Alternative titles; symbols
HGNC Approved Gene Symbol: IFNB1
Cytogenetic location: 9p21.3 Genomic coordinates (GRCh38): 9:21,077,104-21,077,942 (from NCBI)
IFNB1 belongs to the type I inteferon family of cytokines. Binding of IFNB1 to its receptor, IFNAR1 (107450), results in immunoregulation, including antiviral and antiinflammatory effects. IFNB1 also plays a central role in neuronal homeostasis as a regulator of neuronal autophagy (summary by Ejlerskov et al., 2015).
From the nucleotide sequence of the gene for fibroblast interferon, cloned by recombinant DNA technology, Derynck et al. (1980) deduced the complete amino acid sequence of the protein, which contains 166 amino acids.
Cavalieri et al. (1977) showed that leukocyte and fibroblast interferon are encoded by different species of mRNA. That these arise from separate genes was demonstrated by Taniguchi et al. (1980). Between leukocyte interferon, or interferon-alpha (IFNA; 147660), and fibroblast interferon, or interferon-beta, they also found 45% homology at the nucleotide level and 29% at the amino acid level.
Diaz et al. (1988) demonstrated homozygous deletion of both the beta and alpha interferon genes in neoplastic hematopoietic cells, some of which had gross chromosomal deletions of chromosome 9p22-p21. The cell lines also demonstrated deficiency of the enzyme 5-prime-methylthioadenosine phosphorylase. The authors speculated that the homozygous deletions may be associated with the loss of a tumor-suppressor gene involved in neoplastic development; an alternative hypothesis was that the interferon genes themselves act as tumor-suppressor genes, and their deletion or inactivation may be associated with the development of neoplastic growth.
Siegal et al. (1999) demonstrated that purified interferon-producing cells were the CD4(+)CD11c(-) type-2 dendritic cell precursors, which produce 200 to 1,000 times more interferon than other blood cells after microbial challenge. Dendritic cell precursors are thus an effector cell type of the immune system, critical for antiviral and antitumor immune responses.
Takayanagi et al. (2002) demonstrated that RANKL (602642) induces the IFN-beta gene in osteoclast precursor cells, and that IFN-beta inhibits the differentiation of osteoclasts by interfering with the RANKL-induced expression of c-Fos (164810), an essential transcription factor for the formation of osteoclasts. This IFN-beta gene induction mechanism is distinct from that induced by virus, and is dependent on c-Fos itself. Thus an autoregulatory mechanism operates--the RANKL-induced c-Fos induces its own inhibitor. The importance of this regulatory mechanism for bone homeostasis is emphasized by the observation that mice deficient in IFN-beta signaling exhibit severe osteopenia accompanied by enhanced osteoclastogenesis.
Takaoka et al. (2003) demonstrated that transcription of the p53 gene (191170) is induced by IFNA/IFNB, accompanied by an increase in p53 protein level. IFNA/B signaling itself does not activate p53, but contributes to boosting p53 responses to stress signals. Takaoka et al. (2003) showed examples in which p53 gene induction by IFNA/B indeed contributed to tumor suppression. Furthermore, they showed that p53 is activated in virally infected cells to evoke an apoptotic response and that p53 is critical for antiviral defense of the host. Takaoka et al. (2003) showed that the p53 gene is transcriptionally induced by IFNA/B through ISGF3 (147574), demonstrating p53 gene induction by its cytokine. Whereas IFNA/B induce p53 mRNA and increase its protein level, p53-mediated responses such as cell cycle arrest or apoptosis were not observed in cells treated with IFNA/B alone.
Because type I IFNs are critical for regulation of osteoclastogenesis in mice, Coelho et al. (2005) compared the effects of IFNA2 (147562) and IFNB on differentiation of human monocytes into osteoclasts. Although primary monocytes undergoing osteoclastic differentiation were highly and equally sensitive to both proteins, IFNB was 100-fold more potent than IFNA2 at inhibiting osteoclastogenesis. Microarray and RT-PCR analyses showed that CXCL11 (604852) was the only gene differentially upregulated in this cellular system by IFNB compared with IFNA2. Treatment of monocytes with CXCL11 inhibited osteoclastic differentiation, and CXCL11 acted through a receptor distinct from CXCR3 (300574) and not through antagonism of CCR5 (601373). Coelho et al. (2005) proposed that IFNB may have clinical relevance in preventing osteolysis.
Using microarray, PCR, and complementarity analyses, Pedersen et al. (2007) identified 8 miRNAs that were rapidly upregulated in IFNB-stimulated mouse and human liver cell lines that showed sequence complementarity to hepatitis C virus (HCV; see 609532), an RNA virus, but not to hepatitis B virus (HBV; see 610424), a DNA virus. Of the 8 upregulated miRNAs, miR196 (MIRN196; 608632), miR296 (MIRN296; 610945), miR351 (MIRN351), miR431 (MIRN431; 611708), and miR448 (MIRN448; 300686) had anti-HCV activity, and miR196 and miR448 directly targeted HCV genomic RNA. IFNB stimulation downregulated miR122 (MIRN122A; 609582), a liver-specific miRNA essential for HCV replication. Pedersen et al. (2007) concluded that IFNA and IFNB, a common treatment regimen for HCV infection, use cellular miRNA, at least in part, to combat viral infections.
