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β-Amyloid peptides display protective activity against the human Alzheimer’s disease-associated herpes simplex virus-1
- 作者:Karine Bourgade ; Hugo Garneau ; Geneviève Giroux ; Aurélie Y. Le Page…
- 关键词:Beta ; amyloid peptides ; Herpes simplex virus ; 1 ; Human adenovirus type 5 ; Viral replication inhibition ; Antimicrobial peptides ; Alzheimer’s disease
- 刊名:Biogerontology
- 出版年:2015
- 出版时间:February 2015
- 年:2015
- 卷:16
- 期:1
- 页码:85-98
- 全文大小:442 KB
- 参考文献:1. Akhtar J, Shukla D (2009) Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry. FEBS J 276:7228-236 CrossRef
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1. Research Center on Aging, Graduate Program in Immunology, Faculty of Medicine and Health Sciences, University of Sherbrooke, 3001, 12th Avenue North, Sherbrooke, QC, J1H 5N4, Canada 2. Department of Microbiology and Infectious Diseases, Faculty of Medicine and Health Sciences, University of Sherbrooke, Sherbrooke, QC, Canada 3. Department of Medicine, Faculty of Medicine and Health Sciences, University of Sherbrooke, Sherbrooke, QC, Canada 4. Department of Biochemistry, Graduate Program in Immunology, Faculty of Medicine and Health Sciences, University of Sherbrooke, Sherbrooke, QC, Canada
- 刊物类别:Biomedical and Life Sciences
- 刊物主题:Life Sciences
Cell Biology Geriatrics and Gerontology Developmental Biology
- 出版者:Springer Netherlands
- ISSN:1573-6768
文摘
Amyloid plaques, the hallmark of Alzheimer’s disease (AD), contain fibrillar β-amyloid (Aβ) 1-40 and 1-42 peptides. Herpes simplex virus 1 (HSV-1) has been implicated as a risk factor for AD and found to co-localize within amyloid plaques. Aβ 1-40 and Aβ 1-42 display anti-bacterial, anti-yeast and anti-viral activities. Here, fibroblast, epithelial and neuronal cell lines were exposed to Aβ 1-40 or Aβ 1-42 and challenged with HSV-1. Quantitative analysis revealed that Aβ 1-40 and Aβ 1-42 inhibited HSV-1 replication when added 2?h prior to or concomitantly with virus challenge, but not when added 2 or 6?h after virus addition. In contrast, Aβ 1-40 and Aβ 1-42 did not prevent replication of the non-enveloped human adenovirus. In comparison, antimicrobial peptide LL-37 prevented HSV-1 infection independently of its sequence of addition. Our findings showed also that Aβ 1-40 and Aβ 1-42 acted directly on HSV-1 in a cell-free system and prevented viral entry into cells. The sequence homology between Aβ and a proximal transmembrane region of HSV-1 glycoprotein B suggested that Aβ interference with HSV-1 replication could involve its insertion into the HSV-1 envelope. Our data suggest that Aβ peptides represent a novel class of antimicrobial peptides that protect against neurotropic enveloped virus infections such as HSV-1. Overproduction of Aβ peptide to protect against latent herpes viruses and eventually against other infections, may contribute to amyloid plaque formation, and partially explain why brain infections play a pathogenic role in the progression of the sporadic form of AD.
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