epiglucan and Dengue

epiglucan has been researched along with Dengue* in 4 studies

Other Studies

4 other study(ies) available for epiglucan and Dengue

ArticleYear
Sulfated β-glucan from Agaricus subrufescens inhibits flavivirus infection and nonstructural protein 1-mediated pathogenesis.
    Antiviral research, 2022, Volume: 203

    Topics: Agaricus; Animals; Antibodies, Viral; beta-Glucans; Dengue; Dengue Virus; Endothelial Cells; Mice; Mice, Inbred C57BL; Sulfates; Viral Nonstructural Proteins; Zika Virus; Zika Virus Infection

2022
Abnormal Blood Bacteriome, Gut Dysbiosis, and Progression to Severe Dengue Disease.
    Frontiers in cellular and infection microbiology, 2022, Volume: 12

    Topics: beta-Glucans; Dengue; Dysbiosis; Endotoxemia; Humans; Lipopolysaccharides; Severe Dengue

2022
Chemically sulfated natural galactomannans with specific antiviral and anticoagulant activities.
    International journal of biological macromolecules, 2016, Volume: 89

    Naturally occurring galactomannans were sulfated to give sulfated galactomannans with degrees of substitution of 0.7-1.4 per sugar unit and molecular weights of M¯n=0.6×10(4)-2.4×10(4). Sulfated galactomannans were found to have specific biological activities in vitro such as anticoagulant, anti-HIV and anti-Dengue virus activities. The biological activities were compared with those of standard dextran and curdlan sulfates, which are polysaccharides with potent antiviral activity and low cytotoxicity. It was found that sulfated galactomannans had moderate to high anticoagulant activity, 13.4-36.6unit/mg, compared to that of dextran and curdlan sulfates, 22.7 and 10.0unit/mg, and high anti-HIV and anti-Dengue virus activities, 0.04-0.8μg/mL and 0.2-1.1μg/mL, compared to those curdlan sulfates, 0.1μg/mL, respectively. The cytotoxicity on MT-4 and LCC-MK2 cells was low. Surface plasmon resonance (SPR) of sulfated galactomannans revealed strong interaction with poly-l-lysine as a model compound of virus proteins, and suggested that the specific biological activities might originate in the electrostatic interaction of negatively charged sulfate groups of sulfated galactomannans and positively charged amino groups of surface proteins of viruses. These results suggest that sulfated galactomannans effectively prevented the infection of cells by viruses and the degree of substitution and molecular weights played important roles in the biological activities.

    Topics: Anticoagulants; Antiviral Agents; beta-Glucans; Dengue; Dengue Virus; Galactose; HIV; HIV Infections; Humans; Mannans; Polylysine; Sulfates

2016
Sulfated polysaccharide, curdlan sulfate, efficiently prevents entry/fusion and restricts antibody-dependent enhancement of dengue virus infection in vitro: a possible candidate for clinical application.
    PLoS neglected tropical diseases, 2013, Volume: 7, Issue:4

    Curdlan sulfate (CRDS), a sulfated 1→3-β-D glucan, previously shown to be a potent HIV entry inhibitor, is characterized in this study as a potent inhibitor of the Dengue virus (DENV). CRDS was identified by in silico blind docking studies to exhibit binding potential to the envelope (E) protein of the DENV. CRDS was shown to inhibit the DENV replication very efficiently in different cells in vitro. Minimal effective concentration of CRDS was as low as 0.1 µg/mL in LLC-MK2 cells, and toxicity was observed only at concentrations over 10 mg/mL. CRDS can also inhibit DENV-1, 3, and 4 efficiently. CRDS did not inhibit the replication of DENV subgenomic replicon. Time of addition experiments demonstrated that the compound not only inhibited viral infection at the host cell binding step, but also at an early post-attachment step of entry (membrane fusion). The direct binding of CRDS to DENV was suggested by an evident reduction in the viral titers after interaction of the virus with CRDS following an ultrafiltration device separation, as well as after virus adsorption to an alkyl CRDS-coated membrane filter. The electron microscopic features also showed that CRDS interacted directly with the viral envelope, and caused changes to the viral surface. CRDS also potently inhibited DENV infection in DC-SIGN expressing cells as well as the antibody-dependent enhancement of DENV-2 infection. Based on these data, a probable binding model of CRDS to DENV E protein was constructed by a flexible receptor and ligand docking study. The binding site of CRDS was predicted to be at the interface between domains II and III of E protein dimer, which is unique to this compound, and is apparently different from the β-OG binding site. Since CRDS has already been tested in humans without serious side effects, its clinical application can be considered.

    Topics: Animals; Antibody-Dependent Enhancement; beta-Glucans; Cell Line; Dengue; Dengue Virus; Macaca mulatta; Microscopy, Electron; Virus Replication

2013