Modulation of Amyloid-β Aggregation by Surface Proteins from Pathogens Associated with Alzheimer's Disease
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F25%3A00639190" target="_blank" >RIV/60077344:_____/25:00639190 - isvavai.cz</a>
Alternative codes found
RIV/00159816:_____/25:00082334 RIV/00216224:14310/25:00142063 RIV/00027162:_____/25:N0000090
Result on the web
<a href="https://doi.org/10.1021/acschemneuro.5c00444" target="_blank" >https://doi.org/10.1021/acschemneuro.5c00444</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acschemneuro.5c00444" target="_blank" >10.1021/acschemneuro.5c00444</a>
Alternative languages
Result language
angličtina
Original language name
Modulation of Amyloid-β Aggregation by Surface Proteins from Pathogens Associated with Alzheimer's Disease
Original language description
Alzheimer's disease (AD) is a prevalent neurodegenerative disorder. Despite substantial research efforts, our understanding of its pathogenesis remains incomplete, limiting the development of effective treatments and preventive strategies. The potential role of microbial pathogens in AD etiology has gained increasing attention. Various human microbial pathogens have been identified in the brains of AD patients, leading to the pathogen hypothesis, which posits that these microorganisms may disrupt the brain's immune regulation and homeostasis. In this study, we examine the effects of proteins from three pathogens, Borrelia burgdorferi, HSV-1, and Porphyromonas gingivalis, on the aggregation of antimicrobial peptide amyloid-beta (A beta). Three of the four studied proteins were found to attenuate the aggregation of A beta 42 by interacting with its soluble form and inhibiting primary and secondary pathways. These in vitro findings were further supported by experiments using mature neurons derived from human pluripotent stem cells, which showed an increased accumulation of amyloid precursor protein (APP) aggregates upon infection with HSV-1 or exposure to the OspA surface protein from B. burgdorferi. Together, our results provide mechanistic insights into how pathogen-associated proteins modulate A beta 42 aggregation, contributing to an understanding of their potential role in AD pathogenesis.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ACS Chemical Neuroscience
ISSN
1948-7193
e-ISSN
1948-7193
Volume of the periodical
16
Issue of the periodical within the volume
18
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
3554-3566
UT code for WoS article
001559032300001
EID of the result in the Scopus database
2-s2.0-105016491011