text:
Nicola Walker
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Not to be confused with Nicole Walker.
Nicola Walker
Born
(1970-05-15) 15 May 1970 (age 47)
Stepney, London, U.K.
Nationality
British
Education
Forest School, Walthamstow
Alma mater
New Hall, Cambridge
Footlights
Occupation
Actress
Years active
1990–present
Spouse(s)
Barnaby Kay
Children
Harry Kay
Nicola Walker (born 15 May 1970) is an English actress, known for her starring roles in various British television programmes from the 1990s onwards, including Ruth Evershed in the spy drama Spooks from 2003 to 2011. She has also worked in theatre, radio and film. In 2013, she won the Olivier Award for Best Supporting Actress for the play The Curious Incident of the Dog in the Night-Time. In 2014, she was nominated for the BAFTA TV Award for Best Supporting Actress for the BBC drama Last Tango in Halifax.
Contents
[hide]
1 Early life
2 Career
2.1 Television
2.2 Theatre
2.3 Film
2.4 Audio
3 Filmography
3.1 Film
3.2 Television
3.3 Video Games
4 Theatre credits
5 Personal life
6 References
7 External links
Early life[edit]
Walker was born in Stepney in the East End of London and has an older brother. She attended Saint Nicholas School, Old Harlow, and Forest School, Walthamstow, and undertook acting classes from age 12 to speak to boys.[1] Interviewed in 2014 by The Guardian, she said, "I was really encouraged by my mother. My dad thought it was a ridiculous thing to do."[2]
Walker then attended New Hall, Cambridge, where she started her acting career with the Cambridge Footlights. Her contemporaries included Spooks writer David Wolstencroft and comedian Sue Perkins, who were all part of the 1990 national tour.[3] Perkins, then an older undergraduate, was assigned to be her "college mother", although Walker later said: "She was the worst college mother I could have had .. They’re meant to hold your hand. She asked to borrow my bike, got drunk and I never saw it again." Walker acted on stage as Perkins's stooge and years later their partnership was resumed when Perkins cast Walker in her sitcom Heading Out.[2]
Career[edit]
Offered a place at RADA, on graduation from Cambridge, she already had some roles and an agent, so Walker decided to pursue her acting career. Based in London, she shared a flat with Perkins, Sarah Phelps, and Emma Kennedy, and acted at the Edinburgh Festival and the London Festival Fringe.[1]
Television[edit]
Her first major television roles were in 1997, as Gypsy Jones in Channel 4's adaptation of A Dance to the Music of Time, and as English teacher Suzy Travis in two series of Steven Moffat's school-based sitcom Chalk.[4] She has also appeared in guest roles in episodes of series such as Dalziel and Pascoe, Jonathan Creek, Pie in the Sky, and Broken News.
She got the leading part of DI Susan Taylor in the ITV thriller serial Touching Evil in 1997, co-starring opposite Robson Green. She also appeared in its two sequel serials in 1998 and 1999. Also in 1999, she took the lead role in the post-apocalyptic drama serial The Last Train, also screened on ITV (and written by future Spooks writer Matthew Graham). Also in 2003, Walker played Molly in the BBC Radio adaptation of Neuromancer by William Gibson.
In 2003, with the production team of Kudos Television looking to replace the character played by Jenny Agutter in Series 1 of Spooks, the part of Ruth Evershed was specially written for Walker from Series 2.[1] She remained with the show until the fifth series, during the production of which it was announced she was expecting her first child and would be leaving. She returned in 2009 and continued until the series ended in 2011. Benji Wilson of The Daily Telegraph praised Walker's performance, stating: "an actress who has squeezed every drop out of TV’s greatest ever largely dumbstruck doormat for the best part of a decade. Her scenes with Peter Firth, another fine player, have become self-contained little bubbles of weltschmerz within every recent episode".[5]
In 2007, Walker had a prominent supporting role as a child snatcher in the ITV1 drama serial Torn and appeared in the BBC adaptation of Oliver Twist.
In 2009, she appeared as a maid in a new BBC adaptation of Henry James' The Turn of the Screw, which also starred Michelle Dockery and Sue Johnston. In 2010, Walker appeared as a beleaguered wife (Linda Shand) of a murderer in an episode of the BBC1 crime thriller Luther.[6]
In February 2011, she appeared as nervous social worker Wendy in the BBC TV series Being Human.[7] In February 2012, she played a major character in the one off BBC crime drama Inside Men.
In 2012, 2013 and 2014/15, she appeared alongside Derek Jacobi, Anne Reid, and Sarah Lancashire, in three series of the BBC original drama Last Tango in Halifax.
In February and March 2013, Walker reunited with her former Cambridge Footlights colleague Sue Perkins in the BBC comedy Heading Out. She then appeared in the second series of Prisoners' Wives and the third series of Scott & Bailey.
