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

doi:10.1038/s41598-021-00588-w

Cited by 12 publications

(7 citation statements)

References 22 publications

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“…The findings of our current study suggest that Aβ aggregates present in the brains of old cattle are competent to seed amyloid deposition in vivo. This induction has also been observed with other protein aggregates such as AA amyloid (Rising et al, 2021). However, the potential transmission of Aβ cattlederived seeds to humans is unlikely, considering that repeated oral administration of AD brain extracts to susceptible mice failed to accelerate pathological features (Morales et al, 2021).…”

Section: Discussionmentioning

confidence: 63%

Aged Cattle Brain Displays Alzheimer's Disease-Like Pathology and Promotes Brain Amyloidosis in a Transgenic Animal Model

Moreno-González

Edwards

Morales

et al. 2022

Front. Aging Neurosci.

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Alzheimer's disease (AD) is one of the leading causes of dementia in late life. Although the cause of AD neurodegenerative changes is not fully understood, extensive evidence suggests that the misfolding, aggregation and cerebral accumulation of amyloid beta (Aβ) and tau proteins are hallmark events. Recent reports have shown that protein misfolding and aggregation can be induced by administration of small quantities of preformed aggregates, following a similar principle by which prion diseases can be transmitted by infection. In the past few years, many of the typical properties that characterize prions as infectious agents were also shown in Aβ aggregates. Interestingly, prion diseases affect not only humans, but also various species of mammals, and it has been demonstrated that infectious prions present in animal tissues, particularly cattle affected by bovine spongiform encephalopathy (BSE), can infect humans. It has been reported that protein deposits resembling Aβ amyloid plaques are present in the brain of several aged non-human mammals, including monkeys, bears, dogs, and cheetahs. In this study, we investigated the presence of Aβ aggregates in the brain of aged cattle, their similarities with the protein deposits observed in AD patients, and their capability to promote AD pathological features when intracerebrally inoculated into transgenic animal models of AD. Our data show that aged cattle can develop AD-like neuropathological abnormalities, including amyloid plaques, as studied histologically. Importantly, cow-derived aggregates accelerate Aβ amyloid deposition in the brain of AD transgenic animals. Surprisingly, the rate of induction produced by administration of the cattle material was substantially higher than induction produced by injection of similar amounts of human AD material. Our findings demonstrate that cows develop seeding-competent Aβ aggregates, similarly as observed in AD patients.

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Section: Discussionmentioning

confidence: 63%

Aged Cattle Brain Displays Alzheimer's Disease-Like Pathology and Promotes Brain Amyloidosis in a Transgenic Animal Model

Moreno-González

Edwards

Morales

et al. 2022

Front. Aging Neurosci.

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“…The results support the view that amyloid structures from food-derived proteins do not constitute a health risk although more studies on different disease-associated proteins are still needed. It should also be noted that there may be a significant difference between amyloid formed in vitro and amyloid originating from in vivo deposits, as illustrated by the enhanced aggregation of Aβ triggered by AA from cattle 24 . The amyloid-like structures applied in materials, or even food, however, falls within the in vitro category.…”

Section: Discussionmentioning

confidence: 99%

“…The aggregation of amyloid β (Aβ), and in particular the 42 amino acid residues long variant Aβ 1–42 , into senile plaques is a central pathological signature of Alzheimer’s disease 21 . A number of in vitro studies have explored the cross-talk between Aβ and other human disease-associated amyloid proteins and acceleration of Aβ aggregation has been reported for α-synuclein 22 , 23 , AA amyloid 24 and IAPP 25 . Some studies also go beyond the disease-associated proteins and investigate cross-seeding of Aβ by functional amyloid 26 , 27 or non-amyloid protein fibers 25 .…”

