antimycin a (MedChemExpress)
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MedChemExpress
antimycin a
Antimycin A, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/antimycin a/product/MedChemExpress
Average 94 stars, based on 35 article reviews
Antimycin A, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/antimycin a/product/MedChemExpress
Average 94 stars, based on 35 article reviews
antimycin a - by Bioz Stars,
2026-02
94/100 stars
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1) Product Images from "Antimycin A inhibits alpha-herpesvirus replication by disrupting the formation of pyrimidinosomes"
Article Title: Antimycin A inhibits alpha-herpesvirus replication by disrupting the formation of pyrimidinosomes
Journal: Journal of Advanced Research
doi: 10.1016/j.jare.2025.05.016
Figure Legend Snippet: Mapping the stage of BHV-1 life cycle targeted by Antimycin A. (A and B) Time-of-addition assay used to identify the steps of BHV-1 life cycle which can be inhibited by Antimycin A. MDBK cells were infected with BHV-1-ΔgIE-eGFP/Gluc (MOI = 0.5) for 1 h to synchronize infection, after which the inoculum was removed. Cells were incubated with the indicated compound at specific time points. Viral infection was quantified 24 h post-inoculation using a Gaussia Luciferase Flash Assay to measure viral CPE. Data were normalized to the DMSO-treated wells at each time point and are presented as mean ± SEM from n = 3 independent experiments. (C, D, and E) The qPCR analysis of viral genome copies during attachment, entry and replication in the presence of Antimycin A. MDBK cells were pretreated with Antimycin A for 12 h at the indicated concentrations and adsorbed with BHV-1-WT (MOI = 5) for 1 h at 4 °C. Unabsorbed virus was removed by washing with PBS. (C) PBS-washed cells were harvested, and intracellular viral DNA was isolated and quantified by qPCR. (D) Cells were allowed to continue entry of the virus at 37 °C for 1 h. Afterward, cells were harvested, and intracellular viral DNA was isolated and quantified by qPCR. (E) After incubation at 37 °C for 8 h, cells were harvested, and intracellular viral DNA was isolated and quantified by qPCR. For each condition, BHV-1-WT DNA levels relative to DMSO-treated wells are shown for n = 4 biological replicates. Significance was assessed with two-tailed and unpaired Student's t -test, ****p < 0.0001, ***p < 0.001, **p < 0.01, *p < 0.05, ns = no significant.
Techniques Used: Infection, Incubation, Luciferase, Virus, Isolation, Two Tailed Test
Figure Legend Snippet: Antiviral activity of Antimycin A in relevant cell lines and primary cells . Dose–response analysis of Antimycin A against the BHV-1 in MDBK cell line (A), plaque assay (B), Western blotting (C) and TCID 50 (D). MDBK cells were pretreated with increasing concentrations of Antimycin A or Ara-C (50 μM) for 12 h, followed by infection with BHV-1 wild type (WT) at an MOI of 0.5. (A) Dose–response analysis of Antimycin A against the BHV-1-ΔgIE-eGFP/Gluc, showing infectivity (black), cell number (orange) and IC50 values. (B) The quantity of released infectious virions was measured by plaque assay, with data representing the means ± SEM from n = 2 independent experiments, normalized to DMSO-treated controls. The anti-BHV-1 IC50 value was determined through nonlinear regression analysis. (C) Western blot analysis of infected cells after 24 h, using anti-BHV-1 serum to quantify infection levels, with β-actin as a loading control. (D) Quantified the released infectious virions by measuring the CPE in MDBK cells, and data are presented as log10 ± SEM of infectious particle concentration (TCID 50 /mL) from n = 3 independent experiments. HacaT cells (E), Vero-E6 cells (F), primary bovine turbinate osteocytes (G), and primary bovine tracheal epithelial cells (H) were pretreated for 12 h with various concentrations of Antimycin A and subsequently infected with BHV-1-ΔgIE-eGFP/Gluc at an MOI of 0.5. Infection levels were quantified 24 h later using a Gaussia Luciferase Flash Assay, while cell viability was measured using the CCK-8 Assay. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
Techniques Used: Activity Assay, Plaque Assay, Western Blot, Infection, Control, Concentration Assay, Luciferase, CCK-8 Assay
