AA amyloid in human food chain is a possible biohazard

AA amyloidosis can be transmitted experimentally in several mammalian and avian species as well as spontaneously between captive animals, even by oral intake of amyloid seeds. Amyloid seeding can cross species boundaries, and fibrils of one kind of amyloid protein may also seed other types. Here we...

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Detalles Bibliográficos
Autores principales: Rising, Anna, Gherardi, Paola, Chen, Gefei, Johansson, Jan, Oskarsson, Marie E., Westermark, Gunilla T., Westermark, Per
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8548551/
https://www.ncbi.nlm.nih.gov/pubmed/34702933
http://dx.doi.org/10.1038/s41598-021-00588-w
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author Rising, Anna
Gherardi, Paola
Chen, Gefei
Johansson, Jan
Oskarsson, Marie E.
Westermark, Gunilla T.
Westermark, Per
author_facet Rising, Anna
Gherardi, Paola
Chen, Gefei
Johansson, Jan
Oskarsson, Marie E.
Westermark, Gunilla T.
Westermark, Per
author_sort Rising, Anna
collection PubMed
description AA amyloidosis can be transmitted experimentally in several mammalian and avian species as well as spontaneously between captive animals, even by oral intake of amyloid seeds. Amyloid seeding can cross species boundaries, and fibrils of one kind of amyloid protein may also seed other types. Here we show that meat from Swedish and Italian cattle for consumption by humans often contains AA amyloid and that bovine AA fibrils efficiently cross-seed human amyloid β peptide, associated with Alzheimer’s disease.
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spelling pubmed-85485512021-10-28 AA amyloid in human food chain is a possible biohazard Rising, Anna Gherardi, Paola Chen, Gefei Johansson, Jan Oskarsson, Marie E. Westermark, Gunilla T. Westermark, Per Sci Rep Article AA amyloidosis can be transmitted experimentally in several mammalian and avian species as well as spontaneously between captive animals, even by oral intake of amyloid seeds. Amyloid seeding can cross species boundaries, and fibrils of one kind of amyloid protein may also seed other types. Here we show that meat from Swedish and Italian cattle for consumption by humans often contains AA amyloid and that bovine AA fibrils efficiently cross-seed human amyloid β peptide, associated with Alzheimer’s disease. Nature Publishing Group UK 2021-10-26 /pmc/articles/PMC8548551/ /pubmed/34702933 http://dx.doi.org/10.1038/s41598-021-00588-w Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Rising, Anna
Gherardi, Paola
Chen, Gefei
Johansson, Jan
Oskarsson, Marie E.
Westermark, Gunilla T.
Westermark, Per
AA amyloid in human food chain is a possible biohazard
title AA amyloid in human food chain is a possible biohazard
title_full AA amyloid in human food chain is a possible biohazard
title_fullStr AA amyloid in human food chain is a possible biohazard
title_full_unstemmed AA amyloid in human food chain is a possible biohazard
title_short AA amyloid in human food chain is a possible biohazard
title_sort aa amyloid in human food chain is a possible biohazard
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8548551/
https://www.ncbi.nlm.nih.gov/pubmed/34702933
http://dx.doi.org/10.1038/s41598-021-00588-w
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