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Why does the Aβ peptide of Alzheimer share structural similarity with antimicrobial peptides?
- Source :
-
Communications biology [Commun Biol] 2020 Mar 19; Vol. 3 (1), pp. 135. Date of Electronic Publication: 2020 Mar 19. - Publication Year :
- 2020
-
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.
- Subjects :
- Alzheimer Disease immunology
Alzheimer Disease pathology
Amyloid beta-Peptides chemistry
Animals
Bacteria immunology
Bacteria pathogenicity
Brain immunology
Brain pathology
Databases, Protein
Host-Pathogen Interactions
Humans
Immunity, Innate
Models, Molecular
Peptide Fragments chemistry
Pore Forming Cytotoxic Proteins chemistry
Protein Aggregates
Protein Aggregation, Pathological
Protein Conformation
Structure-Activity Relationship
Alzheimer Disease metabolism
Amyloid beta-Peptides metabolism
Brain metabolism
Peptide Fragments metabolism
Pore Forming Cytotoxic Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2399-3642
- Volume :
- 3
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Communications biology
- Publication Type :
- Academic Journal
- Accession number :
- 32193491
- Full Text :
- https://doi.org/10.1038/s42003-020-0865-9