The Alzheimer's Disease-Associated Amyloid β-Protein Is an Antimicrobial Peptide
Open accessAbstract
BACKGROUND: The 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 FINDINGS: Here, 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.
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Aβ is an antimicrobial peptide, released by neural cells in response to infectious agents.
“It is now well known that Aβ is an antimicrobial peptide, released by neural cells in response to infectious agents12,13, so it is not surprising that the presence of bacteria in the brain can result in Aβ deposition reviewed in8.”
From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [12]
The Abstract (Methodology/Principal Findings; page unavailable) reports Aβ’s antimicrobial activity, and the Discussion calls it an antimicrobial peptide. But the Discussion presents increased Aβ generation in response to infection as a possibility, not an established finding, and does not show that neural cells release Aβ in response to infectious agents. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAβ secretion in response to pathogens by (wild-type) neural cells can be rapid.
“Whilst Aβ deposition is of course much more pronounced in Alzheimer’s disease mouse models, Aβ secretion in response to pathogens by (wild-type) neural cells can be rapid12.”
From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [12]
The Discussion proposes that infection could stimulate an innate immune response and subsequent Aβ production in the CNS. It does not report rapid Aβ secretion by wild-type neural cells in response to pathogens; that specific timing and cell-level claim is unsupported. (LLM, conf=0.83)
Experimental — accuracy not yet measuredIn vitro, Aβ42 has been shown to function as an antimicrobial peptide against eight of 12 pathogens being tested, including Escherichia coli, Candida albicans, Staphylococcus epidermidis, Streptococcus pneumoniae, Staphylococcus aureus, Listeria monocytogenes, Enterococcus faecalis, and Streptococcus agalactiae.
“In vitro, Aβ42 has been shown to function as an antimicrobial peptide against eight of 12 pathogens being tested, including Escherichia coli, Candida albicans, Staphylococcus epidermidis, Streptococcus pneumoniae, Staphylococcus aureus, Listeria monocytogenes, Enterococcus faecalis, and Streptococcus agalactiae [111].”
From What would it take to prove that a chronic infection is a causal agent in Alzheimer’s disease? (2025) · cites this paper as [111]
Amyloid-β protein has antimicrobial properties, specifically against Influenza A.
“Other studies showed that Amyloid-β protein has antimicrobial properties [115], specifically against Influenza A [116]”
From Cognitive decline following acute viral infections: literature review and projections for post-COVID-19 (2022) · cites this paper as [115]
Amyloid-β has been shown to act as an antimicrobial peptide that may be overproduced in an immunologic mechanism.
“Aβ has also been shown to act as an antimicrobial peptide that may be overproduced in an immunologic mechanism [115].”
From Cognitive decline following acute viral infections: literature review and projections for post-COVID-19 (2022) · cites this paper as [115]
Brain tissues from AD patients show higher anti-microbial activity than samples from age-matched non-AD individuals, correlated with Aβ levels in brain.
“brain tissues from AD patients show higher anti-microbial activity than samples from age-matched non-AD individuals, which was correlated with Aβ levels in brain.398”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [398]
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- Authors
- Soscia, S. J., Kirby, J. E., Washicosky, K. J., Tucker, S. M., Ingelsson, M., Hyman, B., Burton, M. A., Goldstein, L. E., Duong, S., Tanzi, R. E., & Moir, R. D.
- Affiliations
- Boston University (US)
- Beth Israel Deaconess Medical Center (US)
- Massachusetts General Hospital (US)
- Uppsala University (SE)
- Harvard University (US)
- Corresponding author
- Tanzi, Rudolph E.
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2010-03-03
- Volume
- 5
- Issue
- 3
- Pages
- e9505
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC2831066
- OpenAlex
- W2108629610
- Cited by
- 1,060
- References
- 85
- Citations by year
- 2026: 56 · 2025: 68 · 2024: 55 · 2023: 67 · 2022: 83 · 2021: 110 · 2020: 123 · 2019: 71 · 2018: 71 · 2017: 60 · 2016: 56 · 2015: 47 · 2014: 43 · 2013: 33 · 2012: 50
- FWCI
- 31.85
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- OpenBU (Boston University) (submittedVersion, other-oa)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI081990)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, Alzheimer's disease, antimicrobial peptides, LL-37, innate immunity, antimicrobial activity, brain homogenate
- MeSH terms
- Alzheimer Disease, Brain, Candida albicans, Cell Survival, Environment, Humans, Immunity, Innate, Inflammation, Ligands, Microbial Sensitivity Tests, Oxazines, Recombinant Proteins, Xanthenes, Amyloid beta-Peptides, Antimicrobial Cationic Peptides, Cathelicidins
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