Are there prions in plants?

Chernoff, Yury O.

doi:10.1073/pnas.1605671113

Cited by 10 publications

(7 citation statements)

References 16 publications

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“…Apart from the extraneous PrP Sc in plants, a protein named luminidependens from Arabidopsis thaliana was transformed and propagated like PrP when injected in yeast cells. 442 …”

Section: Prions and Prion Diseasesmentioning

confidence: 99%

Implications of peptide assemblies in amyloid diseases

et al. 2017

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Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the quality of life of millions worldwide, with profound social and economic implications. Despite the significant differences in pathology – much of which are poorly understood – these diseases are commonly characterized by the presence of cross-β amyloid fibrils as well as the loss of neuronal or pancreatic β-cells. In this review, we document research progress on the molecular and mesoscopic self-assembly of amyloid-beta, alpha synuclein, human islet amyloid polypeptide and prions, the peptides and proteins associated with Alzheimer’s, Parkinson’s, type 2 diabetes and prions diseases. In addition, we discuss the toxicities of these amyloid proteins based on their self-assembly as well as their interactions with membranes, metal ions, small molecules and engineered nanoparticles. Through this presentation we show the remarkable similarities and differences in the structural transitions of the amyloid proteins through primary and secondary nucleation, the common evolution from disordered monomers to alpha-helices and then to β-sheets when the proteins encounter the cell membrane, and, the consensus (with a few exceptions) that off-pathway oligomers, rather than amyloid fibrils, are the toxic species regardless of the pathogenic protein sequence or physicochemical properties. In addition, we highlight the crucial role of molecular self-assembly in eliciting the biological and pathological consequences of the amyloid proteins within the context of their cellular environments and their spreading between cells and organs. Exploiting such structure-function-toxicity relationship may prove pivotal for the detection and mitigation of amyloid diseases.

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“…Apart from the extraneous PrP Sc in plants, a protein named luminidependens from Arabidopsis thaliana was transformed and propagated like PrP when injected in yeast cells. 442 …”

Section: Prions and Prion Diseasesmentioning

confidence: 99%

Implications of peptide assemblies in amyloid diseases

et al. 2017

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“…The protein Luminidependens of the plant Arabidopsis thaliana , that is capable of forming amyloid-like oligomers, is involved in the regulation of flowering by temperature [ 19 ]. Notably, this protein is a chromatin remodeler [ 20 ], albeit a connection of this function to amyloidogenecity is still hypothetical [ 21 ]. Curli proteins in Escherichia coli are assembled on a bacterial cell surface as a part of the extracellular matrix during biofilm formation and control resistance to a variety of environmental stresses [ 22 , 23 ].…”

Section: Introductionmentioning

confidence: 99%

Functional Mammalian Amyloids and Amyloid-Like Proteins

Rubel

Fedotov

Grizel

et al. 2020

Life

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Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD), type 2 diabetes (T2D), and prion diseases. Some amyloid-associated diseases, in particular T2D and AD, are widespread and affect hundreds of millions of people all over the world. However, recently it has become evident that many amyloids, termed “functional amyloids,” are involved in various activities that are beneficial to organisms. Functional amyloids were discovered in diverse taxa, ranging from bacteria to mammals. These amyloids are involved in vital biological functions such as long-term memory, storage of peptide hormones and scaffolding melanin polymerization in animals, substrate attachment, and biofilm formation in bacteria and fungi, etc. Thus, amyloids undoubtedly are playing important roles in biological and pathological processes. This review is focused on functional amyloids in mammals and summarizes approaches used for identifying new potentially amyloidogenic proteins and domains.

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“…59 Prionization typically entails the functional inactivation of prionforming protein; 60 therefore, according to the hypothesis of Y. Chernoff, the most likely phenotype of LD prionization would be the delay of the flowering. 61 Notably, temperature is not only a factor controlling vernalization in plants but also affects both the induction 62 and stability of prions. 63 Thus, the influence of temperature on flowering could also be modulated through changes in the induction frequency or the effectiveness of LD prion propagation.…”

Section: Prion-like Protein Luminidependens Of Arabidopsis Thalianamentioning

confidence: 99%

Amyloids and prions in plants: Facts and perspectives

Antonets

Nizhnikov

2017

Prion

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Amyloids represent protein fibrils that have highly ordered structure with unique physical and chemical properties. Amyloids have long been considered lethal pathogens that cause dozens of incurable diseases in humans and animals. Recent data show that amyloids may not only possess pathogenic properties but are also implicated in the essential biological processes in a variety of prokaryotes and eukaryotes. Functional amyloids have been identified in archaea, bacteria, fungi, and animals, including humans. Plants are one of the most poorly studied groups of organisms in the field of amyloid biology. Although amyloid properties have not been shown under native conditions for any plant protein, studies demonstrating amyloid properties for a set of plant proteins in vitro or in heterologous systems in vivo have been published in recent years. In this review, we systematize the data on the amyloidogenic proteins of plants and their functions and discuss the perspectives of identifying novel amyloids using bioinformatic and proteomic approaches.

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Are there prions in plants?

Cited by 10 publications

References 16 publications

Implications of peptide assemblies in amyloid diseases

Implications of peptide assemblies in amyloid diseases

Functional Mammalian Amyloids and Amyloid-Like Proteins

Amyloids and prions in plants: Facts and perspectives

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