Viruses and amyloids - a vicious liaison

Hammarström, Per; Nyström, Sofie

doi:10.1080/19336896.2023.2194212

Cited by 11 publications

(4 citation statements)

References 172 publications

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“…While some recent studies have proposed putative links between SARS-COV-2 proteins and amyloidosis 43,44 , including induction of amyloid formation by human proteins such as surfactant protein-C 47 , α -synuclein 46 , and SAA 48 , relatively little is known about the underlying molecular mechanisms that lead to such complications. Similar links between viral infection and amyloidosis have been made for other human viruses, including HIV, HSV-1 and Influenza A, both as a direct consequence of aggregation-prone viral proteins and as a secondary effect of inflammation 38 .…”

Section: Discussionsupporting

confidence: 55%

“…In patients with chronic inflammation, additional infection with COVID-19 can further increase their risk of AA amyloidosis due to covid-induced expression of proinflammatory cytokines and SAA, adding to their existing high levels 32,37 . The organs and tissues affected by systemic or localized AA amyloidosis are in many instances overlapping with those afflicted by COVID-19 38 . Therefore, it has been hypothesized that AA amyloidosis is an important factor causing systemic complications after COVID-19 39 .…”

Section: Introductionmentioning

confidence: 99%

“…Recent studies have shown that protease cleavage of several SARS-CoV-2 proteins (spike, ORF-10, ORF-6) results in the release of amyloidogenic peptides 43,44 . Adding to recent hypotheses linking viral infection and amyloid diseases, 38 SARS-CoV-2 is able to promote amyloidogenesis of human proteins 45 . For example, the SARS-CoV-2 N protein accelerates fibrillization of human α-synuclein through an electrostatic interaction, 46 and viral induction of surfactant protein amyloidosis in the lung has been proposed as a contributor to acute respiratory distress syndrome (ARDS) in COVID-19 patients 47 .…”

Section: Introductionmentioning

confidence: 99%

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An amyloidogenic fragment of the SARS CoV-2 envelope protein promotes serum amyloid A misfolding and fibrillization

Nady,

Reichheld,

Sharpe

2024

Preprint

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SARS CoV-2 infection can affect a surprising number of organs in the body and cause symptoms such as abnormal blood coagulation, fibrinolytic disturbances, and neurodegeneration. Our study delves into the intricate pathogenic potential of a SARS-CoV-2 envelope protein peptide, shedding light on its implications for multi-organ effects and amyloid formation. Specifically, we focus on the peptide SK9 or54SFYVYSRVK62derived from the C-terminus of human SARS coronavirus 2 envelope protein. We demonstrate that SK9 containing peptides readily form classic amyloid structures consistent with predictions of amyloid aggregation algorithms. In vivo, overexpression of proteases such as neutrophil elastase during inflammation can potentially lead to C-terminal peptides containing SK9. We also demonstrate that SK9 can promote the fibrillization of SAA, a protein marker of acute inflammation. Our investigations reveal that the aromatic residues Phe2 and Tyr3 of SK9 play a pivotal role in its amyloidogenic function. We show that the primary sites of SK9-SAA binding lie in the amyloidogenic hotspots of SAA itself. Our results highlight two possible complications of SARS CoV-2 infection in individuals with hyper-inflammation either due to amyloids arising from SK9 containing peptides or SK9-induced AA amyloidosis.

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Section: Discussionsupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

An amyloidogenic fragment of the SARS CoV-2 envelope protein promotes serum amyloid A misfolding and fibrillization

Nady,

Reichheld,

Sharpe

2024

Preprint

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“…Viral infections are prevalent in humans and can cause permanent injury to various degrees and by different mechanisms (Hammarström and Nyström, 2023). Liu et al (Liu X. et al, 2023) investigated the effect of curcumin on Frontiers in Pharmacology frontiersin.org porcine epidemic diarrhea virus (PEDV) infection by using VERO cells as experimental objects.…”

Section: Antiviral Effectmentioning

confidence: 99%

Sources, morphology, phytochemistry, pharmacology of Curcumae Longae Rhizoma, Curcumae Radix, and Curcumae Rhizoma: a review of the literature

Zhu,

Quan,

Yin

et al. 2023

Front. Pharmacol.

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Curcumae Longae Rhizoma (turmeric), Curcumae Radix and Curcumae Rhizoma are derived from the Curcuma species, and have gradually become three of the most commonly used medicinal herbs in China due to their different origins, processing methods and medicinal part. These three herbs have certain similarities in morphology, chemical composition, and pharmacological effects. All three of these herbs contain curcuminoids and volatile oil compounds, which exhibit anti-inflammatory, anti-tumor, antioxidant, and neuroprotective properties, although modern clinical applications have their own requirements. At present, there is no systematic guidelines for the clinical application of these three of Curcuma species; consequently, there is a high risk of unwanted phenomena associated with the mixing and indiscriminate use of these herbs. In this review, we focus predominantly on morphology, chemical composition, and the pharmacological activity of these three Curcuma herbs and summarize the current status of research in this field. Our goal is to provide a better understanding of clinical value of these Curcuma species so that we can provide reference guidelines for their further development, utilization and rational clinical application.

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The Promising Role of Selenium and Yeast in the Fight Against Protein Amyloidosis

Kieliszek,

Sapazhenkava

2024

Biol Trace Elem Res

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In recent years, increasing attention has been paid to research on diseases related to the deposition of misfolded proteins (amyloids) in various organs. Moreover, modern scientists emphasise the importance of selenium as a bioelement necessary for the proper functioning of living organisms. The inorganic form of selenium—sodium selenite (redox-active)—can prevent the formation of an insoluble polymer in proteins. It is very important to undertake tasks aimed at understanding the mechanisms of action of this element in inhibiting the formation of various types of amyloid. Furthermore, yeast cells play an important role in this matter as a eukaryotic model organism, which is intensively used in molecular research on protein amyloidosis. Due to the lack of appropriate treatment in the general population, the problem of amyloidosis remains unsolved. This extracellular accumulation of amyloid is one of the main factors responsible for the occurrence of Alzheimer’s disease. The review presented here contains scientific information discussing a brief description of the possibility of amyloid formation in cells and the use of selenium as a factor preventing the formation of these protein aggregates. Recent studies have shown that the yeast model can be successfully used as a eukaryotic organism in biotechnological research aimed at understanding the essence of the entire amyloidosis process. Understanding the mechanisms that regulate the reaction of yeast to selenium and the phenomenon of amyloidosis is important in the aetiology and pathogenesis of various disease states. Therefore, it is imperative to conduct further research and analysis aimed at explaining and confirming the role of selenium in the processes of protein misfolding disorders. The rest of the article discusses the characteristics of food protein amyloidosis and their use in the food industry. During such tests, their toxicity is checked because not all food proteins can produce amyloid that is toxic to cells. It should also be noted that a moderate diet is beneficial for the corresponding disease relief caused by amyloidosis.

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Viruses and amyloids - a vicious liaison

Cited by 11 publications

References 172 publications

An amyloidogenic fragment of the SARS CoV-2 envelope protein promotes serum amyloid A misfolding and fibrillization

An amyloidogenic fragment of the SARS CoV-2 envelope protein promotes serum amyloid A misfolding and fibrillization

Sources, morphology, phytochemistry, pharmacology of Curcumae Longae Rhizoma, Curcumae Radix, and Curcumae Rhizoma: a review of the literature

The Promising Role of Selenium and Yeast in the Fight Against Protein Amyloidosis

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