FOB Test Card
- Known as:
- FOB Test Card
- Catalog number:
- INV-1042
- Product Quantity:
- 4.0mm (1000 strips in a card) 25cards/box
- Category:
- -
- Supplier:
- Innoragen
- Gene target:
- FOB Test Card
Related genes to: FOB Test Card
- Gene:
- MAVS NIH gene
- Name:
- mitochondrial antiviral signaling protein
- Previous symbol:
- -
- Synonyms:
- VISA, KIAA1271, IPS-1, Cardif
- Chromosome:
- 20p13
- Locus Type:
- gene with protein product
- Date approved:
- 2009-04-01
- Date modifiied:
- 2017-09-22
Related products to: FOB Test Card
Related articles to: FOB Test Card
- Ferroptosis has emerged as a promising strategy to overcome resistance to conventional cancer therapies. Pancreatic ductal adenocarcinoma (PDAC) is characterized by hypoxia, therapy resistance, and an immunosuppressive microenvironment. Although hypoxia is likely to influence ferroptosis susceptibility and the associated inflammatory pathways that regulate antitumor immunity, their impact on ferroptosis sensitivity and innate immune responses remains poorly understood. In this study, we investigated the effects of hypoxia on the induction of ferroptosis and immune-related signaling in PDAC cell lines. We examined how hypoxia affects the responses of Panc-1, BxPC3, and Capan-1 cells to the ferroptosis inducers RAS-selective lethal 3 (RSL3)/Imidazole ketone erastin (IKE) under normoxic and hypoxic (0.1% O) conditions. Cell viability assays were used to assess ferroptosis sensitivity, and rescue experiments were performed using liproxstatin-1 (LIP). Gene expression analysis was conducted to evaluate changes in immune, interferon, inflammatory, and hypoxia-related genes following ferroptosis induction. Panc-1 cells were the most sensitive, whereas Capan-1 cells were resistant, particularly under hypoxia. Ferroptosis triggered cell line-specific responses involving interferon signaling, inflammation, and stress pathways. Panc-1 cells showed over-expression of and , particularly under hypoxia, indicating activation of Type I interferon (IFN)-associated transcriptional program. BxPC3 cells demonstrated broader cytokine induction, including , , , , and , whereas Capan-1 cells were minimally responsive. Hypoxia also increased and expression following ferroptosis induction. These findings show that hypoxia differentially affects ferroptosis sensitivity and immune responses in PDAC, revealing complex interactions among ferroptosis, innate immunity, and the tumor microenvironment. - Source: PubMed
Publication date: 2026/07/18
Das ShubhankarMahmood Ayda ShahChouaib Salem - Vitamin D deficiency during pregnancy has been associated with increased risk for preterm birth (PTB). However, it is unclear if total 25-hydroxyvitamin D [25(OH)D], the primary measure of vitamin D status in clinical practice, accurately reflects biological availability. Therefore, we investigated three specific measures of Vitamin D (circulating maternal total 25(OH)D, vitamin D binding protein (VDBP), free 25(OH)D levels) in relation to PTB in a cohort of pregnant Black women using a nested case-control analysis. Plasma 25(OH)D was quantified using liquid chromatography-tandem mass spectrometry (LC-MS/MS) and VDBP measured using ELISA methods. Free 25(OH)D levels were calculated using verified equations. PTB was defined as delivery < 37 completed weeks' gestation. Logistic regression models were used to estimate the odds of PTB per 1 ng/mL increase in plasma 25(OH)D, VDBP and free 25(OH)D. Adjusted models accounted for gestational age at blood draw, pre-pregnancy BMI, preeclampsia diagnosis, and seasonality of sampling. Each incremental ng/mL increase in 25(OH)D was associated with a reduction in PTB odds in the unadjusted model (OR 0.95; 95% CI 0.92-0.99; p = 0.023). This association remained significant following multivariable adjustment (OR 0.96; 95% CI 0.92-0.99; p = 0.047). Other measures of Vitamin D were not significantly associated with PTB in unadjusted or adjusted models. These findings support a role for maternal vitamin D stores in maintaining pregnancy duration and highlight the need for mechanistic studies addressing placental steroid metabolism, inflammatory regulation, and interactions between vitamin D-dependent signaling and early parturition pathways. - Source: PubMed
Publication date: 2026/07/22