Figure Legend Snippet: Antimycin A exhibits extensive antiviral activity against alpha-herpesvirus. Antimycin A effectively inhibited HSV-1 (A-C) and HSV-2 (G-H) infections in Vero E6 cells, PRV (D-E) infection in PK-15 cells, and EHV-1 (J-K) infection in RK13 cells. Vero-E6 cells, PK-15 cells, and RK13 cells were pretreated for 12 h with increasing concentrations of Antimycin A and then infected with HSV-1 (A-C), PRV (D-E), HSV-2 (G-I), and EHV-1 (J-K) at MOIs of 0.5, 0.1, 0.5, and 0.5, respectively. At 24 hpi, cells were fixed and analyzed by fluorescence imaging. (A, D, G and J) Infection levels were quantified using a fluorescent microplate reader (black curve), while cell viability was measured using the CCK-8 Assay (orange curve). The CC50 for each compound was calculated via a four-parameter logistic nonlinear regression model in GraphPad Prism. Dotted lines indicate 50 % inhibition. Data represent the means ± SEM from n = 3 independent experiments of infectious virions, normalized to DMSO-treated wells. The IC50 values for HSV-1, PRV, HSV-2, and EHV-1 were determined by nonlinear regression analysis. (B, E, H and K) eGFP expression in infected cells, either untreated (0 μM) or treated with various concentrations (0.0015–5 μM) of Antimycin A, was visualized by fluorescence microscopy at the same time point. Representative images are shown. Bars, 300 µm. Magnification, ×10. (C, F and I) Western blot analysis was performed to quantify infection in cells infected with HSV-1, PRV, or HSV-2. For HSV-1, infection was assessed using ICP4, VP16, and gD as markers. For PRV, infection levels were quantified by immunoblotting for UL54. For HSV-2, infection was quantified by immunoblotting for VP16. β-actin was used as the loading control. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
Techniques Used: Activity Assay, Infection, Fluorescence, Imaging, CCK-8 Assay, Inhibition, Expressing, Microscopy, Western Blot, Control
Figure Legend Snippet: Antimycin A affects the pyrimidine metabolism in infected cells. (A) Flowchart of untargeted metabolomics analysis of MDBK cells infected with BHV-1 and treated with Antimycin A. MDBK cells were pre-treated with 20 nM Antimycin A for 12 h, and then infected with BHV-1 at MOI of 0.5. After infection, the cells were collected and treated with methanol at 24 h. (B) Enrichment analysis of differential metabolites. Comparative analysis against the control group (Unprocessed group) was performed to identify infection- or drug treatment-induced differential metabolites, followed by functional enrichment analysis. (C) Significantly altered metabolites following Antimycin A treatment. The peak area of metabolites in different groups is shown. (D-I) Changes in key metabolites related to de novo pyrimidine synthesis, including aspartate (D), carbamoyl-aspartate (E), dihydroorotate (DHOA) (F), orotate (G), UMP (H), and uridine (I), in the untargeted metabolomics analysis. Changes in the key metabolites related to de novo pyrimidine synthesis. Relative quantification of metabolites was achieved through normalization against the control group. Mean values ± SDs are shown (n = 4). Significance was assessed with two-tailed and unpaired Student's t -test, ***p < 0.001, **p < 0.01, *p < 0.05, ns = no significant.
Techniques Used: Infection, Control, Functional Assay, Quantitative Proteomics, Two Tailed Test
Figure Legend Snippet: Uridine antagonizes the antiviral potency of Antimycin A. (A-C) Inhibitory effect of Antimycin A on BHV-1 infection was counteracted by excess uridine supplementation: MDBK cells were treated with different concentrations of Antimycin A in the presence of excess uridine at the time of BHV-1 infection (MOI = 0.5). (A) Viral infection was quantified at 24 hpi using a Gaussia Luciferase Flash Assay. Statistical significance was determined using a two-tailed unpaired Student's t -test: ****p < 0.0001, ns = no significant difference. (B) eGFP fluorescent expression in infected cells at the same time point (hpi) was visualized. Representative images are shown. Scale bars, 300 µm. Magnification, ×10. (C) Western blot was performed to quantify infection using anti-BHV-1 serum. β-actin was used as a loading control. (D) Schematic of the pyrimidine biosynthesis pathway: The de novo pathway generates uridine triphosphate (UTP) from cellular L-glutamine, while the salvage pathway can support pyrimidine synthesis by recycling preexisting nucleotides from extracellular sources, such as uridine. (E-H) Effect of pyrimidine intermediates on Antimycin A treatment: MDBK cells were treated with Antimycin A along with 100 μM of L-Aspartic acid (E), L-Hydroorotic acid (F), Orotic acid (G), or Orotidine (H) at the time of BHV-1 infection (MOI = 0.5). Infection was quantified at 24 hpi using a Gaussia Luciferase Flash Assay. Statistical significance was assessed using a two-tailed unpaired Student's t -test: ****p < 0.0001.