Walker was again nominated for a Television BAFTA for "Best Supporting Actress" in 2014 for her role in Last Tango in Halifax, but the award was won by her co-star Sarah Lancashire.[8]
In 2015, she appeared as Jackie "Stevie" Stevenson, the colleague of DI John River played by Stellan Skarsgård, in the BBC drama series River.[9][10] She also starred as DCI Cassie Stuart, alongside actor Sanjeev Bhaskar as DS Sunil "Sunny" Khan, in the ITV drama series Unforgotten, which returned for a second series in January 2017.
Theatre[edit]
Walker won an Olivier Award in 2013 for Best Supporting Actress in her role as Judy, the main character Christopher's mother, in The Curious Incident of the Dog in the Night-Time. The play won seven Olivier Awards, equalling Matilda the Musical's record win in 2012.[11]
In 2014, she starred alongside Mark Strong and Phoebe Fox in Arthur Miller's play A View from the Bridge, at the Young Vic theatre. The play received extremely positive reviews from critics[citation needed] and transferred to Wyndham's Theatre in London's West End in 2015 and to the Lyceum Theatre on Broadway.
Film[edit]
In film, her roles have tended to be smaller supporting parts. Her most prominent role has been as the irritating folk singer in Four Weddings and a Funeral (1994), who sings "Can't Smile Without You" at the first wedding. She also appeared in the feature film adaptation of the classic television series Thunderbirds (2004).
In 2005, she portrayed a British journalist caught up in the Rwandan genocide in Shooting Dogs.
Audio[edit]
In July 2011, Walker played the significant supporting role of Medtech Liv Chenka in the Big Finish Productions Doctor Who audio drama Robophobia, opposite Sylvester McCoy as the Seventh Doctor. The Chenka character proved popular both with producers and listeners, and in February 2014 Walker returned to the role, this time as a foil for Paul McGann's Eighth Doctor in Dark Eyes 2. The character was sustained throughout Dark Eyes 3 and Dark Eyes 4, at the end of which it was revealed that Chenka was to continue as the Doctor's established travelling companion. In October 2015, Walker again returned to the role in the first volume of the 4-volume Doom Coalition. In 2017, she starred in the company's adaptation of the H.G. Wells novel The Shape of Things to Come.
Since 2013, Walker has voiced the Norwegian detective Annika Strandhed in three series of the BBC Radio 4 drama series Annika Stranded.
Filmography[edit]
Film[edit]
Year
Film
Role
Notes
1994 Four Weddings and a Funeral Frightful Folk Duo — Wedding One
1994 Milner Colette Brustein Television movie
1994 Faith Grace Television movie
1996 The Fortunes and Misfortunes of Moll Flanders Lucy Diver Television movie
1997 Cows Shirley Johnson Television movie
2000 Shiner Det. Sgt. Garland
2004 Thunderbirds Panhead's Mother
2005 Shooting Dogs Rachel
2007 Oliver Twist Sally Television movie
2009 The Turn of the Screw Carla Television movie
2014 Second Coming Counsellor
Television[edit]
Year
Film
Role
Notes
1997 Pie in the Sky Carol Episode: "In the Smoke"
1997 A Dance to the Music of Time Gypsy Jones Episode: "The Twenties"
1997 Chalk Suzy Travis 12 episodes
1997–1999 Touching Evil Susan Taylor/D.I. Susan Taylor 16 episodes
1998 Jonathan Creek WPC Fay Radnor Episode: "Mother Redcap"
1999 The Last Train Harriet Ambrose 5 episodes
2000 Dalziel and Pascoe Abbie Hallingsworth Episode: "A Sweeter Lazarus"
2001 People Like Us Helen Meredith Episode: "The Journalist"
2003–2011 Spooks Ruth Evershed 33 episodes
2004 Red Cap Maj. Rebecca Garton Episode: "Fighting Fit"
2005 Broken News Katie Willard 3 episodes
2007 Torn Joanna Taylor 3 episodes
2010 Luther Linda Shand Episode: "#1.4"
2010 Law & Order: UK Daniela Renzo Episode: "ID"
2011 Being Human Wendy Episode: "The Longest Day"
2012 Inside Men Kirsty Coniston 4 episodes
2012 New Tricks Helen Hadley Episode: "Old School Ties"
2012 A Mother's Son DC Sue Upton 2 episodes
2012–present Last Tango in Halifax Gillian 18 episodes
Nominated—BAFTA TV Award for Best Supporting Actress
Nominated—Satellite Award for Best Supporting Actress – Series, Miniseries or Television Film
2013 Prisoners' Wives DCI Jo Fontaine 4 episodes
2013 Heading Out Justine 6 episodes
2013 Scott & Bailey Helen Bartlett 4 episodes
2014 Babylon Sharon Franklin, Assistant Commissioner 7 episodes
2015— Unforgotten DCI Cassie Stuart 2 series (12 episodes)
2015 River DS Jackie "Stevie" Stevenson 6 episodes
2018 Collateral Jane Oliver Miniseries
Video Games[edit]
Year
Film
Role
2011 The Witcher 2: Assassins of Kings Síle de Tansarville
2015 The Witcher 3: Wild Hunt Síle de Tansarville
Theatre credits[edit]
Relocated – Royal Court Theatre London (2008)
Gethsemane – National Theatre London (2008/9)
Season's Greetings – National Theatre London (2010/11)
Di and Viv and Rose – Hampstead Theatre (Downstairs) London (2011)
The Curious Incident of the Dog in the Night-Time – National Theatre London (2012) for which she won the 2013 Olivier Award in the category 'Best Actress in a Supporting Role'
A View from the Bridge – Young Vic/Wyndham's Theatre (West End) London (2014/15), Lyceum Theatre on Broadway (2015/16)
Personal life[edit]
She is married to actor Barnaby Kay. The couple have a son Harry (born 2006), who is named after Harry Pearce, the character of her co-star Peter Firth in Spooks.[1]
References[edit]
^ Jump up to: a b c d "Spooks: Nicola Walker". Life of Wylie. Retrieved 28 February 2013.
