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Alzheimer's Disease-Associated ?-Amyloid Is Rapidly Seeded by Herpesviridae to Protect against Brain Infection.

ABSTRACT: Amyloid-? peptide (A?) fibrilization and deposition as ?-amyloid are hallmarks of Alzheimer's disease (AD) pathology. We recently reported A? is an innate immune protein that protects against fungal and bacterial infections. Fibrilization pathways mediate A? antimicrobial activities. Thus, infection can seed and dramatically accelerate ?-amyloid deposition. Here, we show A? oligomers bind herpesvirus surface glycoproteins, accelerating ?-amyloid deposition and leading to protective viral entrapment activity in 5XFAD mouse and 3D human neural cell culture infection models against neurotropic herpes simplex virus 1 (HSV1) and human herpesvirus 6A and B. Herpesviridae are linked to AD, but it has been unclear how viruses may induce ?-amyloidosis in brain. These data support the notion that A? might play a protective role in CNS innate immunity, and suggest an AD etiological mechanism in which herpesviridae infection may directly promote A? amyloidosis.

SUBMITTER: Eimer WA 

PROVIDER: S-EPMC6075814 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

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Amyloid-β peptide (Aβ) fibrilization and deposition as β-amyloid are hallmarks of Alzheimer's disease (AD) pathology. We recently reported Aβ is an innate immune protein that protects against fungal and bacterial infections. Fibrilization pathways mediate Aβ antimicrobial activities. Thus, infection can seed and dramatically accelerate β-amyloid deposition. Here, we show Aβ oligomers bind herpesvirus surface glycoproteins, accelerating β-amyloid deposition and leading to protective viral entrapm  ...[more]

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