ArticleInternational journal for parasitology. Drugs and drug resistance2017
Disulfiram as a novel inactivator of Giardia lamblia triosephosphate isomerase with antigiardial potential.
Article in International journal for parasitology. Drugs and drug resistance, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Off-label and repurposed use of disulfiram beyond alcohol dependence: A systematic review of clinical and preclinical evidence.iScience · 2026Article
- Trichomonas vaginalis Drug Targets and Their Role in Drug Discovery and Development.Pharmaceutical research · 2026Review
- Disulfiram induces redox imbalance and perturbations in central glucose catabolism and metal homeostasis to inhibit the growth of Staphylococcus aureus.Scientific reports · 2025Article
- Anti-alcoholism drug disulfiram inhibits PANoptosis by blocking mitochondrial permeabilization in macrophages.Frontiers in immunology · 2025Article
- Exploration of innovative drug repurposing strategies for combating human protozoan diseases: Advances, challenges, and opportunities.Journal of pharmaceutical analysis · 2025Review
- Repurposing FDA-approved disulfiram for targeted inhibition of diphtheria toxin and the binary protein toxins ofFrontiers in pharmacology · 2024Article
- Unveiling the flames: macrophage pyroptosis and its crucial role in liver diseases.Frontiers in immunology · 2024Review
- Repurposing Terfenadine as a Novel Antigiardial Compound.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Ultrastructural Alterations of the Human PathogenPathogens (Basel, Switzerland) · 2023Review
- Disulfiram, an aldehyde dehydrogenase inhibitor, works as a potent drug against sepsis and cancer via NETosis, pyroptosis, apoptosis, ferroptosis, and cuproptosis.Blood science (Baltimore, Md.) · 2022Review
- Disulfiram: A Repurposed Drug in Preclinical and Clinical Development for the Treatment of Infectious Diseases.Anti-infective agents · 2022Article
- An Overview of Mucosa-Associated Protozoa: Challenges in Chemotherapy and Future Perspectives.Frontiers in cellular and infection microbiology · 2022Review
- Drug Repurposing of the Alcohol Abuse Medication Disulfiram as an Anti-Parasitic Agent.Frontiers in cellular and infection microbiology · 2021Article
- FDA-approved disulfiram inhibits pyroptosis by blocking gasdermin D pore formation.Nature immunology · 2020Article
- Crystal structures of Triosephosphate Isomerases from Taenia solium and Schistosoma mansoni provide insights for vaccine rationale and drug design against helminth parasites.PLoS neglected tropical diseases · 2020Article
- Recent Advances in the Discovery of Novel Antiprotozoal Agents.Molecules (Basel, Switzerland) · 2019Review
- Structure-based identification of a potential non-catalytic binding site for rational drug design in the fructose 1,6-biphosphate aldolase from Giardia lamblia.Scientific reports · 2019Article
- Gasdermin D (GSDMD) as a new target for the treatment of infection.MedChemComm · 2019Review
- Treatment-refractory giardiasis: challenges and solutions.Infection and drug resistance · 2018Review
- Effects of Cytokines IFN-γ and TGF-β on the Functional Activity of Blood Mononuclear Cells againstIranian journal of parasitologyArticle
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8 authors.
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Abstract
Giardiasis, the infestation of the intestinal tract by Giardia lamblia, is one of the most prevalent parasitosis worldwide. Even though effective therapies exist for it, the problems associated with its use indicate that new therapeutic options are needed. It has been shown that disulfiram eradicates trophozoites in vitro and is effective in vivo in a murine model of giardiasis; disulfiram inactivation of carbamate kinase by chemical modification of an active site cysteine has been proposed as the drug mechanism of action. The triosephosphate isomerase from G. lamblia (GlTIM) has been proposed as a plausible target for the development of novel antigiardial pharmacotherapies, and chemical modification of its cysteine 222 (C222) by thiol-reactive compounds is evidenced to inactivate the enzyme. Since disulfiram is a cysteine modifying agent and GlTIM can be inactivated by modification of C222, in this work we tested the effect of disulfiram over the recombinant and trophozoite-endogenous GlTIM. The results show that disulfiram inactivates GlTIM by modification of its C222. The inactivation is species-specific since disulfiram does not affect the human homologue enzyme. Disulfiram inactivation induces only minor conformational changes in the enzyme, but substantially decreases its stability. Recombinant and endogenous GlTIM inactivates similarly, indicating that the recombinant protein resembles the natural enzyme. Disulfiram induces loss of trophozoites viability and inactivation of intracellular GlTIM at similar rates, suggesting that both processes may be related. It is plausible that the giardicidal effect of disulfiram involves the inactivation of more than a single enzyme, thus increasing its potential for repurposing it as an antigiardial drug.
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