Evidence map›Paper›PMID 20209079›Full record

ArticlePloS one2010

The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide.

Stephanie J Soscia, James E Kirby, Kevin J Washicosky, Stephanie M Tucker, Martin Ingelsson, Bradley Hyman, Mark A Burton, Lee E Goldstein, Scott Duong, Rudolph E Tanzi and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 585 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
585citing papers in PubMed, 2 pooled it
48.4field-weighted citation impact, top 1% 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

585 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,013 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
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  7. Review
  8. Article
  9. Article
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  13. β-Amyloid (Aβ) and Human Cathelicidin LL-37: Two Sides of the Same Coin?International journal of molecular sciences · 2026
    Review
  14. Review
  15. Article
  16. Article
  17. Monocolonization withMicrobiology spectrum · 2026
    Article
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525 more citing papers are in PubMed but not listed here.

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

11 authors at 5 institutions in 2 countries.

Stephanie J SosciaGenetics and Aging Research Unit, Mass General Institute for Neurodegenerative Disease and Department of Neurology, Massachusetts General Hospital, Charlestown, Massachusetts, United States of America.
James E Kirby
Kevin J Washicosky
Stephanie M Tucker
Martin Ingelsson
Bradley Hyman
Mark A Burton
Lee E Goldstein
Scott Duong
Rudolph E Tanzi
Robert D Moir
Massachusetts General Hospital · USBoston University · USBeth Israel Deaconess Medical Center · USHarvard University · USUppsala University · SE

Funding

The Abeta protein of Alzheimer's Disease is an antimicrobial peptideR01AI081990 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI MOIR, ROBERT D · 2010 to 2014
$2.2M
NIAID NIH HHS R01 AI081990
6 · The paper itself

Abstract

backgroundThe amyloid beta-protein (Abeta) is believed to be the key mediator of Alzheimer's disease (AD) pathology. Abeta is most often characterized as an incidental catabolic byproduct that lacks a normal physiological role. However, Abeta has been shown to be a specific ligand for a number of different receptors and other molecules, transported by complex trafficking pathways, modulated in response to a variety of environmental stressors, and able to induce pro-inflammatory activities. METHODOLOGY/PRINCIPAL

findingsHere, we provide data supporting an in vivo function for Abeta as an antimicrobial peptide (AMP). Experiments used established in vitro assays to compare antimicrobial activities of Abeta and LL-37, an archetypical human AMP. Findings reveal that Abeta exerts antimicrobial activity against eight common and clinically relevant microorganisms with a potency equivalent to, and in some cases greater than, LL-37. Furthermore, we show that AD whole brain homogenates have significantly higher antimicrobial activity than aged matched non-AD samples and that AMP action correlates with tissue Abeta levels. Consistent with Abeta-mediated activity, the increased antimicrobial action was ablated by immunodepletion of AD brain homogenates with anti-Abeta antibodies. CONCLUSIONS/SIGNIFICANCE: Our findings suggest Abeta is a hitherto unrecognized AMP that may normally function in the innate immune system. This finding stands in stark contrast to current models of Abeta-mediated pathology and has important implications for ongoing and future AD treatment strategies.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAntimicrobial Cationic PeptidesBrainCandida albicansCathelicidinsCell SurvivalEnvironmentHumansImmunity, InnateInflammationLigandsMicrobial Sensitivity TestsOxazinesRecombinant ProteinsXanthenesAmyloid beta-PeptidesAntimicrobial Cationic PeptidesCathelicidinsLigandsOxazinesRecombinant ProteinsresazurinXanthenes

Identifiers

PMID20209079
PMCPMC2831066
OpenAlexW2108629610

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.