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Monitoring the interactions between alpha-synuclein and Tau in vitro and in vivo using bimolecular fluorescence complementation

Torres-Garcia, Laura LU ; Domingues, Joana M. P. ; Brandi, Edoardo LU ; Haikal, Caroline LU ; Mudannayake, Janitha M. LU orcid ; Brás, Inês C. ; Gerhardt, Ellen ; Li, Wen LU ; Svanbergsson, Alexander LU orcid and Outeiro, Tiago F. , et al. (2022) In Scientific Reports 12. p.1-11
Abstract

Parkinson’s disease (PD) and Alzheimer’s disease (AD) are characterized by pathological accumulation and aggregation of different amyloidogenic proteins, α-synuclein (aSyn) in PD, and amyloid-β (Aβ) and Tau in AD. Strikingly, few PD and AD patients’ brains exhibit pure pathology with most cases presenting mixed types of protein deposits in the brain. Bimolecular fluorescence complementation (BiFC) is a technique based on the complementation of two halves of a fluorescent protein, which allows direct visualization of protein–protein interactions. In the present study, we assessed the ability of aSyn and Tau to interact with each other. For in vitro evaluation, HEK293 and human neuroblastoma cells were used, while in vivo studies were... (More)

Parkinson’s disease (PD) and Alzheimer’s disease (AD) are characterized by pathological accumulation and aggregation of different amyloidogenic proteins, α-synuclein (aSyn) in PD, and amyloid-β (Aβ) and Tau in AD. Strikingly, few PD and AD patients’ brains exhibit pure pathology with most cases presenting mixed types of protein deposits in the brain. Bimolecular fluorescence complementation (BiFC) is a technique based on the complementation of two halves of a fluorescent protein, which allows direct visualization of protein–protein interactions. In the present study, we assessed the ability of aSyn and Tau to interact with each other. For in vitro evaluation, HEK293 and human neuroblastoma cells were used, while in vivo studies were performed by AAV6 injection in the substantia nigra pars compacta (SNpc) of mice and rats. We observed that the co-expression of aSyn and Tau led to the emergence of fluorescence, reflecting the interaction of the proteins in cell lines, as well as in mouse and rat SNpc. Thus, our data indicates that aSyn and Tau are able to interact with each other in a biologically relevant context, and that the BiFC assay is an effective tool for studying aSyn-Tau interactions in vitro and in different rodent models in vivo.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scientific Reports
volume
12
article number
2987
pages
1 - 11
publisher
Nature Publishing Group
external identifiers
  • scopus:85125155172
  • pmid:35194057
ISSN
2045-2322
DOI
10.1038/s41598-022-06846-9
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2022, The Author(s).
id
632a07b8-3f33-4b73-b2ca-b11c480f3093
date added to LUP
2022-03-07 13:47:07
date last changed
2024-04-12 09:51:48
@article{632a07b8-3f33-4b73-b2ca-b11c480f3093,
  abstract     = {{<p>Parkinson’s disease (PD) and Alzheimer’s disease (AD) are characterized by pathological accumulation and aggregation of different amyloidogenic proteins, α-synuclein (aSyn) in PD, and amyloid-β (Aβ) and Tau in AD. Strikingly, few PD and AD patients’ brains exhibit pure pathology with most cases presenting mixed types of protein deposits in the brain. Bimolecular fluorescence complementation (BiFC) is a technique based on the complementation of two halves of a fluorescent protein, which allows direct visualization of protein–protein interactions. In the present study, we assessed the ability of aSyn and Tau to interact with each other. For in vitro evaluation, HEK293 and human neuroblastoma cells were used, while in vivo studies were performed by AAV6 injection in the substantia nigra pars compacta (SNpc) of mice and rats. We observed that the co-expression of aSyn and Tau led to the emergence of fluorescence, reflecting the interaction of the proteins in cell lines, as well as in mouse and rat SNpc. Thus, our data indicates that aSyn and Tau are able to interact with each other in a biologically relevant context, and that the BiFC assay is an effective tool for studying aSyn-Tau interactions in vitro and in different rodent models in vivo.</p>}},
  author       = {{Torres-Garcia, Laura and Domingues, Joana M. P. and Brandi, Edoardo and Haikal, Caroline and Mudannayake, Janitha M. and Brás, Inês C. and Gerhardt, Ellen and Li, Wen and Svanbergsson, Alexander and Outeiro, Tiago F. and Gouras, Gunnar K. and Li, Jia Yi}},
  issn         = {{2045-2322}},
  language     = {{eng}},
  pages        = {{1--11}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Scientific Reports}},
  title        = {{Monitoring the interactions between alpha-synuclein and Tau in vitro and in vivo using bimolecular fluorescence complementation}},
  url          = {{http://dx.doi.org/10.1038/s41598-022-06846-9}},
  doi          = {{10.1038/s41598-022-06846-9}},
  volume       = {{12}},
  year         = {{2022}},
}