Modulation of host HIF-1α activity and the tryptophan pathway contributes to the anti-Toxoplasma gondii potential of nanoparticles

Adeyemi, O. S. and Murata, Yuho and Sugi, Tatsuki and Han, Yongmei and Kato, Kentaro (2017) Modulation of host HIF-1α activity and the tryptophan pathway contributes to the anti-Toxoplasma gondii potential of nanoparticles. Biochemistry and Biophysics Reports, 11. pp. 84-92. ISSN 2405-5808

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Abstract

Toxoplasmosis constitutes a large global burden that is further exacerbated by the shortcomings of available therapeutic options, thus underscoring the urgent need for better anti-Toxoplasma gondii therapy or strategies. Recently, we showed that the anti-parasitic action of inorganic nanoparticles (NPs) could, in part, be due to changes in redox status as well as in the parasite mitochondrial membrane potential. Methods: In the present study, we explored the in vitro mode of action of the anti-T. gondii effect of NPs by evaluating the contributions of host cellular processes, including the tryptophan pathway and hypoxia-inducing factor activity. NPs, at concentrations ranging from 0.01 to 200 µg/ml were screened for anti-parasitic activity. Sulfadiazine and/or pyrimethamine served as positive controls. Results: We found that interplay among multiple host cellular processes, including HIF-1αactivity, indoleamine 2,3-dioxygenase activity,andto alargerextentthetryptophanpathway,contributeto theanti-parasitic actionof NPs. Conclusion: To our knowledge, this is the first study to demonstrate an effect of NPs on the tryptophan and/or kynurenine pathway. General significance: Our findings deepen our understanding of the mechanism of action of NPs and suggest that modulation of the host nutrient pool may represent a viable approach to the development of new and effective anti-parasitic agents

Item Type: Article
Subjects: Q Science > QD Chemistry
Depositing User: Mr DIGITAL CONTENT CREATOR LMU
Date Deposited: 26 Apr 2019 11:01
Last Modified: 26 Apr 2019 11:01
URI: https://eprints.lmu.edu.ng/id/eprint/2138

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