HemoVoid™ - Blood Card Reagent
- Known as:
- HemoVoid™ - Blood Card Reagent
- Catalog number:
- HVBC-10
- Product Quantity:
- 10 Dried Whole Blood Card 0.5” Spots
- Category:
- -
- Supplier:
- Biotech support group
- Gene target:
- HemoVoid™ - Blood Card Reagent
Related genes to: HemoVoid™ - Blood Card Reagent
- 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: HemoVoid™ - Blood Card Reagent
(Hydrazinocarbonyl)ferrocene labeling reagent for HP(Trifluoromethyl)trimethylsilane Ruppert reagent*Folic Acid Casei Medium USE For microbiological assay of folic acid in blood serum using Lactobacillus casei ATCC 7469.*Phenylethyl Blood Agar Base (Anaerobic) USE For selective isolation and cultivation of fastidious anaerobic bacteri0.5 m Reagent Feed Tube
0.5 m Reagent Feed Tube1,1,-CARBONYLDIMIDAZOLE 99% (CDI) (Reagent for Peptide Synthesis) (For Synthesis) CAS: 530-62-11,1,-CARBONYLDIMIDAZOLE 99% (CDI) (Reagent for Peptide Synthesis) (For Synthesis) CAS: 530-62-11,4-Dioxane 99% ACS Reagent Grade
1,4-Dioxane 99% ACS Reagent Grade
1,4-Dioxane 99% ACS Reagent Grade
1,4_Dioxane 99% ACS Reagent Grade _ Carc.1,4_Dioxane 99% ACS Reagent Grade _ Carc.1,4_Dioxane 99% ACS Reagent Grade1,4_Dioxane 99% ACS Reagent Grade Related articles to: HemoVoid™ - Blood Card Reagent
- Interferon (IFN) and inflammation are the key early defence mechanisms that combat pathogen infection. The cytosolic DNA sensor cGAS activates immune signaling via the stimulator of interferon genes (STING) protein. Emerging evidence suggests crosstalk between innate immune DNA and RNA sensing, implicating a role of STING protein in RNA virus infection. This study characterizes STING in the context of Japanese encephalitis virus (JEV), an RNA virus of the flaviviridae family. We observe that activation of type I IFN through MAVS is essential for cGAS and STING activation. Knockdown, null mutant and inhibitor studies confirm that STING restricts JEV replication independently of IFNβ signaling and autophagy. Transcriptomic analysis of STING (Goldenticket) bone-marrow derived macrophages (BMDMs) shows enhanced IFN response, but reduced activation of inflammatory cytokines and chemokines. Phosphorylated STING is recruited to the virus replication complex (RC), marked by the non-structural protein NS1, subsequently triggering the assembly of the NLRP3 inflammasome on the RC. STING proton channel activity is essential for NLRP3 inflammasome activation, IL-1β production, and activation of pyroptotic cell death markers. STING mice, show higher viremia, earlier disease onset, reduced survival, and decreased brain inflammation. These findings establish STING as a key regulator of JEV-induced inflammation and antiviral defence. - Source: PubMed
Publication date: 2026/05/30
Chhabra SimranPatel DhruvinSharma Kiran BalaSah VishalHarshan Krishnan HChauhan SantoshKalia Manjula - The genus Orthoflavivirus, encompassing formidable global pathogens such as Dengue (DENV), Zika (ZIKV), and West Nile (WNV) viruses, utilizes a compact positive-sense RNA genome to encode a sophisticated arsenal of seven non-structural (NS) proteins that dictate the outcome of the host-pathogen standoff. These proteins-NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5-function as a multifunctional molecular consortium, where the enzymatic dominance of the NS3 protease/helicase and NS5 polymerase/methyltransferase drives viral proteolysis and genomic synthesis. Simultaneously, the hydrophobic scaffolds of NS2A, NS4A, and NS4B orchestrate the biogenesis of endoplasmic reticulum-derived replication organelles, providing a privileged microenvironment that shields viral RNA from cellular sensors. Beyond replication, these proteins serve as the frontline of immune evasion; the secreted lipoprotein NS1 acts as a potent virulence factor by triggering "cytokine storms" and vascular permeability, while NS5 and the NS4 complex potently suppress Type I Interferon (IFN) signalling by intercepting the RIG-I/MDA5-MAVS axis and inducing the degradation of STAT transducers. Given the rapid expansion of mosquito vectors and the persistent absence of broad-spectrum antivirals, reviewing the structural biology and interactomes of these NS proteins is a critical priority for global biosecurity. By synthesising the current understanding of these "molecular architects," this review highlights how targeting the conserved interfaces of the replication complex can bridge the "therapeutic gap," offering a pathway toward universal countermeasures against current and emerging threats. - Source: PubMed
Publication date: 2026/05/27
