ArticleNature chemical biology2013
Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Targets for the diagnosis ofmSphere · 2025Article
- Novel anti-Frontiers in cellular and infection microbiology · 2024Article
- War of the microbial world: Acanthamoeba spp. interactions with microorganisms.Folia microbiologica · 2021Review
- Two VHH Antibodies Neutralize Botulinum Neurotoxin E1 by Blocking Its Membrane Translocation in Host Cells.Toxins · 2020Article
- Flowering Poration-A Synergistic Multi-Mode Antibacterial Mechanism by a Bacteriocin Fold.iScience · 2020Article
- Production and Functional Characterization of a Recombinant Predicted Pore-Forming Protein (TVSAPLIP12) ofFrontiers in cellular and infection microbiology · 2020Article
- Review
- The many lives of nontuberculous mycobacteria.Journal of bacteriology · 2018Article
- Environmental adaptation ofInternational journal of biological sciences · 2018Article
- Article
- pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Novel hemagglutinating, hemolytic and cytotoxic activities of the intermediate subunit of Entamoeba histolytica lectin.Scientific reports · 2015Article
- Superdiffusion dominates intracellular particle motion in the supercrowded cytoplasm of pathogenic Acanthamoeba castellanii.Scientific reports · 2015Article
- Cytotoxic activity and degradation patterns of structural proteins by corneal isolates of Acanthamoeba spp.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2015Article
- An update on Acanthamoeba keratitis: diagnosis, pathogenesis and treatment.Parasite (Paris, France) · 2015Review
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Authors and funding
16 authors.
Funding
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Abstract
Human pathogens often produce soluble protein toxins that generate pores inside membranes, resulting in the death of target cells and tissue damage. In pathogenic amoebae, this has been exemplified with amoebapores of the enteric protozoan parasite Entamoeba histolytica. Here we characterize acanthaporin, to our knowledge the first pore-forming toxin to be described from acanthamoebae, which are free-living, bacteria-feeding, unicellular organisms that are opportunistic pathogens of increasing importance and cause severe and often fatal diseases. We isolated acanthaporin from extracts of virulent Acanthamoeba culbertsoni by tracking its pore-forming activity, molecularly cloned the gene of its precursor and recombinantly expressed the mature protein in bacteria. Acanthaporin was cytotoxic for human neuronal cells and exerted antimicrobial activity against a variety of bacterial strains by permeabilizing their membranes. The tertiary structures of acanthaporin's active monomeric form and inactive dimeric form, both solved by NMR spectroscopy, revealed a currently unknown protein fold and a pH-dependent trigger mechanism of activation.
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