ArticleAntimicrobial agents and chemotherapy2014
Reduced antimony accumulation in ARM58-overexpressing Leishmania infantum.
Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Unlocking the power of AI models: exploring protein folding prediction through comparative analysis.Journal of integrative bioinformatics · 2024Article
- Antimony resistance and gene expression inParasitology · 2024Review
- Global distribution of treatment resistance gene markers for leishmaniasis.Journal of clinical laboratory analysis · 2022Review
- Health economic evaluation of moist wound care in chronic cutaneous leishmaniasis ulcers in Afghanistan.Infectious diseases of poverty · 2018Article
- Hsp90 inhibitors radicicol and geldanamycin have opposing effects on Leishmania Aha1-dependent proliferation.Cell stress & chaperones · 2017Article
- Biophysical and Pharmacological Characterization of Energy-Dependent Efflux of Sb in Laboratory-Selected Resistant Strains ofFrontiers in cell and developmental biology · 2017Article
- A Telomeric Cluster of Antimony Resistance Genes on Chromosome 34 of Leishmania infantum.Antimicrobial agents and chemotherapy · 2016Article
- A novel marker, ARM58, confers antimony resistance to Leishmania spp.International journal for parasitology. Drugs and drug resistance · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Antimony-based drugs are still the mainstay of chemotherapy against Leishmania infections in many countries where the parasites are endemic. The efficacy of antimonials has been compromised by increasing numbers of resistant infections, the basis of which is not fully understood and likely involves multiple factors. By using a functional cloning strategy, we recently identified a novel antimony resistance marker, ARM58, from the parasite Leishmania braziliensis that protects the parasites against antimony-based antileishmanial compounds. Here we show that the Leishmania infantum homologue also confers resistance against antimony but not against other antileishmanial drugs and that its function depends critically on one of four conserved domains of unknown function. This critical domain requires at least two hydrophobic amino acids and is predicted to form a transmembrane structure. Overexpression of ARM58 in antimony-exposed parasites reduces the intracellular Sb accumulation by over 70%, indicating a role for ARM58 in Sb extrusion pathways, but without involvement of energy-dependent transporter proteins.
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