Techniques Used: Infection, Luciferase, Two Tailed Test, Expressing, Western Blot, Control
Figure Legend Snippet: Antimycin A reduces the pyrimidinosome formation in BHV-1 infected cells. (A) Molecular docking of Antimycin A and DHODH. (B) Molecular docking of Antimycin A and VDAC3. (C) In vitro purification of DHODH and VDAC3. (D) SPR tests of the binding between Antimycin A and DHODH. With the DHODH concentration fixed at 10 μg /mL, the association and dissociation rates of Antimycin A binding to DHODH were measured at various concentrations. (E) SPR tests of the binding between Antimycin A and VDAC3. With the VDAC3 concentration fixed at 10 μg/mL, the association and dissociation rates of Antimycin A binding to VDAC3 were measured at various concentrations. (F) Molecular docking of Antimycin A, DHODH, and VDAC3. (G) Immunofluorescence analysis of the co-localization of VDAC3-Flag and DHODH-HA in Vero-E6 cells under three conditions: normal cells, cells infected with BHV-1 (MOI = 0.5), and cells infected with BHV-1 (MOI = 0.5) treated with 20 nM Antimycin A. (H) Co-immunoprecipitation analysis of the interaction between VDAC3-Flag and DHODH-HA in MDBK cells under the same conditions.
Techniques Used: Infection, In Vitro, Purification, Binding Assay, Concentration Assay, Immunofluorescence, Immunoprecipitation
Figure Legend Snippet: Antimycin A inhibits PRV proliferation in vivo . (A) The flow diagram of the mice animal experiment. (B) Survival rate calculation and survival curve plotting used the Kaplan–Meier method. (C) Histopathological lesions of brain, lung and spleen from PRV-, PRV + Antimycin A- and mock-inoculated mice. The brain, lung and spleen were collected at 72 hpi and stained with hematoxylin and eosin. (D) The organs were collected at 72 hpi, and the viral DNA copies were detected by qPCR. Mean values ± SDs are shown (n = 3). Significance was assessed with two-tailed and unpaired Student's t -test, ***p < 0.001, **p < 0.01, *p < 0.05, ns = no significant. (E) The organs were collected from surviving mice inoculated with PRV and Antimycin A, and the viral DNA copies were detected by qPCR. Mean values ± SDs are shown (n = 3). Significance was assessed with two-tailed and unpaired Student's t -test, ns = no significant. (F) The organs were collected from died mice. The groups include two mice inoculated with PRV, two mice inoculated with PRV and 1 mg/kg Antimycin A, and one mouse inoculated with PRV, and 0.2 mg/kg Antimycin A. Viral DNA copies were detected by qPCR. Significance was assessed with two-tailed and unpaired Student's t -test, ****p < 0.0001, ns = no significant.
Techniques Used: In Vivo, Staining, Two Tailed Test
Figure Legend Snippet: Model illustrating the mechanism by which Antimycin A inhibits alpha- herpesviruses infection. Upon alpha-herpesvirus infection, cells form pyrimidinosomes—specialized complexes that meet the heightened demand for pyrimidine nucleotides essential for viral DNA replication. These structures comprise key enzymes of the de novo pyrimidine synthesis pathway, including cytosolic glutamate oxaloacetate transaminase 1 (GOT1), carbamoyl-phosphate synthetase (CAD), and uridine monophosphate synthetase (UMPS), which associate with dihydroorotate dehydrogenase (DHODH) via the mitochondrial outer membrane protein voltage-dependent anion-selective channel protein 3 (VDAC3). Antimycin A disrupts this process by inhibiting the DHODH-VDAC3 interaction, critical for functional pyrimidinosome assembly. This disruption limits the production of pyrimidine nucleotides, such as UTP, thereby hindering viral replication.
Techniques Used: Infection, Membrane, Functional Assay, Disruption