune organization genes. Some STATs are activated by both type I and type II IFNs. Yet each IFN blazon tin can also activate unique STATs.[22]

STAT activation initiates the well-nigh well-defined prison 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, following receptor engagement with IFN, phosphorylate both STAT1 and STAT2. As a result, an IFN-stimulated factor factor three (ISGF3) complex forms—this contains STAT1, STAT2 and a 3rd transcription factor called IRF9—and moves into the cell nucleus. Within the nucleus, the ISGF3 circuitous 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 grade from dissimilar combinations of STAT-ane, -3, -iv, -5, or -vi during IFN signaling; these dimers initiate gene transcription by binding to IFN-activated site (GAS) elements in gene promoters.[22] Type I IFNs tin induce expression of genes with either ISRE or GAS elements, just gene induction by blazon Ii IFN can occur only in the presence of a GAS element.[22]

In addition to the JAK-STAT pathway, IFNs tin can activate several other signaling cascades. For instance, both type I and type II IFNs activate a fellow member of the CRK family unit of adaptor proteins chosen CRKL, a nuclear adaptor for STAT5 that likewise regulates signaling through the C3G/Rap1 pathway.[22] Type I IFNs further activate p38 mitogen-activated protein kinase (MAP kinase) to induce gene transcription.[22] Antiviral and antiproliferative effects specific to type I IFNs effect from p38 MAP kinase signaling. The phosphatidylinositol three-kinase (PI3K) signaling pathway is also regulated past both type I and type Two IFNs. PI3K activates P70-S6 Kinase one, an enzyme that increases protein synthesis and jail cell proliferation; phosphorylates ribosomal poly peptide s6, which is involved in poly peptide synthesis; and phosphorylates a translational repressor protein chosen eukaryotic translation-initiation factor 4E-bounden protein 1 (EIF4EBP1) in order to conciliate it.[22]

Interferons can disrupt signaling by other stimuli. For example, Interferon alpha induces RIG-G, which disrupts the CSN5-containing COP9 signalosome (CSN), a highly conserved multiprotein complex implicated in poly peptide deneddylation, deubiquitination, and phosphorylation.[24] RIG-G has shown the chapters 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 take 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, past 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 as man cytomegalovirus (HCMV) and Kaposi's sarcoma-associated herpesvirus (KSHV or HHV8).[26] [27] Viral proteins proven to impact IFN signaling include EBV nuclear antigen 1 (EBNA1) and EBV nuclear antigen two (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.[27] [28] 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).[26] Several poxviruses encode soluble IFN receptor homologs—similar the B18R protein of the vaccinia virus—that bind to and forbid IFN interacting with its cellular receptor, impeding advice between this cytokine and its target cells.[28] Some viruses can encode proteins that demark 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 cistron, p25.[29] [30] [31] The ability of interferon to induce poly peptide product from interferon stimulated genes (ISGs) tin also be affected. Product of protein kinase R, for example, tin can exist disrupted in cells infected with JEV.[26] Some viruses escape the anti-viral activities of interferons by gene (and thus protein) mutation. The H5N1 influenza virus, also known every bit bird flu, has resistance to interferon and other anti-viral cytokines that is attributed to a single amino acrid change in its Non-Structural Protein one (NS1), although the precise mechanism of how this confers immunity is unclear.[32]

Coronavirus response [edit]

Coronaviruses evade innate immunity during the kickoff 10 days of viral infection.[33] In the early stages of infection, SARS-CoV-two induces an fifty-fifty lower interferon type I (IFN-I) response than SARS-CoV, which itself is a weak IFN-I inducer in man cells.[33] SARS-CoV-2 limits the IFN-III response also.[34] Reduced numbers of plasmacytoid dendritic cells with age is associated with increased COVID-xix severity, possibly because these cells are substantial interferon producers.[35]

Ten percent of patients with life-threatening COVID-19 have autoantibodies against type I interferon.[35]

Delayed IFN-I response contributes to the pathogenic inflammation (cytokine storm) seen in later 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 control multiple sclerosis, an autoimmune disorder. This handling may help in reducing attacks in relapsing-remitting multiple sclerosis[37] and slowing affliction progression and activity in secondary progressive multiple sclerosis.[38]

Interferon therapy is used (in combination with chemotherapy and radiation) as a handling for some cancers.[39] This handling can exist 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.[40] Both hepatitis B and hepatitis C are treated with IFN-α, oft 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 exist treated with a 60-80% success rate with the current standard-of-care treatment of interferon-α, ribavirin and recently approved protease inhibitors such every bit Telaprevir (Incivek) May 2011, Boceprevir (Victrelis) May 2011 or the nucleotide analog polymerase inhibitor Sofosbuvir (Sovaldi) December 2013.[43] Biopsies of patients given the handling show reductions in liver damage and cirrhosis. Some evidence shows giving interferon immediately post-obit infection tin can foreclose chronic hepatitis C, although diagnosis early on in infection is difficult since concrete symptoms are sparse in early hepatitis C infection. Control of chronic hepatitis C by IFN is associated with reduced hepatocellular carcinoma.[44]

