Evidence map›Paper›PMID 30157279›Full record

ArticlePloS one2018

Extending the functional characteristics of naturally occurring autoantibodies against β-Amyloid, Prion Protein and α-Synuclein.

Alexandra Albus, Maike Gold, Jan-Philipp Bach, Monika Burg-Roderfeld, Marit Jördens, Yvonne Kirchhein, Yannick Kronimus, David Mengel, Inga Zerr, Richard Dodel

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2018. 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
0.5field-weighted citation impact, top 36% 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, 12 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Alexandra AlbusChair of Geriatrics, University Hospital Essen, University Duisburg-Essen, Essen, Germany.ORCID 0000-0002-4897-6972
Maike GoldDepartment of Neurology, Philipps-University, Marburg, Germany.
Jan-Philipp BachDepartment of Neurology, Philipps-University, Marburg, Germany.
Monika Burg-RoderfeldDepartment of Hematology and Immunology, Justus-Liebig-University, Giessen, Germany.
Marit JördensDepartment of Neurology, Philipps-University, Marburg, Germany.
Yvonne KirchheinDepartment of Neurology, Philipps-University, Marburg, Germany.
Yannick KronimusChair of Geriatrics, University Hospital Essen, University Duisburg-Essen, Essen, Germany.
David MengelDepartment of Neurology, Philipps-University, Marburg, Germany.
Inga ZerrDepartment of Neurology, University Goettingen, Goettingen, Germany.
Richard DodelChair of Geriatrics, University Hospital Essen, University Duisburg-Essen, Essen, Germany.
Philipps University of Marburg · DEJustus-Liebig-Universität Gießen · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAbnormal aggregation of proteins induces neuronal cell loss in neurodegenerative disorders such as Alzheimer's Disease, Creutzfeldt-Jakob Disease and Parkinson's Disease. Specific stimuli initialize conformational changes in physiological proteins, causing intra- or extracellular protein aggregation. We and other groups have identified naturally occurring autoantibodies (nAbs) as part of the human antibody pool that are able to prevent peptide fibrillation. These nAbs show a rescue effect following exposure of toxic aggregates on neurons, and they support microglial uptake of aggregated peptides.

objectiveIdentification of a putative common epitope among the relevant proteins β-Amyloid, α-Synuclein and Prion Protein for the respective nAbs. MATERIAL AND

methodsBinding affinity between the aforementioned proteins and nAbs was tested by Dot Blot, ELISA and SPR-technology. Furthermore, the functionality of the protein-nAbs-complexes was studied in Thioflavin-T assays and microglial uptake experiments to study dependent inhibition of protein aggregation and enhancement of Fcγ mediated uptake by microglial cells.

resultsβ-Amyloid and Prion Protein fragment showed considerable binding affinity and functional efficacy for all applied nAbs. Thereby, no significant difference within the different nAbs was detected. In contrast, α-Synuclein was bound exclusively by nAbs-α-Synuclein, which was reproduced in all binding studies. Surprisingly, functional assays with α-Synuclein revealed no significant effect of nAbs in comparison to IVIg treatment. However, all applied nAbs as well as IVIg show a minimal functionality on the microglial uptake of α-Synuclein.

conclusionnAbs-Aβ, nAbs-PrP possibly display comparable affinity to the same structural epitope within Aβ and PrP106-126 A117V whereas the epitope recognized by nAbs-α-Syn is only present in α-Syn. The structural similarity of Aβ and PrP fragment promotes the outline for an efficient antibody for the treatment of several neurodegenerative disorders and extend the functional characteristics of the investigated nAbs.

Indexed as

alpha-SynucleinAmyloid beta-PeptidesAnimalsAutoantibodiesCell LineEpitopesHumansMicePeptide FragmentsPrion Proteinsalpha-SynucleinAmyloid beta-Peptidesamyloid beta-protein (1-42)AutoantibodiesEpitopesPeptide FragmentsPrion Proteins

Identifiers

PMID30157279
PMCPMC6114858
OpenAlexW2889142244

What OpenQuestion holds

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Registered trials

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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.