^ Jump up to: a b "Nicola Walker: 'I've got a feisty face'". Telegraph.co.uk. 4 April 2014. Retrieved 1 February 2015.
Jump up ^ "Bestselling Fiction & Non-Fiction Authors, from The Orion Publishing Group". Orionbooks.co.uk. Retrieved 2013-11-26.
Jump up ^ After the Chalk Dust Settled, featurette on Chalk Series 1 DVD, ReplayDVD.co.uk, prod. & dir. Craig Robins
Jump up ^ Wilson, Benji (23 October 2011). "Spooks: the final episode, so ludicrously silly it might just be true, review". The Daily Telegraph. Telegraph Media Group. Retrieved 28 October 2011.
Jump up ^ "BBC One — Luther, Series 1". Bbc.co.uk. 2012-09-18. Retrieved 2013-11-26.
Jump up ^ "BBC Three — Being Human". Bbc.co.uk. 2013-05-24. Retrieved 2013-11-26.
Jump up ^ "Bafta for Last Tango in Halifax star Sarah Lancashire". Halifax Courier. 19 May 2014. Retrieved 6 September 2015.
Jump up ^ Adejobi, Alicia (4 September 2015). "Missing Broadchurch? ITV's new crime drama Unforgotten will become your new addiction". International Business Times. Retrieved 6 September 2015.
Jump up ^ "River – BBC One". BBC. Retrieved 2015-11-04.
Jump up ^ "Curious Incident wins seven". BBC News. 28 April 2013. Retrieved 28 April 2013.
External links[edit]
Nicola Walker on IMDb
Nicola Walker profile on the Spooks website at bbc.co.uk.
[hide]
v
t
e
Laurence Olivier Award for Best Performance in a Supporting Role
1977–1984
Actor
Nigel Hawthorne (1977)
Robert Eddison (1978)
Patrick Stewart (1979)
David Threlfall (1980)
Joe Melia (1981)
David Healy (1982)
Alan Devlin (1983)
Edward Petherbridge (1984)
Actress
Mona Washbourne (1977)
Elizabeth Spriggs (1978)
Doreen Mantle (1979)
Suzanne Bertish (1980)
Gwen Watford (1981)
Anna Massey (1982)
Abigail McKern (1983)
Marcia Warren (1984)
1985–1990
Merged
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Paul Jesson (1986)
Michael Bryant (1987)
Eileen Atkins (1988)
Michael Bryant (1989/1990)
1991–1995
Actor
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Julian Glover (1993)
Joseph Mydell (1994)
Ken Stott (1995)
Actress
Sara Crowe (1991)
Frances de la Tour (1992)
Barbara Leigh-Hunt (1993)
Helen Burns (1994)
Dora Bryan (1995)
1996–2002
Actor
Trevor Eve (1997)
Roger Allam (2000)
Ben Daniels (2001)
Toby Jones (2002)
Actress
Deborah Findlay (1997)
Patricia Hodge (2000)
Essie Davis (2001)
Marcia Warren (2002)
Merged
Simon Russell Beale (1996)
Sarah Woodward (1998)
Brendan Coyle (1999)
2003–2009
Merged
Essie Davis (2003)
Warren Mitchell (2004)
Amanda Harris (2005)
Noma Dumezweni (2006)
Jim Norton (2007)
Rory Kinnear (2008)
Patrick Stewart (2009)
2010–present
Actor
Eddie Redmayne (2010)
Adrian Scarborough (2011)
Richard McCabe (2013)
Jack Lowden (2014)
Nathaniel Parker (2015)
Mark Gatiss (2016)
Anthony Boyle (2017)
Actress
Ruth Wilson (2010)
Michelle Terry (2011)
Nicola Walker (2013)
Sharon D. Clarke (2014)
Angela Lansbury (2015)
Judi Dench (2016)
Noma Dumezweni (2017)
Merged
Sheridan Smith (2012)
Authority control
WorldCat Identities
VIAF: 9386331
SUDOC: 174316216
BNF: cb16509570k (data)
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Interferon
From Wikipedia, the free encyclopedia
Jump to: navigation, search
"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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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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