Medical Activities of Aesculus hippocastaneum (Horse-Chestnut) Saponins

Dworschák, E.; Antal, M.; Biró, Lajos; Regöly-Mérei, Andrea; Nagy, Katalin; Szépvölgyi, J.; Gaál, Ö.; Bíró, G.

doi:10.1007/978-1-4899-1367-8_37

Cited by 6 publications

(2 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These primers amplified a 263 bp product in an empty vector, while they produce a product of 1747 bp in the recombinant clones (additional 1484 bp represents the cloned fragment containing tig of 1284 bp). The recombinant plasmid was purified using a commercial kit (Qiagen) and an aliquot was transformed into WU2Δ tig Erm , as described previously 75 , to produce the complemented strain WU2Δ tig tig /Erm/Kan . The transformants were selected on blood agar plates supplemented with erythromycin (125 μg/ml) and kanamycin (500 μg/ml).…”

Section: Methodsmentioning

confidence: 99%

Streptococcus pneumoniae Cell Wall-Localized Trigger Factor Elicits a Protective Immune Response and Contributes to Bacterial Adhesion to the Host

Cohen

Troib

Dotan³

et al. 2019

Sci Rep

View full text Add to dashboard Cite

Trigger factor (TF) has a known cytoplasmic function as a chaperone. In a previous study we showed that pneumococcal TF is also cell-wall localized and this finding combined with the immunogenic characteristic of TF, has led us to determine the vaccine potential of TF and decipher its involvement in pneumococcal pathogenesis. Bioinformatic analysis revealed that TF is conserved among pneumococci and has no human homologue. Immunization of mice with recombinant (r)TF elicited a protective immune response against a pneumococcal challenge, suggesting that TF contributes to pneumococcal pathogenesis. Indeed, rTF and an anti-rTF antiserum inhibited bacterial adhesion to human lung derived epithelial cells, indicating that TF contributes to the bacterial adhesion to the host. Moreover, bacteria lacking TF demonstrated reduced adhesion, in vitro, to lung-derived epithelial cells, neural cells and glial cells. The reduced adhesion could be restored by chromosomal complementation. Furthermore, bacteria lacking TF demonstrated significantly reduced virulence in a mouse model. Taken together, the ability of rTF to elicit a protective immune response, involvement of TF in bacterial adhesion, conservation of the protein among pneumococcal strains and the lack of human homologue, all suggest that rTF can be considered as a future candidate vaccine with a much broader coverage as compared to the currently available pneumococcal vaccines.

show abstract

Section: Methodsmentioning

confidence: 99%

Streptococcus pneumoniae Cell Wall-Localized Trigger Factor Elicits a Protective Immune Response and Contributes to Bacterial Adhesion to the Host

Cohen

Troib

Dotan³

et al. 2019

Sci Rep

View full text Add to dashboard Cite

show abstract

“…These primers amplified 263 bp product in empty vector, while they produce a product of 913 bp in the recombinant clones (additional 650 bp represents the cloned fragment containing flaR ). The recombinant plasmid was purified using a commercial kit (Qiagen), and an aliquot was transformed into WU2Δ flaR Erm as described previously 89 to produce the complemented strain WU2Δ flaR flaR /Erm/Kan chromosome. The transformants were selected on blood agar plates supplemented with erythromycin (125 μg/ml) and kanamycin (500 μg/ml).…”

Section: Methodsmentioning

confidence: 99%

Flavin Reductase Contributes to Pneumococcal Virulence by Protecting from Oxidative Stress and Mediating Adhesion and Elicits Protection Against Pneumococcal Challenge

Morozov

Porat

Kushnir

et al. 2018

Sci Rep

View full text Add to dashboard Cite

Pneumococcal flavin reductase (FlaR) is known to be cell-wall associated and possess age dependent antigenicity in children. This study aimed at characterizing FlaR and elucidating its involvement in pneumococcal physiology and virulence. Bioinformatic analysis of FlaR sequence identified three-conserved cysteine residues, suggesting a transition metal-binding capacity. Recombinant FlaR (rFlaR) bound Fe2+ and exhibited FAD-dependent NADP-reductase activity, which increased in the presence of cysteine or excess Fe2+ and inhibited by divalent-chelating agents. flaR mutant was highly susceptible to H2O2 compared to its wild type (WT) and complemented strains, suggesting a role for FlaR in pneumococcal oxidative stress resistance. Additionally, flaR mutant demonstrated significantly decreased mice mortality following intraperitoneal infection. Interestingly, lack of FlaR did not affect the extent of phagocytosis by primary mouse peritoneal macrophages but reduced adhesion to A549 cells compared to the WT and complemented strains. Noteworthy are the findings that immunization with rFlaR elicited protection in mice against intraperitoneal lethal challenge and anti-FlaR antisera neutralized bacterial virulence. Taken together, FlaR’s roles in pneumococcal physiology and virulence, combined with its lack of significant homology to human proteins, point towards rFlaR as a vaccine candidate.

show abstract

Buckeye ( Aesculus Species)

Barceloux

2008

Medical Toxicology of Natural Substances

View full text Add to dashboard Cite

Medical Activities of Aesculus hippocastaneum (Horse-Chestnut) Saponins

Cited by 6 publications

References 3 publications

Streptococcus pneumoniae Cell Wall-Localized Trigger Factor Elicits a Protective Immune Response and Contributes to Bacterial Adhesion to the Host

Streptococcus pneumoniae Cell Wall-Localized Trigger Factor Elicits a Protective Immune Response and Contributes to Bacterial Adhesion to the Host

Flavin Reductase Contributes to Pneumococcal Virulence by Protecting from Oxidative Stress and Mediating Adhesion and Elicits Protection Against Pneumococcal Challenge

Buckeye ( Aesculus Species)

Contact Info

Product

Resources

About