Drug Database
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interferon

✓ Approved

Sidus · IFNAR2 · Recombinant Proteins

What is interferon?

interferon is a recombinant proteins developed by Sidus. It is approved for therapeutic indications via injectable (others).

Drug Profile

CompanySidus
Drug ClassRecombinant Proteins
Molecular TargetIFNAR2
RouteInjectable (Others)
StatusApproved
Sources: ClinicalTrials.gov, Sidus

Mechanism of Action

Molecular Targets

interferon acts on 1 molecular target:

IFNAR2interferon alpha and beta receptor subunit 2 (IFNARB, IFN-alpha-REC)
Want deeper analysis?Noah AI can explain complex mechanisms and compare to similar drugs.

Therapeutic Indications

interferon is developed for 2 unique indications across 2 therapeutic areas.

Therapeutic AreaConditionPhase
Neoplasms benign, malignant and unspecified (incl cysts and polyps)Hairy cell leukaemia✓ Approved
Infections and infestationsSalmonellosis✓ Approved

Related Research Articles

PubMedJournal of molecular medicine (Berlin, Germany)2026-09-19

MicroRNA-122 as a regulator and biomarker of liver disease.

Ahmadova Sara S, Wicik Zofia Z, Mucha Joanna J, Palatini Jeff J et al.

MicroRNA-122 (miR-122) is the most abundant liver-specific microRNA, comprising ~ 70% of the hepatic miRNA pool, and a central regulator of lipid metabolism, inflammation, fibrosis, viral replication, and hepatocarcinogenesis. This review synthesizes experimental, clinical, and molecular evidence on the role of miR-122 across the spectrum of liver disease, including metabolic dysfunction-associated fatty liver disease (MAFLD) and steatohepatitis (MASH), drug-induced acute liver injury, hepatitis B and C virus (HBV/HCV) infection, hepatocellular carcinoma (HCC), and colorectal cancer liver metastasis. Mechanistically, miR-122 governs hepatic lipogenesis through the Sirt1/LKB1/AMPK axis, modulates inflammation via LPS/TLR-4/FoxO3 signaling, and exerts tumor-suppressive and antiviral effects through Cyclin G1/p53, HO-1, NDRG3, GALNT10, PEG10, and NEGR1. A recurring theme is the compartment- and stage-dependent behavior of miR-122: hepatic expression declines with disease progression, whereas circulating levels rise with hepatocyte injury, reconciling apparently contradictory reports and underscoring the importance of specimen source and disease stage in biomarker interpretation. We further contrast the etiology-specific regulation of miR-122 in HBV- versus HCV-associated disease, in which epigenetic silencing and interferon-linked mechanisms drive divergent expression. Finally, we critically appraise the failed clinical translation of anti-miR-122 therapeutics (miravirsen, RG-101), highlighting viral resistance, safety liabilities, and the tumor-suppressor paradox that constrains inhibition-based strategies. Collectively, miR-122 emerges as a minimally invasive biomarker and a biologically informative, though therapeutically challenging, target in liver disease.

PMID 42760391
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PubMedWorld journal of surgical oncology2026-09-19

Stress-driven reprogramming of plasmacytoid dendritic cells in intrahepatic cholangiocarcinoma defines a reversible targetable immunosuppressive state.

Chen Mei-Ru MR, Xie Xiao-Li XL, Zhou Yan-Li YL, Tian Jin-Mei JM et al.