Section: Introductionmentioning

confidence: 99%

Food protein-derived amyloids do not accelerate amyloid β aggregation

Rahman

Pires

Herneke

et al. 2023

Sci Rep

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The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are not associated with disease can form amyloid with similar structural characteristics as the disease-associated fibrils, which highlights the potential risk of cross-seeding of disease amyloid by amyloid-like structures encountered in our surrounding. Of particular interest are common food proteins that can be transformed into amyloid under conditions similar to cooking. We here investigate cross-seeding of amyloid-β (Aβ), a peptide known to form amyloid during the development of Alzheimer’s disease, by 16 types of amyloid fibrils derived from food proteins or peptides. Kinetic studies using thioflavin T fluorescence as output show that none of the investigated protein fibrils accelerates the aggregation of Aβ. In at least two cases (hen egg lysozyme and oat protein isolate) we observe retardation of the aggregation, which appears to originate from interactions between the food protein seeds and Aβ in aggregated form. The results support the view that food-derived amyloid is not a risk factor for development of Aβ pathology and Alzheimer’s disease.

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“…It is worth mentioning that the A𝛽42 peptide is extremely active, and can be self-seeded (also see below) and cross-seeded by different preformed fibrils, [69] including cattle meat (human consumable) extracted AA fibrils. [71] Interestingly, the fibrillization traces of A𝛽42 with and without preformed Rep MiSp amyloidlike fibril seeds were able to be superimposed, and the aggregation half time 𝜏 1/2 and maximum aggregation rate r max both showed approximately flat lines, even with up to 40% (of the A𝛽42 monomer molar concentration) of seeds (Figure 4a,b), indicating no cross-seeding effects, which is different form the above mentioned fibrillar materials as well as the eADF-4 (MaSp2 derivative) fibrils. [33,68] The aggregation in cross-seeding results from intermolecular interaction between different proteins, especially oppositely charged proteins.…”

Section: Cross-seeding Effects and Cytotoxicity Of Rep Misp Nanofibrilsmentioning

confidence: 99%

Spider Silk Protein Forms Amyloid‐Like Nanofibrils through a Non‐Nucleation‐Dependent Polymerization Mechanism

Wang

et al. 2023

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Amyloid fibrils—nanoscale fibrillar aggregates with high levels of order—are pathogenic in some today incurable human diseases; however, there are also many physiologically functioning amyloids in nature. The process of amyloid formation is typically nucleation‐elongation‐dependent, as exemplified by the pathogenic amyloid‐β peptide (Aβ) that is associated with Alzheimer's disease. Spider silk, one of the toughest biomaterials, shares characteristics with amyloid. In this study, it is shown that forming amyloid‐like nanofibrils is an inherent property preserved by various spider silk proteins (spidroins). Both spidroins and Aβ capped by spidroin N‐ and C‐terminal domains, can assemble into macroscopic spider silk‐like fibers that consist of straight nanofibrils parallel to the fiber axis as observed in native spider silk. While Aβ forms amyloid nanofibrils through a nucleation‐dependent pathway and exhibits strong cytotoxicity and seeding effects, spidroins spontaneously and rapidly form amyloid‐like nanofibrils via a non‐nucleation‐dependent polymerization pathway that involves lateral packing of fibrils. Spidroin nanofibrils share amyloid‐like properties but lack strong cytotoxicity and the ability to self‐seed or cross‐seed human amyloidogenic peptides. These results suggest that spidroins´ unique primary structures have evolved to allow functional properties of amyloid, and at the same time direct their fibrillization pathways to avoid formation of cytotoxic intermediates.

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AA amyloid in human food chain is a possible biohazard

Cited by 12 publications

References 22 publications

Aged Cattle Brain Displays Alzheimer's Disease-Like Pathology and Promotes Brain Amyloidosis in a Transgenic Animal Model

Aged Cattle Brain Displays Alzheimer's Disease-Like Pathology and Promotes Brain Amyloidosis in a Transgenic Animal Model

Food protein-derived amyloids do not accelerate amyloid β aggregation

Spider Silk Protein Forms Amyloid‐Like Nanofibrils through a Non‐Nucleation‐Dependent Polymerization Mechanism

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