ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 79 citations in OpenAlex.
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- Ribosomal RNA Modulates Aggregation of theInternational journal of molecular sciences · 2020Article
- Full atomistic model of prion structure and conversion.PLoS pathogens · 2019Article
- Review
- Comparing the Folds of Prions and Other Pathogenic Amyloids.Pathogens (Basel, Switzerland) · 2018Review
- The Structure of PrPPathogens (Basel, Switzerland) · 2018Review
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Elucidating the structure of an infectious protein.PLoS pathogens · 2017Review
- Mapping the Broad Structural and Mechanical Properties of Amyloid Fibrils.Biophysical journal · 2017Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- The HET-S/s Prion Motif in the Control of Programmed Cell Death.Cold Spring Harbor perspectives in biology · 2016Review
- The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy.PLoS pathogens · 2016Article
- Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- α-Synuclein Amyloid Fibrils with Two Entwined, Asymmetrically Associated Protofibrils.The Journal of biological chemistry · 2016Article
- Rapid Filament Supramolecular Chirality Reversal of HET-s (218-289) Prion Fibrils Driven by pH Elevation.The journal of physical chemistry. B · 2015Article
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.PLoS pathogens · 2014Article
- Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.Biochemistry · 2014Article
- Is supramolecular filament chirality the underlying cause of major morphology differences in amyloid fibrils?Journal of the American Chemical Society · 2014Article
- Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.Journal of the American Chemical Society · 2013Article
- Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289).The Journal of biological chemistry · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
HET-s is a prion protein of the fungus Podospora anserina which, in the prion state, is active in a self/nonself recognition process called heterokaryon incompatibility. Its prionogenic properties reside in the C-terminal "prion domain." The HET-s prion domain polymerizes in vitro into amyloid fibrils whose properties depend on the pH of assembly; above pH 3, infectious singlet fibrils are produced, and below pH 3, noninfectious triplet fibrils. To investigate the correlation between structure and infectivity, we performed cryo-EM analyses. Singlet fibrils have a helical pitch of approximately 410 Å and a left-handed twist. Triplet fibrils have three protofibrils whose lateral dimensions (36 × 25 Å) and axial packing (one subunit per 9.4 Å) match those of singlets but differ in their supercoiling. At 8.5-Å resolution, the cross-section of the singlet fibril reconstruction is largely consistent with that of a β-solenoid model previously determined by solid-state NMR. Reconstructions of the triplet fibrils show three protofibrils coiling around a common axis and packed less tightly at pH 3 than at pH 2, eventually peeling off. Taken together with the earlier observation that fragmentation of triplet fibrils by sonication does not increase infectivity, these observations suggest a novel mechanism for self-propagation, whereby daughter fibrils nucleate on the lateral surface of singlet fibrils. In triplets, this surface is occluded, blocking nucleation and thereby explaining their lack of infectivity.
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