Maity ChirantanMitra SouvikTripathi AnjaliKhobdagade SamyakBalachandran ChandhuSingh Pushpendra - Chikungunya virus (CHIKV) is an alphavirus that infects dermal fibroblasts as a primary target cell during natural mosquito-borne transmission. While primary human dermal fibroblasts (hDFs) have been implicated as a key source of type I interferon (IFN-I) during CHIKV infection, the dynamics of this response and its sufficiency for antiviral protection remain incompletely understood. Here, we systematically characterize in vitro CHIKV infection of primary hDFs, evaluating the effects of single-passage viral stock origin (mammalian- vs. mosquito-propagated), donor variability, and multiplicity of infection (MOI) on infection kinetics and innate immune induction. We demonstrate that hDFs support high-titered CHIKV replication at both MOI 1 and 0.01, resulting in universal cell death by 72 hpi despite robust IFNβ transcript induction-reaching up to ~2800-fold over mock-and secretion of pro-inflammatory cytokines, including IFNα2, TNFα, IL-1β, and IL-8. Notably, IFNβ protein levels remained below 10 pg/mL under all infection conditions, revealing a disconnect between transcriptional and translational responses, suggesting CHIKV-mediated translational suppression. Pharmacological inhibition of TBK1/IKKε via amlexanox did not suppress IFNβ transcript induction at any tested concentration, suggesting that canonical PRR signaling through this node-including both RIG-I/MAVS and TLR3/TRIF pathways-is not the major driver of the observed transcriptional response. In contrast, co-inoculation with exogenous IFNβ as low as 20 pg/mL activated IFNAR signaling, robustly upregulated interferon-stimulated genes (ISGs), and fully rescued hDFs from otherwise lethal infection. Together, these findings demonstrate that CHIKV-infected hDFs mount a transcriptionally robust but translationally insufficient innate immune response and that the transcriptional response appears to operate independently of TBK1/IKKε. These results have direct implications for understanding how the skin microenvironment may modulate early CHIKV pathogenesis and suggest that paracrine IFNβ signaling from neighboring cell types may be critical for fibroblast survival during natural infection. - Source: PubMed
Publication date: 2026/04/28
Taylor Meagan MRoberts Rosemary WRayner Jonathan O - The HIV-2/SIV lineage of lentiviruses encodes for Vpx, which is a virus-associated protein that is absent from HIV-1. Vpx enhances HIV-2 replication by degrading host proteins that possess antiviral activity. For example, Vpx is known to degrade the host dNTPase SAMHD1 (which reduces dNTP levels to inhibit viral DNA synthesis in macrophages) and components of the epigenetic regulator complex HUSH (where degradation enhances proviral gene expression and viral replication). Here, we used a transcriptomic analysis to investigate host gene expression response to HIV-2 infection of THP-1 cells in the presence and absence of Vpx. Analysis of HIV-2 WT and ΔVpx infected cells revealed an increase of gene expression of several interferon stimulating genes (ISGs), with an increase in ISG expression in HIV-2 WT infected cells relative to that of HIV-2 ΔVpx infected cells. Analysis of Vpx mutants implicated that Vpx-mediated induction of ISG expression was due to Vpx-mediated degradation of TASOR, one protein of the HUSH complex. Based upon these observations, we sought to determine whether Vpx-mediated degradation of TASOR and subsequent inhibition of HUSH complex activity induces ISG expression. TASOR degradation by Vpx led to increased LINE-1 activity and Vpx-mediated TASOR degradation induction of ISGs and was observed to rely on both RNA sensing that was mediated by MAVS signaling and DNA sensing mediated by cGAS/STING signaling. Taken together, these findings support a model in which Vpx-mediated inhibition of the HUSH complex is a key aspect of how Vpx affects the host response to HIV-2 replication in monocytic cells. - Source: PubMed
Publication date: 2026/05/25
Hanson Heather MDamkot Madeline RMansky Louis M - Duck plague virus (DPV) is a highly contagious pathogen that causes severe immunosuppression and high mortality in waterfowl, resulting in substantial economic losses to the poultry industry. However, the mechanisms by which DPV evades host innate immune responses remain incompletely understood. In this study, we investigated the role of the DPV tegument protein US2 in regulating host antiviral responses. pUS2 significantly suppressed IFN-β promoter activation induced by poly(I:C) and poly(dA:dT) and reduced the transcription of IFN-β and interferon-stimulated genes (ISGs), including OASL and Mx. Further analysis showed that pUS2 specifically inhibited IFN-β promoter activation triggered by the RIG-I/MDA5-MAVS signaling pathway. Co-immunoprecipitation and immunofluorescence assays demonstrated that pUS2 directly interacted with RIG-I in the cytoplasm and reduced its protein abundance in a dose-dependent manner. Mechanistically, pUS2 enhanced K48-linked ubiquitination of RIG-I and promoted its degradation through a p62-mediated autophagy pathway. Deletion of the US2 gene moderately reduced viral replication efficiency in DEF cells and enhanced expression of type I interferons and ISGs. In vivo experiments further showed that ducks infected with the US2-deleted virus exhibited reduced pathogenicity, including lower viral loads, milder tissue damage, and increased survival rates compared with those infected with the parental virus. Collectively, these findings demonstrate that DPV US2 antagonizes host innate immunity by targeting the RIG-I signaling pathway and promoting RIG-I degradation through autophagy. This study provides new insights into the immune evasion strategies of DPV and advances our understanding of DPV-host interactions. - Source: PubMed
Publication date: 2026/05/20
Hao YuanyuanXiong MeiyuanWang MingshuCheng Anchun