Woo JenniferGuffey ThomasHoang JennyObasanya MercyCarlson NicoleChun ReneMisra DawnGiurgescu Carmen - Porcine deltacoronavirus (PDCoV) is an emerging enteric coronavirus that causes substantial morbidity in swine and may pose a zoonotic risk because of its cross-species transmission potential. Type I interferon (IFN-I) signaling is central to antiviral defense, initiated through the mitochondrial antiviral signaling (MAVS)-TBK1-IFN regulatory factor 3 (IRF3) axis and executed by the downstream JAK-STAT1-STAT2-IRF9 (ISGF3) pathway; however, how PDCoV circumvents both the induction and effector arms of this cascade remains incompletely understood. Here, we identify PDCoV nonstructural protein 13 (Nsp13) as a potent antagonist of IFN-I responses. Ectopic expression of Nsp13 markedly reduces IFN-β production and the expression of IFN-stimulated genes (ISGs, such as ISG56 and CXCL10). Mechanistically, Nsp13 directly binds the C-terminal domain (CTD) of TBK1 and competitively disrupts TBK1 interactions with IRF3 and MAVS. In addition, Nsp13 preferentially binds IRF9 and impairs its nuclear translocation, thereby inhibiting IFN-α-induced signaling. Notably, PDCoV Nsp13 exhibits a host-target binding profile similar to that of SARS-CoV-2 Nsp13, yet it does not alter TBK1 ubiquitination or protein stability. Collectively, these findings reveal a dual-layer immune evasion strategy whereby PDCoV Nsp13 suppresses both IFN induction and downstream signaling, and highlighting Nsp13 as a potential target for antiviral intervention. - Source: PubMed
Wang YingLan ShijinFang ZhenghuiYang ShixingWang XiaochunShen QuanLiu YuweiWu PingZhou ChenglinZhang WenJi Likai - The persistent threat of porcine epidemic diarrhea virus (PEDV) to the global swine industry is compounded by high neonatal piglet mortality and the absence of effective antiviral therapies. Host-directed strategies that reinforce immunity offer a promising avenue to counter viral immune evasion. Through screening of an FDA-approved compound library, we identify the small-molecule cyclocytidine hydrochloride (Cyclo-C) as a potent inhibitor of PEDV replication that acts by stabilizing the peroxisomal biogenesis factor PEX13, a previously unrecognized host restriction factor. The antiviral activity of Cyclo-C is strictly PEX13-dependent, as it is completely abrogated in PEX13 knockout cells. Mechanistically, Cyclo-C disrupts the interaction between PEX13 and the viral nonstructural protein 8 (NSP8), thereby preventing NSP8-mediated PEX13 degradation and the subsequent induction of PI3K/AKT/mTOR-driven pexophagy. Preservation of peroxisomal integrity stabilizes the peroxisome-localized pool of MAVS, leading to a robust enhancement of type III interferon (IFN-III) responses that suppress viral replication. Critically, this mechanism translates , where Cyclo-C treatment of PEDV-challenged piglets significantly reduces mortality, lowers viral loads, and protects intestinal villus architecture. Our findings establish Cyclo-C as a first-in-class host-directed therapeutic candidate and validate the concept that pharmacological preservation of peroxisome-mediated innate immunity represents an effective antiviral strategy against enteric coronaviruses. - Source: PubMed
Publication date: 2026/07/17
Lou JinxiuGuo ZhiweiChen KangTian YuanmingyueTang ZhenpengXin ZhendongJiang PingLiu GongguanWang Xianwei - Coordination between innate immune signaling and glucose metabolism is fundamental to organismal homeostasis, yet despite decades of study linking immunity and metabolism, the mechanisms by which metabolic cells restrain antiviral innate signaling while preserving glycolytic competence during overnutrition remain poorly defined. Here we identify Tetherin (BST2) as a unique cell-intrinsic immunometabolic checkpoint that couples restraint of type I interferon (IFN-I) signaling to preservation of glycolytic capacity in adipocytes. Tetherin localizes to endoplasmic reticulum and organizes an interactome enriched for antiviral sensing regulators and glycolytic control nodes in adipocytes. Mechanistically, Tetherin directly engages the ubiquitin-dependent degradation machinery NDFIP1 and RNF128 to terminate IRF3 activation, thereby limiting pro-inflammatory, anti-glycolytic signaling and protecting adipocytes from metabolic dysfunction. In parallel, multiomics integration reveals that Tetherin also acts as a scaffold that binds and spatially organizes and activates PFKFB3 to increase glycolytic capacity and restrain MAVS-IRF3 innate immune signalling. In vivo, adipocyte-specific loss of Tetherin amplifies high sucrose diet and high-fat-diet-induced glucose intolerance and liver steatosis, whereas overexpression of human Tetherin in adipocyte suppresses obesity-driven interferon signaling, restores glycolytic pathway, and improves metabolic homeostasis. Orthogonal perturbations in cancer and insulinoma cells further confirm an immunometabolic role for Tetherin. Together, these findings define Tetherin as a dual node immunometabolic checkpoint that couples restraint of antiviral innate inflammatory signaling to maintenance of glycolytic competence, thereby safeguarding adipocyte metabolic homeostasis. - Source: PubMed
Publication date: 2026/07/07
Cho Chung HwanJang YoungUkWarnock AidanYildiz RamazanJhang JingDavi KajalBrisnovali Niki FHuhn VictoriaWang PengBevaqua RominaGoedeke LeighSchotsaert Michael ABerisa MirelaPuleston DanielRajbhandari Prashant