Plasmacytoid dendritic cells (pDCs) have been implicated in both restraining and promoting intrahepatic cholangiocarcinoma (iCCA), leaving their clinical relevance and therapeutic potential unresolved. Mendelian randomization was used to assess the causal association between circulating pDC levels and iCCA risk. Bulk and single-cell transcriptomic analyses were performed to characterize pDC-related programs and tumor-conditioned states, and multiplex immunofluorescence was used to define spatial distribution and clinical associations in iCCA tissues. To assess reversibility of stress-associated pDC features, IRE1α RNase activity was pharmacologically inhibited with 4µ8C under tumor-conditioned stress in vitro. Genetically predicted higher circulating pDC levels were associated with lower iCCA risk, consistent with a systemic protective association. In bulk cohorts, higher expression of pDC markers (CLEC4C, NRP1, IL3RA) was associated with an immune-inflamed microenvironment and improved survival in early-stage disease. Single-cell analyses indicated that intratumoral pDCs acquired stress-associated transcriptional programs, including enrichment of endoplasmic reticulum stress and unfolded protein response pathways. In vitro, 4µ8C reduced IRE1α-dependent XBP1 splicing and partially restored type I interferon-linked activation and pDC immunogenic readouts under tumor-conditioned stress. Spatial profiling further showed that higher intratumoral CD303⁺IRF7⁺ pDC activation was associated with advanced stage and poorer overall survival, whereas higher activation in adjacent non-tumor tissues correlated with more favorable outcomes. Together, these findings support a context-dependent, stress-associated pDC program in iCCA and provide a rationale for further evaluating the IRE1α-XBP1 stress axis as a potential approach to modulate pDC-associated immune states within the tumor microenvironment.

PMID 42760567
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PubMedCell proliferation2026-09-19

Olfactory Tuft Cells Are Critical to Basal Inflammation, Innate Immune Response to Viral Infection, and Modulation of Quiescent Stem Cell Activation, Proliferation and Differentiation.

Zhang Sai-Sai SS, Wang Haiyan H, Yang Yi-Sen YS, Li Yi-Hong YH et al.

The olfactory mucosa serves as both a sensory organ and an immune barrier to protect against bacterial and viral invasion and other insults. It is unclear how different types of olfactory mucosal cells coordinate and contribute to these two functions. We set out to reveal the critical roles of a subset of microvillous cells of the mucosa, olfactory tuft cells, in protecting and reconstructing this vital olfactory sensory organ. We first validated the expression of canonical gustatory signalling proteins and other molecular markers in olfactory tuft cells. Genetic disruption of the Gng13 and Trpm5 genes that encode the two gustatory signalling proteins, G protein subunit Gγ13 and transient receptor potential ion channel Trpm5, respectively, resulted in elevated basal inflammation and enhanced activation of the quiescent stem cells-horizontal basal cells (HBCs) in the mucosa. Nasal infection of H1N1 influenza virus further exacerbated the inflammation and delayed the resolution of inflammation in the mutant mucosa, including more immune cell infiltration, augmented cytokine production and cell death, increased HBC proliferation and direct differentiation into tuft cells, and prolonged olfactory tuft cell hyperplasia. Cytokine treatment of the cultured olfactory epithelial organoids indicated that the cytokines that were found to be elevated in the mutant mucosa, including interleukin-4 (IL-4), IL-13 and interferon-γ (INF-γ), are able to stimulate HBC activation. Together, our results indicate that olfactory tuft cells play an important role in maintaining the baseline inflammation under the steady-state condition, and altering inflammatory magnitude and modulating HBC activation and differentiation in the olfactory mucosa following the viral infection. Our findings shed light on new roles of olfactory tuft cells in innate immune response, quiescent stem cell activation and neuroimmune interactions, and provide novel therapeutic targets for preventing and treating stem cell-related olfactory disorders such as chronic rhinosinusitis and long COVID.

PMID 42760864
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PubMedFrontiers in immunology2026-09-18

In vitro functional characterization of Tadarida brasiliensis interferon-β: promoter responsiveness, antiviral activity, and JAK-dependent transcriptional responses.

Liu Xingyu X, Li Shuhan S, Chen Weijia W, Wang Jie J et al.

