Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion

Elmallah, Mohammed I. Y.; Borgmeyer, Uwe; Betzel, Christian; Redecke, Lars

doi:10.4161/pri.26745

Cited by 26 publications

(19 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Pseudosulfoxidation mutants have been used to mimic methionine oxidation, confirming that oxidation of surface exposed methionine residues perturbs the PrP C structure resulting in destabilization and misfolding 44 . Interestingly, the D178N variant of PrP C was recently found to be more susceptible to methionine oxidation 45 .…”

Section: Conflicting Evidence Linking Methionine Oxidation With Mammamentioning

confidence: 95%

Sup35 methionine oxidation is a trigger forde novo[PSI⁺] prion formation

Grant¹

2015

Prion

View full text Add to dashboard Cite

The molecular basis by which fungal and mammalian prions arise spontaneously is poorly understood. A number of different environmental stress conditions are known to increase the frequency of yeast [PSI(+)] prion formation in agreement with the idea that conditions which cause protein misfolding may promote the conversion of normally soluble proteins to their amyloid forms. A recent study from our laboratory has shown that the de novo formation of the [PSI(+)] prion is significantly increased in yeast mutants lacking key antioxidants suggesting that endogenous reactive oxygen species are sufficient to promote prion formation. Our findings strongly implicate oxidative damage of Sup35 as an important trigger for the formation of the heritable [PSI(+)] prion in yeast. This review discusses the mechanisms by which the direct oxidation of Sup35 might lead to structural transitions favoring conversion to the transmissible amyloid-like form. This is analogous to various environmental factors which have been proposed to trigger misfolding of the mammalian prion protein (PrP(C)) into the aggregated scrapie form (PrP(Sc)).

show abstract

Section: Conflicting Evidence Linking Methionine Oxidation With Mammamentioning

confidence: 95%

Sup35 methionine oxidation is a trigger forde novo[PSI⁺] prion formation

Grant¹

2015

Prion

View full text Add to dashboard Cite

show abstract

“…More concretely, the side chain hydrophobicity index decreases from 0.738 (Met) to 0.238 (MetO) after the sulfoxidation reaction . Not surprisingly, polar amino acids such as Gln (hydrophobicity index of 0.251) and Thr (0.450) can sometimes mimic the sulfoxidized state of a protein . Herein, we would like to put forward the idea that nature may also employ this trick, but in reverse, evolving methionine sites from glutamine and threonine residues.…”

Section: Do the Signaling‐competent Methionines Have A Traceable Evolmentioning

confidence: 99%

“…Now, we shall address the other case, that is, when the methionine PTM leads to activation. Given that the extant protein is inactive with Met but active with MetO, under the same sensible assumption that the ancestral protein was constitutively active, we must look at amino acids quite different in properties to Met but similar to MetO, and we already know that the obvious candidates are glutamine and threonine …”

Section: Do the Signaling‐competent Methionines Have A Traceable Evolmentioning

confidence: 99%

Methionine in proteins: The Cinderella of the proteinogenic amino acids

Aledo

2019

Protein Science

111

View full text Add to dashboard Cite

Methionine in proteins, apart from its role in the initiation of translation, is assumed to play a simple structural role in the hydrophobic core, in a similar way to other hydrophobic amino acids such as leucine, isoleucine, and valine. However, research from a number of laboratories supports the concept that methionine serves as an important cellular antioxidant, stabilizes the structure of proteins, participates in the sequence‐independent recognition of protein surfaces, and can act as a regulatory switch through reversible oxidation and reduction. Despite all these evidences, the role of methionine in protein structure and function is largely overlooked by most biochemists. Thus, the main aim of the current article is not so much to carry out an exhaustive review of the many and diverse processes in which methionine residues are involved, but to review some illustrative examples that may help the nonspecialized reader to form a richer and more precise insight regarding the role‐played by methionine residues in such processes.

show abstract

“…8 Approximately 85% of all CJD cases are sporadic (sCJD) and considered to arise from somatic alteration in PrP C . 30,35 A modern classification of sCJD into 5 distinct subtypes combines 2 types of PrP Sc (Type 1 and Type 2) and 3 possible genotypes at codon 129 (129 M/M, 129 M/V, and 129 V/V). Each subtype of sCJD is characterized by a distinct clinical and histopathological phenotype.…”

Section: Human Prion Diseases In the 21st Centurymentioning

confidence: 99%

Human prion diseases: surgical lessons learned from iatrogenic prion transmission

Bonda

Manjila

Mehndiratta

et al. 2016

FOC

105

View full text Add to dashboard Cite

The human prion diseases, or transmissible spongiform encephalopathies, have captivated our imaginations since their discovery in the Fore linguistic group in Papua New Guinea in the 1950s. The mysterious and poorly understood “infectious protein” has become somewhat of a household name in many regions across the globe. From bovine spongiform encephalopathy (BSE), commonly identified as mad cow disease, to endocannibalism, media outlets have capitalized on these devastatingly fatal neurological conditions. Interestingly, since their discovery, there have been more than 492 incidents of iatrogenic transmission of prion diseases, largely resulting from prion-contaminated growth hormone and dura mater grafts. Although fewer than 9 cases of probable iatrogenic neurosurgical cases of Creutzfeldt-Jakob disease (CJD) have been reported worldwide, the likelihood of some missed cases and the potential for prion transmission by neurosurgery create considerable concern. Laboratory studies indicate that standard decontamination and sterilization procedures may be insufficient to completely remove infectivity from prion-contaminated instruments. In this unfortunate event, the instruments may transmit the prion disease to others. Much caution therefore should be taken in the absence of strong evidence against the presence of a prion disease in a neurosurgical patient. While the Centers for Disease Control and Prevention (CDC) and World Health Organization (WHO) have devised risk assessment and decontamination protocols for the prevention of iatrogenic transmission of the prion diseases, incidents of possible exposure to prions have unfortunately occurred in the United States. In this article, the authors outline the historical discoveries that led from kuru to the identification and isolation of the pathological prion proteins in addition to providing a brief description of human prion diseases and iatrogenic forms of CJD, a brief history of prion disease nosocomial transmission, and a summary of the CDC and WHO guidelines for prevention of prion disease transmission and decontamination of prion-contaminated neurosurgical instruments.

show abstract

Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion

Cited by 26 publications

References 55 publications

Sup35 methionine oxidation is a trigger forde novo[PSI⁺] prion formation

Sup35 methionine oxidation is a trigger forde novo[PSI⁺] prion formation

Methionine in proteins: The Cinderella of the proteinogenic amino acids

Human prion diseases: surgical lessons learned from iatrogenic prion transmission

Contact Info

Product

Resources

About

Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion

Cited by 26 publications

References 55 publications

Sup35 methionine oxidation is a trigger forde novo[PSI+] prion formation

Sup35 methionine oxidation is a trigger forde novo[PSI+] prion formation

Methionine in proteins: The Cinderella of the proteinogenic amino acids

Human prion diseases: surgical lessons learned from iatrogenic prion transmission

Contact Info

Product

Resources

About

Sup35 methionine oxidation is a trigger forde novo[PSI⁺] prion formation

Sup35 methionine oxidation is a trigger forde novo[PSI⁺] prion formation