Amphetamine Test Card (Urine)
- Known as:
- Amphetamine Test Card (Urine)
- Catalog number:
- 4s00109
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Good Biotech Corp - GBC
- Gene target:
- Amphetamine Test Card (Urine)
Related genes to: Amphetamine Test Card (Urine)
- 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: Amphetamine Test Card (Urine)
Related articles to: Amphetamine Test Card (Urine)
- Herpes simplex virus 1 (HSV-1) is a globally prevalent pathogen that poses a significant health threat due to its lifelong latency. This persistence is driven by intricate immune evasion mechanisms, the deciphering of which remains a challenge. Here, we identified the HSV-1 tegument protein UL16 as a novel viral immunosuppressive factor, which significantly suppresses the RIGI-like receptor (RLR)-mediated antiviral immunity. We found that UL16 can interact with MAVS (mitochondrial antiviral signaling protein) and induce its degradation, thereby inhibiting type I interferon (IFN-I) production. Further investigation revealed that UL16-induced MAVS degradation was facilitated via mitophagy involving the mitochondrial cargo receptor FUNDC1 (FUN14 domain containing 1). Knockout of expression completely disrupted UL16-induced MAVS degradation and restricted HSV-1 replication. In contrast, overexpression of FUNDC1 augmented the suppressive effect of UL16 on MAVS-triggered IFN-I signaling and consequently benefited viral replication. Notably, the C-terminal domain (CTD) of UL16 primarily accounted for its immunosuppressive function, which was also demonstrated to be essential for UL16 engagement with MAVS, FUNDC1 and MAP1LC3/LC3 (microtubule associated protein 1 light chain 3). A conserved LC3-interacting region (LIR) motif within the UL16 CTD was identified to play a critical role in LC3 recruitment enhancement. Furthermore, the UL16-deficient HSV-1 exhibited markedly attenuated viral infectivity and pathogenicity . In summary, our findings uncover a previously uncharacterized pathway through which HSV-1 UL16 subverts host immunity by inducing mitophagy. This study provides critical insights into host-pathogen interactions and establishes a rational foundation for developing novel therapeutics against HSV-1 infection.:3-MA: 3-methyladenine; BNIP3L/NIX: BCL2 interacting protein 3 like; BSA: bovine serum albumin; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; CARD: caspase recruitment domain; Cas9: CRISPR-associated system 9; CGAS: cyclic GMP-AMP synthase; co-IP: co-immunoprecipitation; COX8: cytochrome c oxidase subunit 8; CQ: chloroquine; CRISPR: clustered regulatory interspaced short palindromic repeat; CTD: C-terminal domain; Ctrl: control; CXCL10: C-X-C motif chemokine ligand 10; DAPI: 4,'6-diamidino-2-phenylindole; DMEM: Dulbecco's modified Eagle's medium; DMSO: dimethyl sulfoxide; ds: double-stranded; FBS: fetal bovine serum; FUNDC1: FUN14 domain containing 1; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GFP: green fluorescent protein; HEK: human embryonic kidney; HSV-1: herpes simplex virus 1; IAV: influenza A virus; IFIH1/MDA5: interferon induced with helicase C domain 1; IFIT1/ISG56: interferon induced protein with tetratricopeptide repeats 1; IFN-I: type I interferon; IgG: Immunoglobulin G; IRF3: interferon regulatory factor 3; ISGs: IFN-stimulated genes; kDa: kilodalton; KO: knockout; KSHV: Kaposi sarcoma-associated herpesvirus; LIR: LC3-interacting region; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MAVS: mitochondrial antiviral signaling protein; Mdivi-1: mitochondrial division inhibitor 1; MG132: cbz-leu-leu-leucinal; MOI: multiplicity of infection; NanoBiT: NanoLuc Binary Technology; NC: negative control; NTD: N-terminal domain; OPTN: optineurin; p-: phosphorylated; PFU: plaque-forming unit; PINK1: PTEN induced kinase 1; poly(I:C): polyinosinic-polycytidylic acid; PRKN/parkin: parkin RBR E3 ubiquitin protein ligase; qPCR: quantitative polymerase chain reaction; RIGI/RIG-I: RNA sensor RIG-I; RLR: RIGI-like receptor; SARS-CoV-2: severe acute respiratory syndrome coronavirus 2; SeV: Sendai virus; sgRNA: single guide RNA; shRNA: short hairpin RNA; SQSTM1/p62: sequestosome 1; STING1: stimulator of interferon response cGAMP interactor 1; TBK1: TANK binding kinase 1; TM: transmembrane; TOMM20: translocase of outer mitochondrial membrane 20; TRAF: TNF receptor associated factor; TUFM: Tu translation elongation factor, mitochondrial; UL16: unique long region 16; VSV: vesicular stomatitis virus; VZV: varicella zoster virus; WCL: whole-cell lysate; WT: wild-type; Z-VAD-FMK: carbobenzoxy-valyl-alanyl-aspartyl-[O-methyl]-fluoromethylketone. - Source: PubMed
Publication date: 2026/07/02
