期刊
FRONTIERS IN MOLECULAR NEUROSCIENCE
卷 14, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fnmol.2021.670513
关键词
prion structure; amyloid fibril; solid-state NMR; functional amyloids; structural biology
资金
- European Research Council (ERC) under the European Union [639020]
- ANR [ANR-17-CE11-0035, ANR16-CE11-0020-01]
- INCEPTION project [PIA/ANR-16-CONV-0005]
- Nouvelle Aquitaine Regional Council
- Swiss National Science Foundation [P2EZP2_184258]
- Swiss National Science Foundation (SNF) [P2EZP2_184258] Funding Source: Swiss National Science Foundation (SNF)
- Agence Nationale de la Recherche (ANR) [ANR-17-CE11-0035] Funding Source: Agence Nationale de la Recherche (ANR)
This article explores the structures of pathological and functional amyloids, discussing the obtained structural models through techniques such as solid-state NMR. The review concludes with a perspective on integrative approaches to structurally explore various aspects of prion biology.
Infectious proteins or prions are a remarkable class of pathogens, where pathogenicity and infectious state correspond to conformational transition of a protein fold. The conformational change translates into the formation by the protein of insoluble amyloid aggregates, associated in humans with various neurodegenerative disorders and systemic protein-deposition diseases. The prion principle, however, is not limited to pathogenicity. While pathological amyloids (and prions) emerge from protein misfolding, a class of functional amyloids has been defined, consisting of amyloid-forming domains under natural selection and with diverse biological roles. Although of great importance, prion amyloid structures remain challenging for conventional structural biology techniques. Solid-state nuclear magnetic resonance (SSNMR) has been preferentially used to investigate these insoluble, morphologically heterogeneous aggregates with poor crystallinity. SSNMR methods have yielded a wealth of knowledge regarding the fundamentals of prion biology and have helped to solve the structures of several prion and prion-like fibrils. Here, we will review pathological and functional amyloid structures and will discuss some of the obtained structural models. We will finish the review with a perspective on integrative approaches combining solid-state NMR, electron paramagnetic resonance and cryo-electron microscopy, which can complement and extend our toolkit to structurally explore various facets of prion biology.
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