Evidence map›Paper›PMID 32193491›Full record

ArticleCommunications biology2020

Why does the Aβ peptide of Alzheimer share structural similarity with antimicrobial peptides?

Annalisa Pastore, Francesco Raimondi, Lawrence Rajendran, Piero Andrea Temussi

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Science advances · 2025
    Article
  5. Peripheral proteinopathy in neurodegenerative diseases.Translational neurodegeneration · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  11. Review
  12. γ-Secretase fanning the fire of innate immunity.Biochemical Society transactions · 2023
    Review
  13. Review
  14. Article
  15. Review
  16. Testing Antimicrobial Properties of Selected Short Amyloids.International journal of molecular sciences · 2023
    Article
  17. Article
  18. 1-L Transcription in Alzheimer's Disease.Current issues in molecular biology · 2022
    Article
  19. Review
  20. Article
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

4 authors at 2 institutions in 2 countries.

Annalisa PastoreUK-Dementia Research Institute (UK-DRI) at King's College London, London, UK. annalisa.pastore@crick.ac.uk.ORCID http://orcid.org/0000-0002-3047-654X
Francesco RaimondiScuola Normale Superiore, Piazza dei Cavalieri, Pisa, Italy.
Lawrence RajendranUK-Dementia Research Institute (UK-DRI) at King's College London, London, UK.
Piero Andrea TemussiUK-Dementia Research Institute (UK-DRI) at King's College London, London, UK. temussi@unina.it.
King's College London · GBScuola Normale Superiore · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Aβ peptides causally associated with Alzheimer disease have been seen as seemingly purposeless species produced by intramembrane cleavage under both physiological and pathological conditions. However, it has been increasingly suggested that they could instead constitute an ancient, highly conserved effector component of our innate immune system, dedicated to protecting the brain against microbial attacks. In this antimicrobial protection hypothesis, Aβ aggregation would switch from an abnormal stochastic event to a dysregulated innate immune response. In this perspective, we approach the problem from a different and complementary perspective by comparing the structure and sequence of Aβ(1-42) with those of bona fide antimicrobial peptides. We demonstrate that Aβ(1-42) bears convincing structural similarities with both viral fusion domains and antimicrobial peptides, as well as sequence similarities with a specific family of bacterial bacteriocins. We suggest a model of the mechanism by which Aβ peptides could elicit the immune response against microbes.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsBacteriaBrainDatabases, ProteinHost-Pathogen InteractionsHumansImmunity, InnateModels, MolecularPeptide FragmentsPore Forming Cytotoxic ProteinsProtein AggregatesProtein Aggregation, PathologicalProtein ConformationStructure-Activity RelationshipAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide FragmentsPore Forming Cytotoxic ProteinsProtein Aggregates

Identifiers

PMID32193491
PMCPMC7081199
OpenAlexW3012434222

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.