Bats display diverse antiviral responses, but interferon-β remains poorly characterized in many bat species. Here, we characterized interferon-β from Tadarida brasiliensis (TBIFN-β) in Tb 1 Lu cells, focusing on its sequence features, promoter responsiveness, antiviral activity, and downstream signaling. TBIFN-β was analyzed by comparative sequence analysis and homology modeling. TBIFNB promoter fragments were evaluated using dual-luciferase assays following batIRF1 expression or poly(I:C) treatment. Antiviral activity was assessed using VSV-GFP and VACV-GFP infection models, together with viral transcript quantification by RT-qPCR. Downstream signaling was examined through interferon-stimulated gene expression, Pyridone 6-mediated JAK inhibition, conditioned-medium stimulation, STAT1 phosphorylation, and exploratory RNA sequencing followed by GO/KEGG enrichment analysis and RT-qPCR validation. TBIFN-β retained the principal predicted structural features of mammalian type I interferons. VSV-GFP and VACV-GFP infection induced distinct temporal changes in endogenous TBIFNB and interferon-stimulated gene expression. Both -900/0 and -500/0 TBIFNB promoter fragments responded to batIRF1 and poly(I:C). Transfection with the TBIFN-β expression construct reduced VSV-GFP and VACV-GFP fluorescence and decreased VSV-NP and VACV-C23L transcript copy equivalents. TBIFN-β induced context-dependent expression of PKR, OAS1, and Mx-1, with OAS1 showing the most consistent response. Pyridone 6 attenuated TBIFN-β-associated STAT1 and ISG responses and partially reduced its antiviral effects. Conditioned medium containing Flag-tagged TBIFN-β induced Pyridone 6-sensitive STAT1 phosphorylation in recipient cells. Transcriptomic analysis further revealed coordinated interferon-associated and antiviral transcriptional responses following TBIFN-β overexpression. These findings provide an integrated in vitro characterization of TBIFN-β promoter responsiveness, antiviral activity, and JAK-dependent transcriptional effects in Tb 1 Lu cells. The results establish a basis for further functional studies of T. brasiliensis interferon biology, while validation in primary bat cells and in vivo models remains necessary.

PMID 42755578
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PubMedFrontiers in immunology2026-09-18

Organelle-centered ISG15 biology: distinguishing covalent ISGylation from interferon-associated responses.

Li Zhuoer Z, Wang Chunli C, Zhang Jinrong J, Guo Zhiqiang Z

ISGylation is an interferon-inducible ubiquitin-like post-translational modification mediated by the interferon-stimulated gene 15 conjugation system. Initially characterized as an antiviral effector pathway, ISGylation is now increasingly recognized as a regulator of organelle homeostasis and cellular stress responses. This review summarizes emerging evidence linking ISG15-related mechanisms and covalent ISGylation to major organelle systems, including mitochondria, the endoplasmic reticulum-Golgi axis, endolysosomal compartments, ribosome-associated translation, and lipid droplets. We distinguish covalent ISGylation from free ISG15 signaling and ubiquitin specific protease 18-mediated interferon regulation, and further classify existing findings into evidence-based levels ranging from substrate-validated modification to correlative interferon signatures. At the mitochondrial level, direct and pathway-level evidence implicates ISG15 biology in DRP1-mediated fission, MFN1/2-associated mitophagy, oxidative metabolism, and redox regulation; direct effects of MFN1/2 ISGylation on mitochondrial fusion remain unproven. Along the ER-Golgi axis, ISG15-related pathways intersect with unfolded protein response signaling, endoplasmic reticulum-associated degradation, and stimulator of interferon genes-mediated innate immune activation. In the endolysosomal system, ISGylation and ISG15-associated pathways modulate autophagic flux, multivesicular body fate, and exosome secretion in a context-dependent manner. Ribosome-associated co-translational ISGylation links nascent protein surveillance with antiviral defense, whereas lipid droplet-associated ISG15/ISGylation pathways are linked to lipid metabolism and immune signaling. Current evidence supports an organelle-centered view of ISG15 biology but indicates that validated covalent mechanisms remain confined to selected substrates and contexts. Clinical translation will require organelle-resolved ISGylome mapping, substrate-level validation, and standardized biomarker assays before context-selective targeting can be considered.

PMID 42757191
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PubMedKidney international2026-09-18

Interferon signature in anti-neutrophil cytoplasmic antibody-negative patients.

Ilciukas Miquel Hugo H, De Saint Gilles David D, Rafat Cedric C

PMID 42760001
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