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In the present study, we investigated the ability of different \u03b1-syn aggregates to trigger inflammatory responses. We showed that \u03b1-syn induced inflammation through activation of Toll-like receptor 2 (TLR2) and the nucleotide oligomerization domain-like receptor pyrin domain containing 3 (NLRP3) inflammasome only when folded as amyloid fibrils. Oligomeric species, thought to be the primary species responsible for the disease, were surprisingly unable to trigger the same cascades. As neuroinflammation is a key player in PD pathology, these results put fibrils back to the fore and rekindles discussions about the primary toxic species contributing to the disease. Our data also suggest that the inflammatory properties of \u03b1-syn fibrils are linked to their intrinsic structure, most probably to their cross-\u03b2 structure. Since fibrils of other amyloids induce similar immunological responses, we propose that the canonical fibril-specific cross-\u03b2 structure represents a new generic motif recognized by the innate immune system.<\/jats:p>","DOI":"10.1042\/bj20150617","type":"journal-article","created":{"date-parts":[[2015,8,14]],"date-time":"2015-08-14T02:44:19Z","timestamp":1439520259000},"page":"323-333","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":177,"title":["Amyloid fibrils are the molecular trigger of inflammation in Parkinson's disease"],"prefix":"10.1042","volume":"471","author":[{"given":"Adelin","family":"Gustot","sequence":"first","affiliation":[{"name":"Laboratory of Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, Brussels 1050, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9\u00a0Ignacio","family":"Gallea","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica Biol\u00f3gica, Centro de Investigaciones en Qu\u00edmica Biol\u00f3gica de C\u00f3rdoba (CIQUIBIC, CONICET), Facultad de Ciencias Qu\u00edmicas, Universidad Nacional de C\u00f3rdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria, X5000HUA C\u00f3rdoba, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rabia","family":"Sarroukh","sequence":"additional","affiliation":[{"name":"Laboratory of Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, Brussels 1050, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mar\u00eda\u00a0Soledad","family":"Celej","sequence":"additional","affiliation":[{"name":"Departamento de Qu\u00edmica Biol\u00f3gica, Centro de Investigaciones en Qu\u00edmica Biol\u00f3gica de C\u00f3rdoba (CIQUIBIC, CONICET), Facultad de Ciencias Qu\u00edmicas, Universidad Nacional de C\u00f3rdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria, X5000HUA C\u00f3rdoba, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marie","family":"Ruysschaert","sequence":"additional","affiliation":[{"name":"Laboratory of Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, Brussels 1050, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent","family":"Raussens","sequence":"additional","affiliation":[{"name":"Laboratory of Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, Brussels 1050, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2015,10,16]]},"reference":[{"key":"2021112216233532600_B1","doi-asserted-by":"publisher","first-page":"889","DOI":"10.1016\/S0896-6273(03)00568-3","article-title":"Parkinson's disease: mechanisms and models","volume":"39","author":"Dauer","year":"2003","journal-title":"Neuron"},{"key":"2021112216233532600_B2","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. 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