Wang JingwenZhu RongliYi PingGan MengyaoLong Feng - Largemouth bass virus (LMBV) infection poses a significant threat to largemouth bass farming in China, yet effective and safe vaccines remain scarce. In this study, we designed and evaluated four mRNA vaccine candidates against LMBV, all encoding the viral major capsid protein (MCP). The fully configured construct (LMUM) contained a 5' cap1, untranslated regions (UTRs), and a poly(A) tail, and was produced by in vitro transcription. Each mRNA was encapsulated into lipid nanoparticles (LNPs), yielding homogeneous particles (∼110 nm diameter, ∼54 mV zeta potential) with >96% encapsulation efficiency that provided substantial protection against RNase degradation (43% of mRNA remained intact in LNP-encapsulated groups versus 10% in unprotected controls). Intramuscular immunization of largemouth bass with LNP-encapsulated LMUM (0.2 μg/g body weight) induced MCP-specific serum antibodies after primary immunization, with a strong booster response after the second dose. In the LMUM-immunized group, spleen mRNA levels of IgM and CD4 were upregulated 3.4-fold and 3.2-fold, respectively, by day 14, while the groups lacking UTR or cap/poly(A) tail failed to induce these adaptive immune markers. Interestingly, the incomplete constructs triggered stronger activation of the RIG-I pathway (RIG-I, MAVS, TBK1) than the fully modified LMUM, suggesting that the combination of cap1, UTR, and poly(A) tail helps dampen excessive innate sensing. Following a lethal LMBV challenge, the LMUM vaccine conferred 45-50% relative survival after primary immunization, which increased to 53-57% after the booster dose. In contrast, the incomplete vaccine constructs and naked mRNA gave only 10-15% survival, and control groups experienced nearly complete mortality. These results demonstrate that a fully modified mRNA-LNP vaccine against LMBV induces robust humoral and cellular immune responses and provides significant protective efficacy in largemouth bass. - Source: PubMed
Publication date: 2026/06/30
Liu YujunZhang GengrongQu HaozheHu ZiyuHe MaoshengLing FeiWang GaoxueLiu Tianqiang - Human trophoblast organoids (TOs) are three-dimensional ex vivo culture models that enable the study of placental development, physiology and pathology. A major limitation of TOs grown in Matrigel or other extracellular matrices is their apical-inward polarity, in which cytotrophoblasts (CTBs) line the outer surface and the multinucleated syncytiotrophoblast (STB) forms the interior layer, opposite to their orientation in vivo. Here we present a detailed protocol to reverse TO polarity, producing organoids that recapitulate the cellular orientation of human chorionic villi. Standard TOs with inward-facing STBs (STB) undergo polarity reversal during suspension culture to generate outward-facing STBs (STB). In parallel, we describe a complementary protocol for CRISPR-Cas9-mediated gene editing in TOs and illustrate its application in generating CGA (hCG) knockout organoids, which disrupt placental hormone secretion, and MAVS knockouts, which impair antiviral signaling. The outward-facing STB protocol can be completed in ~2 weeks, whereas the establishment of stable gene-edited TO lines requires 2-3 months. Successful implementation requires experience in TO culture, lentiviral transduction and CRISPR-Cas9-based genome editing. Together, these protocols provide versatile and reproducible methods for modeling placental architecture and studying gene function in vitro, enabling functional interrogation of trophoblast biology within physiologically oriented organoids. - Source: PubMed
Publication date: 2026/06/29
Yang LihengHatterschide JoshuaWorota Rizban ECooley KailaCoyne Carolyn B - How antiviral immunity first arose in animals is a central question in evolutionary biology. Here, using the sea anemone Nematostella vectensis, we identify CARDIB, a previously uncharacterized gene located next to RLRb-a cnidarian homologue of the vertebrate RIG-I-like receptor family. This conserved genomic linkage across Anthozoa reveals an ancient coupling between immune sensing and regulation. Despite sequence similarity to vertebrate MAVS, CARDIB performs an opposing function: it represses immune genes under basal conditions yet is essential for activation upon viral challenge. CARDIB binds RLRb through a single CARD domain, forming a repressive complex. Loss of either gene abolishes antiviral transcription, disrupts apoptosis and elevates viral load under laboratory conditions. Both genes, as well as the RLRb paralogue RLRa, are essential for antiviral defence under native conditions. Phylogeny places the cnidarian CARDs distinctly from the vertebrate RLR-MAVS families, revealing an ancient mechanism that regulates the antiviral response through CARD-based signalling. - Source: PubMed
Publication date: 2026/06/26
Sharoni TonJaimes-Becerra AdrianBirch SydneyKwak Hee-JinAleshkina DariaLewandowska MagdaSurm Joachim MJustin HannahAharoni ReuvenReitzel Adam MMoran Yehu - Mitochondria are dynamic organelles that continuously remodel their morphology through fusion and fission in response to cellular cues. While this dynamic behavior is essential for diverse cellular functions, how mitochondrial dynamics influence innate immune responses remains incompletely understood. Here, we show that mitochondrial hyperfusion-induced by loss of the fission factor DRP1 or by cellular stress, including cycloheximide or doxorubicin treatment-is associated with activation of a RIG-I-MAVS-dependent innate immune response and BAX-dependent cytosolic release of mitochondrial RNA. Functionally, our data suggest that this pathway contributes to enhanced susceptibility to NK cell-mediated cytotoxicity in vitro and reduced tumor growth in a xenograft model. Collectively, our findings identify mitochondrial hyperfusion-induced mtRNA release as a mechanism that engages innate immune signaling downstream of impaired mitochondrial dynamics. - Source: PubMed
Publication date: 2026/06/26
Yasuda TatsukiIchikawa AoiOnoue KentaOgasawara EmiIshihara TakayaKosako HidetakaIshihara Naotada