Alzheimerrs Disease-Associated -amyloid Is Rapidly Seeded by herpesviridae to Protect Against Brain Infection

Citation data:

SSRN Electronic Journal

Publication Year:
2017
Usage 2122
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SSRN
SSRN Id:
3155923
DOI:
10.2139/ssrn.3155923
Author(s):
William A. Eimer; Deepak Kumar Vijaya Kumar; Nanda Kumar N. Shanmugam; Kevin J. Washicosky; Alex S. Rodriguez; Bence Gyyrgy; Xandra O. Breakefield; Rudolph E. Tanzi; Robert D. Moir
Publisher(s):
Elsevier BV
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article description
Amyloid-β peptide (Aβ) fibrilization and deposition as β-amyloid is a hallmark Alzheimer's disease (AD) pathology. We recently reported Aβ is an innate immune protein and the peptides expression protects against fungal and bacterial infections in animal and cell culture models, doubling host survival in some cases. However, fibrilization pathways mediate Aβ's antimicrobial activities. Thus, infection can dramatically accelerate β- amyloid deposition. Here, we show herpesvirus glycoprotein B binding induces Aβ fibrillization, mediating protective activities against neurotropic herpes simplex virus 1 (HSV1) and human herpesvirus 6 (HHV6). Moreover, herpesviridae infection rapidly seed plaque deposition in 5XFAD mice and 3-dimensional human neural cell cultures. The accompanying paper by Readhead et al. show AD progression correlates with increased abundance of HSV1, HHV6, and herpesvirus 7 across multiple brain regions. Our findings, together with those of Readhead et al., provide a novel etiological mechanism for AD, in which infection with herpesviridae may promote Aβ-amyloidosis.