Unconfirmed results suggested that interferon eye drops may be an effective treatment for people who have herpes simplex virus epithelial keratitis, a type of centre infection.[45] There is no clear evidence to suggest that removing the infected tissue (debridement) followed past interferon drops is an constructive treatment approach for these types of eye infections.[45] Unconfirmed results suggested that the combination of interferon and an antiviral agent may speed the healing process compared to antiviral therapy lone.[45]

When used in systemic therapy, IFNs are generally administered by an intramuscular injection. The injection of IFNs in the muscle or under the skin is generally well tolerated. The virtually frequent adverse effects are flu-similar 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 frequently observed. IFN therapy causes immunosuppression, in detail through neutropenia and tin result in some infections manifesting in unusual ways.[46]

Drug formulations [edit]

Pharmaceutical forms of interferons
Generic name Brand proper noun
Interferon alfa Multiferon
Interferon alpha 2a Roferon A
Interferon alpha 2b Intron A/Reliferon/Uniferon
Human being leukocyte Interferon-alpha (HuIFN-blastoff-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 blastoff 2a Pegasys
PEGylated interferon alpha 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 utilize in humans. One was offset approved for medical use in 1986.[47] For example, in Jan 2001, the Nutrient and Drug Administration (FDA) approved the use of PEGylated interferon-alpha in the Us; 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 Oct 2002. These PEGylated drugs are injected once weekly, rather than administering two or 3 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 do good 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).[48] [49] [50] Interferon-containing regimens may too include protease inhibitors such as 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 Institute for Medical Inquiry 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 arrangement 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 oestrus-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 have been widely confirmed and corroborated in the literature.[56]

Furthermore, others may accept 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—2 Japanese virologists working at the Plant 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 narrate this factor from tissue homogenates.[57] Independently, Monto Ho, in John Enders's lab, observed in 1957 that attenuated poliovirus conferred a species specific anti-viral upshot in human amniotic cell cultures. They described these observations in a 1959 publication, naming the responsible factor viral inhibitory gene (VIF).[58] It took another fifteen to twenty years, using somatic cell genetics, to show that the interferon action gene and interferon cistron reside in different human chromosomes.[59] [60] [61] The purification of homo beta interferon did not occur until 1977. Y.H. Tan and his co-workers purified and produced biologically active, radio-labeled human beta interferon by superinducing the interferon cistron in fibroblast cells, and they showed its active site contains tyrosine residues.[62] [63] Tan's laboratory isolated sufficient amounts of human beta interferon to perform the first amino acid, sugar limerick and N-terminal analyses.[64] They showed that man 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 action by chemical verification.[64] [65] [66] [67] The purification of human alpha interferon was non reported until 1978. A series of publications from the laboratories of Sidney Pestka and Alan Waldman between 1978 and 1981, depict 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 further definitive proof that interferons were responsible for interfering with viral replication.[68] [69] Factor cloning also confirmed that IFN-α was encoded past a family of many related genes.[lxx] The type Two IFN (IFN-γ) gene was also isolated around this time.[71]

Interferon was first synthesized manually at Rockefeller University in the lab of Dr. Bruce Merrifield, using solid stage peptide synthesis, one amino acrid at a fourth dimension. He afterwards won the Nobel Prize in chemistry. Interferon was scarce and expensive until 1980, when the interferon gene was inserted into leaner using recombinant Dna engineering science, assuasive mass cultivation and purification from bacterial cultures[72] or derived from yeasts. Interferon can also be produced by recombinant mammalian cells.[73] Before the early 1970s, big calibration production of human being interferon had been pioneered by Kari Cantell. He produced big amounts of man alpha interferon from large quantities of human being white blood cells collected by the Finnish Claret Bank.[74] Large amounts of human beta interferon were fabricated by superinducing the beta interferon gene in human fibroblast cells.[75] [76]

Cantell'southward and Tan's methods of making large amounts of natural interferon were critical for chemic characterisation, clinical trials and the preparation of small amounts of interferon messenger RNA to clone the human being alpha and beta interferon genes. The superinduced man beta interferon messenger RNA was prepared by Tan's lab for Cetus corp. to clone the homo beta interferon gene in bacteria and the recombinant interferon was adult as 'betaseron' and canonical for the treatment of MS. Superinduction of the human beta interferon gene was as well used by Israeli scientists to industry homo beta interferon.

Homo 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]

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External links [edit]

  • Media related to Interferons at Wikimedia Commons

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

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