Evidence map›Paper›PMID 38428032›Full record

ArticleBrain : a journal of neurology2024

Vaccination with structurally adapted fungal protein fibrils induces immunity to Parkinson's disease.

Verena Pesch, José Miguel Flores-Fernandez, Sara Reithofer, Liang Ma, Pelin Özdüzenciler, Yannick Busch, Aishwarya Sriraman, YongLiang Wang, Sara Amidian, Chiara V M Kroepel and 7 more

Open access · hybridAbstract read
In one paragraph

Article in Brain : a journal of neurology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 8 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors at 2 institutions in 2 countries.

Verena PeschInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
José Miguel Flores-FernandezDepartment of Biochemistry and Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB T6G 2M8, Canada.
Sara ReithoferInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Liang MaInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Pelin ÖzdüzencilerInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Yannick BuschInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Aishwarya SriramanDepartment of Biochemistry and Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB T6G 2M8, Canada.
YongLiang WangDepartment of Biochemistry and Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB T6G 2M8, Canada.
Sara AmidianDepartment of Biochemistry and Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB T6G 2M8, Canada.
Chiara V M KroepelInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Laura MüllerInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Yi LienInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Olivia RudtkeInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Benedikt FriegInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Gunnar F SchröderInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Holger WilleDepartment of Biochemistry and Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB T6G 2M8, Canada.ORCID 0000-0001-5102-8706
Gültekin TamgüneyInstitut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-6933-5154
Forschungszentrum Jülich · DEUniversity of Alberta · CA

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
NIGMS NIH HHS R01 GM129325
6 · The paper itself

Abstract

The pathological misfolding and aggregation of soluble α-synuclein into toxic oligomers and insoluble amyloid fibrils causes Parkinson's disease, a progressive age-related neurodegenerative disease for which there is no cure. HET-s is a soluble fungal protein that can form assembled amyloid fibrils in its prion state. We engineered HET-s(218-298) to form four different fibrillar vaccine candidates, each displaying a specific conformational epitope present on the surface of α-synuclein fibrils. Vaccination with these four vaccine candidates prolonged the survival of immunized TgM83+/- mice challenged with α-synuclein fibrils by 8% when injected into the brain to model brain-first Parkinson's disease or by 21% and 22% when injected into the peritoneum or gut wall, respectively, to model body-first Parkinson's disease. Antibodies from fully immunized mice recognized α-synuclein fibrils and brain homogenates from patients with Parkinson's disease, dementia with Lewy bodies and multiple system atrophy. Conformation-specific vaccines that mimic epitopes present only on the surface of pathological fibrils but not on soluble monomers, hold great promise for protection against Parkinson's disease, related synucleinopathies and other amyloidogenic protein misfolding disorders.

Indexed as

alpha-SynucleinMice, TransgenicParkinson DiseaseAmyloidAnimalsBrainFemaleFungal ProteinsHumansMiceMice, Inbred C57BLVaccinationalpha-SynucleinAmyloidFungal Proteinsalpha-synucleinamyloidconformationfibrilimmunizationvaccine

Identifiers

PMID38428032
PMCPMC11068327
OpenAlexW4392389074

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.