Wilson et al. (2013) demonstrated in mice infected with lymphocytic choriomeningitis virus (LCMV) that blockade of type I interferon (IFN-I) signaling diminished chronic immune activation and immune suppression, restored lymphoid tissue architecture, and increased immune parameters associated with control of virus replication, ultimately facilitating clearance of the persistent infection. The accelerated control of persistent infection induced by blocking IFN-I signaling required CD4 T cells and was associated with enhanced IFN-gamma (IFNG; 147570) production. Wilson et al. (2013) concluded that interfering with chronic IFN-I signaling during persistent infection redirects the immune environment to enable control of infection. Wilson et al. (2013) noted that human HIV and HCV infections are also associated with immune activation driven by chronic IFN-I signaling and suggested that a similar blockade of IFN-I may improve control of these infections.
Using RT-PCR and immunohistochemistry, Teles et al. (2013) demonstrated increased expression of the type I interferon IFNB in lesions of lepromatous leprosy (i.e., multibacillary, or L-lep) patients compared with tuberculoid leprosy (i.e., paucibacillary, or T-lep) patients (see 609888). Expression of an IFNB receptor, IFNAR1, was also increased in L-lep lesions. Increased expression of IFNB was associated with increased expression of IL10 (124092), and IFNB alone induced IL10 expression in mononuclear cells in vitro. There was an inverse correlation between IL10 expression and expression of the antimicrobial peptides CAMP (600474) and DEFB4 (DEFB4A; 602215). Measurement of uncultivable Mycobacterium leprae viability based on the ratio of M. leprae 16S rRNA to M. leprae repetitive element DNA indicated that IFNG induced antimicrobial activity against M. leprae in monocytes by about 35%, which was abrogated by the addition of either IFNB or IL10. Teles et al. (2013) concluded that the type I interferon gene expression program prominently expressed in L-lep lesions inhibits the IFNG-induced antimicrobial response against M. leprae through an intermediary, IL10.
The herpes simplex virus-1 (HSV-1) tegument protein UL36 contains an N-terminal deubiquitinase (DUB) motif called UL36 ubiquitin-specific protease (UL36USP). By expressing UL36USP in human embryonic kidney cells, Wang et al. (2013) identified host pathways affected by HSV-1 infection that resulted in inhibition of IFNB expression. UL36USP inhibited Sendai virus (SeV)-induced IRF3 (603734) dimerization and activation and transcription of IFNB. Mutation analysis confirmed that the DUB activity of UL36USP1 was required to block IFNB production. UL36USP also inhibited IFNB promoter activity induced by overexpression of the RIGI (DDX58; 609631) N terminus or MAVS (609676), but not TBK1 (604834), IKKE (IKBKE; 605048), or the active form of IRF3. UL36USP deubuitinated TRAF3 (601896) and prevented recruitment of TBK1. Cells infected with recombinant HSV-1 lacking UL36USP DUB activity produced more IFNB than cells infected with wildtype HSV-1. Wang et al. (2013) concluded that HSV-1 UL36USP removes polyubiquitin chains on TRAF3 and counteracts the IFNB pathway.
Using transfected HEK293T cells, Chen et al. (2015) showed that overexpression of RNF166 (617178) enhanced activation of the IFNB promoter after infection with SeV. RNF166 had no effect on cGAS (MB21D1; 613973)- or STING (612374)-induced activation of the IFNB promoter, suggesting that RNF166 responds selectively to RNA and not DNA virus infection. Knockdown of RNF166 in HEK293T cells inhibited IFNB promoter activation, IFNB transcription, and IFNB secretion in response to SeV infection. Similar results were observed with knockdown of RNF166 in HeLa cells. RNF166 interacted with TRAF3 and TRAF6 (602355), and knockdown of RNF166 suppressed SeV-induced ubiquitination of TRAF3 and TRAF6. Chen et al. (2015) proposed that RNF166 positively regulates RNA virus-triggered IFNB production by enhancing ubiquitination of TRAF3 and TRAF6.
