Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
A hallmark of α-synucleinopathies (e.g., Parkinson's disease) is the misfolding and aggregation of α-synuclein in tissues and biological fluids. Protein amplification assays like real-time quaking-induced conversion (RT-QuIC) are sensitive yet currently limited to semi-invasive sample types such as cerebrospinal fluid because more accessible samples, such as blood, contain inhibitors. Here, we show that Nanoparticle-enhanced Quaking-induced Conversion (Nano-QuIC) can double the speed of reactions spiked with misfolded α-synuclein while increasing sensitivity 100-fold in human plasma. Nano-QuIC detected spike concentrations down to 90 pg/mL in lysed whole blood, while reactions without nanoparticles (RT-QuIC) failed to have any detection due to the presence of strong inhibitors. Moreover, Nano-QuIC showed increased seeding activity in plasma samples from Parkinson's patients (n = 4) versus healthy controls (n = 4). This sets the groundwork for the noninvasive diagnostic use of Nano-QuIC, potentially enabling early disease detection and management through blood-based testing.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.nanolett.4c03768 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Coexistence of CSF anti-Ma2 antibody and 14-3-3 protein: a diagnostic dilemma between autoimmune encephalitis and Creutzfeldt-Jakob disease, a Case Report.
Front Immunol
August 2025
Department of Neurology, The Second Clinical Medical College, Jinan University, Shenzhen, Guangdong, China.
Background: Anti-Ma2 antibody encephalitis is a rare paraneoplastic autoimmune encephalitis (AE) caused by anti-Ma2 antibody. Creutzfeldt-Jakob disease (CJD), a group of human prion diseases, is a rapidly advancing and fatal neurodegenerative disorder. The two diseases may display comparable clinical symptoms that are easily misdiagnosed.
View Article and Find Full Text PDFUnlabelled: α-Synuclein (α-syn) is an abundant monomeric protein that can aggregate into fibrils and form neuropathological inclusions in the brains of patients with synucleinopathies. New evidence suggests that the mouse-human transmission barrier of α-syn is lower than previously reported, emphasizing the need for improved biosafety procedures when working with α-syn aggregates. Histopathology of α-syn-infected brain represents a significant potential source of occupational exposure, and current methods for tissue fixation do not inactivate the ability of pathologic α-syn to seed the conversion of endogenous, monomeric α-syn into fibrils.
View Article and Find Full Text PDFMonomeric α-Synuclein Real-Time Induced Conversion: A New Approach to the Diagnostics of Neurodegenerative Synucleinopathies with Weak RT-QuIC Responses.
Acta Naturae
January 2025
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997 Russia.
Neurodegenerative disorders classified as synucleinopathies (Parkinson's disease, dementia with Lewy bodies, and multiple-system atrophy) are characterized by the accumulation of aberrant α-synuclein aggregates in neurons and glial cells. These diseases manifest clinically several years after the initial formation of pathological protein aggregates in the brain, making early and accurate diagnosis challenging. In recent years, a new method, which is based on real-time quaking-induced conversion (RT-QuIC) of α-synuclein, has been developed and validated.
View Article and Find Full Text PDFCreutzfeldt-Jakob Disease in South Texas: A Case Series of Three Hispanic Patients.
Cureus
June 2025
Neurology Institute, Doctors Hospital at Renaissance, McAllen, USA.
Creutzfeldt-Jakob disease (CJD) is a rare, rapidly progressive neurodegenerative disorder instigated by the pleating of prion proteins. Most cases are sporadic, with no identifiable genetic or environmental trigger. This retrospective case series aims to bridge the current knowledge gap in regard to CJD in Hispanic populations.
View Article and Find Full Text PDFHuman PrP E219K: a new and promising substrate for robust RT-QuIC amplification of human prions with potential for strain discrimination.
Microbiol Spectr
August 2025
Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université Versailles-Saint Quentin, Unité de Virologie et d'Immunologie Moléculaires, Jouy-en-Josas, France.
Unlabelled: Mammalian prion diseases are fatal neurodegenerative disorders caused by the conformational conversion of the host-encoded prion protein (PrP) into a pathogenic, misfolded isoform, known as PrP. Definitive diagnosis currently relies on post-mortem histopathological examination of the central nervous system. Among emerging diagnostic tools, amplification techniques such as Real-Time Quaking-Induced Conversion (RT-QuIC) have demonstrated high sensitivity, specificity, and speed, although certain prion strains remain difficult to amplify.
View Article and Find Full Text PDF