ArticleThe Journal of biological chemistry2012
Microcin amyloid fibrils A are reservoir of toxic oligomeric species.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 70 citations in OpenAlex.
- Antibacterial microcins self-assemble to promote biofilm formation in Acinetobacter baumannii.Cell reports · 2026Article
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation.NPJ biofilms and microbiomes · 2023Article
- Natural Antimicrobials forMicroorganisms · 2023Review
- Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Review
- Microbiome Impact on Amyloidogenesis.Frontiers in molecular biosciences · 2022Review
- Application of Natural Preservatives for Meat and Meat Products against Food-Borne Pathogens and Spoilage Bacteria: A Review.Foods (Basel, Switzerland) · 2021Review
- Purification, characterization, and mode of action of Paracin 54, a novel bacteriocin against Staphylococci.Applied microbiology and biotechnology · 2021Article
- Aging, Frailty, and the Microbiome-How Dysbiosis Influences Human Aging and Disease.Gastroenterology · 2021Article
- Multifunctional Amyloids in the Biology of Gram-Positive Bacteria.Microorganisms · 2020Review
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- The manifold roles of microbial ribosomal peptide-based natural products in physiology and ecology.The Journal of biological chemistry · 2020Review
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.Biophysical reviews · 2019Review
- Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species.Scientific reports · 2019Article
- The Role of Functional Amyloids in Bacterial Virulence.Journal of molecular biology · 2018Review
- Iron Dysregulation and Dormant Microbes as Causative Agents for Impaired Blood Rheology and Pathological Clotting in Alzheimer's Type Dementia.Frontiers in neuroscience · 2018Review
- M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils.PloS one · 2018Article
- Molecular interaction between type 2 diabetes and Alzheimer's disease through cross-seeding of protein misfolding.Molecular psychiatry · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microcin E492 (Mcc), a low molecular weight bacteriocin produced by Klebsiella pneumoniae RYC492, has been shown to exist in two forms: soluble forms that are believed to be toxic to the bacterial cell by forming pores and non-toxic fibrillar forms that share similar biochemical and biophysical properties with amyloids associated with several human diseases. Here we report that fibrils polymerized in vitro from soluble forms sequester toxic species that can be released upon changing environmental conditions such as pH, ionic strength, and upon dilution. Our results indicate that basic pH (≥8.5), low NaCl concentrations (≤50 mm), and dilution (>10-fold) destabilize Mcc fibrils into more soluble species that are found to be toxic to the target cells. Additionally, we also found a similar conversion of non-toxic fibrils into highly toxic oligomers using Mcc aggregates produced in vivo. Moreover, the soluble protein released from fibrils is able to rapidly polymerize into amyloid fibrils under fibril-forming conditions and to efficiently seed aggregation of monomeric Mcc. Our findings indicate that fibrillar forms of Mcc constitute a reservoir of toxic oligomeric species that is released into the medium upon changing the environmental conditions. These findings may have substantial implications to understand the dynamic process of interconversion between toxic and non-toxic aggregated species implicated in protein misfolding diseases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.