. Amyloid polymorphisms constitute distinct clouds of conformational variants in different etiological subtypes of Alzheimer's disease. Proc Natl Acad Sci U S A. 2017 Dec 5;114(49):13018-13023. Epub 2017 Nov 20 PubMed.


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  1. I read with interest the intriguing finding of "distinct clouds of conformational variants" of amyloid, as reported by Rasmussen et al. This work adds to the concept that there are distinct strains of amyloid conformations that may be responsible for varying disease phenotypes in neurodegenerative disorders. The biological basis of these unique fibril structures may involve the microbiota. My coworkers and I have proposed that distinctive fibril structures of Aβ and related molecules may be caused by cross-seeding with amyloids produced by bacteria and fungi residing in the mouth, nose, and intestines (Friedland, 2015; Chen et al., 2016). Our microbiota are known to include many organisms that produce functional amyloid proteins, and cross-seeding of amyloid misfolding has been documented. The microbiota constitute our largest environmental exposure, and their potential role in AD and related disorders is worth consideration. 


    . Mechanisms of molecular mimicry involving the microbiota in neurodegeneration. J Alzheimers Dis. 2015;45(2):349-62. PubMed.

    . Exposure to the Functional Bacterial Amyloid Protein Curli Enhances Alpha-Synuclein Aggregation in Aged Fischer 344 Rats and Caenorhabditis elegans. Sci Rep. 2016 Oct 6;6:34477. PubMed.

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  1. Paper Alert: Aβ Fibril Structures Vary by AD Subtype