Exposure to bacterial endotoxin generates a distinct strain of α-synuclein fibril View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-11

AUTHORS

Changyoun Kim, Guohua Lv, Jun Sung Lee, Byung Chul Jung, Masami Masuda-Suzukake, Chul-Suk Hong, Elvira Valera, He-Jin Lee, Seung R Paik, Masato Hasegawa, Eliezer Masliah, David Eliezer, Seung-Jae Lee

ABSTRACT

A single amyloidogenic protein is implicated in multiple neurological diseases and capable of generating a number of aggregate "strains" with distinct structures. Among the amyloidogenic proteins, α-synuclein generates multiple patterns of proteinopathies in a group of diseases, such as Parkinson disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). However, the link between specific conformations and distinct pathologies, the key concept of the strain hypothesis, remains elusive. Here we show that in the presence of bacterial endotoxin, lipopolysaccharide (LPS), α-synuclein generated a self-renewable, structurally distinct fibril strain that consistently induced specific patterns of synucleinopathies in mice. These results suggest that amyloid fibrils with self-renewable structures cause distinct types of proteinopathies despite the identical primary structure and that exposure to exogenous pathogens may contribute to the diversity of synucleinopathies. More... »

PAGES

30891

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep30891

DOI

http://dx.doi.org/10.1038/srep30891

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009917413

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27488222


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