ArticlePLoS neglected tropical diseases2016
Proteomic Identification of Oxidized Proteins in Entamoeba histolytica by Resin-Assisted Capture: Insights into the Role of Arginase in Resistance to Oxidative Stress.
Article in PLoS neglected tropical diseases, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
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- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Riluzole, a Derivative of Benzothiazole as a Potential Anti-Amoebic Agent againstPharmaceuticals (Basel, Switzerland) · 2023Article
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- Insights into the Mechanisms ofAntioxidants (Basel, Switzerland) · 2022Article
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- Proteomics Reveals Distinct Changes Associated with Increased Gamma Radiation Resistance in the Black YeastGenes · 2020Article
- Biological activity of esters of quinoxaline-7-carboxylate 1,4-di-N-oxide against E. histolytica and their analysis as potential thioredoxin reductase inhibitors.Parasitology research · 2020Article
- Revisiting Drug Development Against the Neglected Tropical Disease, Amebiasis.Frontiers in cellular and infection microbiology · 2020Review
- Escherichia coli mediated resistance of Entamoeba histolytica to oxidative stress is triggered by oxaloacetate.PLoS pathogens · 2018Article
- The Sole DNA Ligase inFrontiers in cellular and infection microbiology · 2018Article
- Utilization of Different Omic Approaches to Unravel Stress Response Mechanisms in the ParasiteFrontiers in cellular and infection microbiology · 2018Review
- Entamoeba histolytica under Oxidative Stress: What Countermeasure Mechanisms Are in Place?Cells · 2017Review
- Identification of S-Nitrosylated (SNO) Proteins inFrontiers in cellular and infection microbiology · 2017Article
- Phosphorylation of Eukaryotic Initiation Factor-2α during Stress and Encystation in Entamoeba Species.PLoS pathogens · 2016Article
- N-acetyl ornithine deacetylase is a moonlighting protein and is involved in the adaptation of Entamoeba histolytica to nitrosative stress.Scientific reports · 2016Article
- Proteome analysis of excretory-secretory proteins ofClinical proteomics · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entamoeba histolytica is an obligate protozoan parasite of humans, and amebiasis, an infectious disease which targets the intestine and/or liver, is the second most common cause of human death due to a protozoan after malaria. Although amebiasis is usually asymptomatic, E. histolytica has potent pathogenic potential. During host infection, the parasite is exposed to reactive oxygen species that are produced and released by cells of the innate immune system at the site of infection. The ability of the parasite to survive oxidative stress (OS) is essential for a successful invasion of the host. Although the effects of OS on the regulation of gene expression in E. histolytica and the characterization of some proteins whose function in the parasite's defense against OS have been previously studied, our knowledge of oxidized proteins in E. histolytica is lacking. In order to fill this knowledge gap, we performed a large-scale identification and quantification of the oxidized proteins in oxidatively stressed E. histolytica trophozoites using resin-assisted capture coupled to mass spectrometry. We detected 154 oxidized proteins (OXs) and the functions of some of these proteins were associated with antioxidant activity, maintaining the parasite's cytoskeleton, translation, catalysis, and transport. We also found that oxidation of the Gal/GalNAc impairs its function and contributes to the inhibition of E. histolytica adherence to host cells. We also provide evidence that arginase, an enzyme which converts L-arginine into L-ornithine and urea, is involved in the protection of the parasite against OS. Collectively, these results emphasize the importance of OS as a critical regulator of E. histolytica's functions and indicate a new role for arginase in E. histolytica's resistance to OS.
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