Ferri et al. (2015) found that Trim33 (605769) deficiency was associated with increased Ifnb1 mRNA levels and increased IFN-beta secretion during the late stages of lipopolysaccharide (LPS) activation of mouse bone-marrow-derived macrophages (BMDMs). The coiled-coil domain of Trim33 was required for Ifnb1 regulation, as Trim33 lacking the coiled-coil domain failed to restore Ifnb1 expression to normal in activated Trim33 -/- cells. Chromatin immunoprecipitation-sequencing analysis revealed that Trim33 bound to a distal Ifnb1 gene regulatory element (ICE) in mouse macrophages. ICE functioned as a cis-acting transcriptional repressor element of Ifnb1 activation in macrophages. Binding of Trim33 and Pu.1 (165170) to ICE appeared to play an important role in repressing Ifnb1 transcription during the late phase of macrophage activation. ICE exhibited a promoter-like chromatin signature established early during myeloid differentiation. ICE interacted with the Ifnb1 proximal region in a constitutive and Trim33-independent manner, and this interaction was strengthened following LPS stimulation. Further investigation revealed that Trim33 regulated Ifnb1 expression by inhibiting Cbp (CREBBP; 600140)/p300 (EP300; 602700) recruitment, as enhanced CBP/p300 recruitment and activity at late times of activation were required for sustained Ifnb1 expression in Trim33 -/- BMDMs. The authors concluded that TRIM33 regulates IFNB1 expression at the late phase of macrophage activation by preventing recruitment of CBP/p300.
By study of human-mouse cell hybrids, Meager et al. (1979) concluded that chromosome 5 is not involved in production of interferon. Instead they found correlation between interferon production and chromosome 9, and the interferon produced by the hybrids was predominantly of the fibroblast type. Chany et al. (1980) likewise concluded that chromosome 9 carries a locus for an interferon, which they referred to as beta. Chromosome 13 also appeared to be involved. Chany et al. (1980) suggested that the locus on chromosome 13 might have something to do with IFNA synthesis.
Tavernier et al. (1981) presented evidence for a single fibroblast interferon gene. As in the case of IFN-alpha, no intervening sequences were discovered. Houghton et al. (1981) independently arrived at the same findings. Using radioactive probes from purified cDNA clones of interferons, Owerbach et al. (1981) located at least 8 leukocyte interferon genes and a fibroblast interferon gene on chromosome 9. Ohno and Taniguchi (1981) also showed that the beta-interferon gene(s), like the alpha-interferon genes, lacks intervening sequences. Comparison of the cDNA sequence of alpha and beta interferons showed apparent homology in amino acid sequence and in nucleotide sequence, indicating that they were presumably derived from a common ancestor. The fact that they are syntenic supports that conclusion.
By in situ hybridization, Trent et al. (1982) confirmed the location of IFF and IFL on chromosome 9p and concluded that IFF is distal to IFL. They mapped IFB to chromosome 9pter-p21. Studying 2 patients with unbalanced rearrangements of 9p, Henry et al. (1984) used a genomic clone for IFNB1 and concluded that the gene is located on chromosome 9p21.
Sagar et al. (1984) concluded that IFN-beta-related DNA is dispersed in the human genome. The data from study of human-rodent somatic cell hybrids induced with poly(I)poly(C) or with viral inducers were consistent with assignment of IFB mRNA species of different lengths to chromosomes 9, 5, and 2 (reviewed by Sagar et al., 1984). Another IFN-beta had been assigned to chromosome 4 (Sehgal et al., 1983).
Ohlsson et al. (1985) identified 5 RFLPs associated with the alpha- and beta-interferon gene cluster. Heterozygosities made them excellent markers for the short arm of chromosome 9. In a study of 25 Caucasian families, no recombination was found between the alpha and beta markers. Furthermore, 12 of 32 possible haplotypes were found, indicating linkage disequilibrium which was of similar magnitude between various alpha markers as it was between alpha and beta markers. Thus, the alpha and beta genes must be clustered within a few hundred kilobases. Duplication of the beta gene, apparently of recent origin, was found in some persons and segregated regularly.
By studying an acute monocytic leukemia (AMoL)-associated translocation t(9;11)(p22;q23), Diaz et al. (1986) concluded that the IFNB1 gene is located in chromosome 9p22, distal to alpha-interferon.
In 3 patients with AMoL and t(9;11)(p22;q23), Diaz et al. (1986) showed that the breakpoint on 9p split the interferon genes and that IFNB1 gene was translocated to chromosome 11. The ETS1 gene (164720) was translocated from chromosome 11 to 9p adjacent to the interferon genes. They suggested that juxtaposition of interferon and ETS1 genes may be involved in the pathogenesis of AMoL.
Ejlerskov et al. (2015) found that Ifnb -/- mice developed behavioral and cognitive impairments and neurodegeneration with age, as Ifnb was essential for neuronal survival, neurite outgrowth, and branching. Microarray analysis of Ifnb -/- neurons revealed pathways associated with neurodegenerative diseases, particularly Parkinson disease (PD; see 168600). Lack of Ifnb caused defects in the nigrostriatal dopaminergic pathway and led to Lewy body accumulation in Ifnb -/- brain. Ifnb signaling promoted neuronal autophagy and alpha-synuclein (SNCA; 163890) clearance. Consequently, Ifnb deficiency caused late-stage autophagy block, leading to reduced lysosomal fusion and alpha-synuclein accumulation in brain. In support of these results, Ifnb overexpression prevented dopaminergic neuron loss in a rat model of familial PD.
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