A novel panel of α-synuclein antibodies reveal distinctive staining profiles in synucleinopathies.

Bibliographic Details
Title: A novel panel of α-synuclein antibodies reveal distinctive staining profiles in synucleinopathies.
Authors: Jess-Karan S Dhillon, Cara Riffe, Brenda D Moore, Yong Ran, Paramita Chakrabarty, Todd E Golde, Benoit I Giasson
Source: PLoS ONE, Vol 12, Iss 9, p e0184731 (2017)
Publisher Information: Public Library of Science (PLoS), 2017.
Publication Year: 2017
Collection: LCC:Medicine
LCC:Science
Subject Terms: Medicine, Science
More Details: Synucleinopathies are a spectrum of neurodegenerative diseases characterized by the intracellular deposition of the protein α-synuclein leading to multiple outcomes, including dementia and Parkinsonism. Recent findings support the notion that across the spectrum of synucleinopathies there exist diverse but specific biochemical modifications and/or structural conformations of α-synuclein, which would give rise to protein strain specific prion-like intercellular transmission, a proposed model that could explain synucleinopathies disease progression. Herein, we characterized a panel of antibodies with epitopes within both the C- and N- termini of α-synuclein. A comprehensive analysis of human pathological tissue and mouse models of synucleinopathy with these antibodies support the notion that α-synuclein exists in distinct modified forms and/or structural variants. Furthermore, these well-characterized and specific tools allow the investigation of biochemical changes associated with α-synuclein inclusion formation. We have identified several antibodies of interest with diverse staining and epitope properties that will prove useful in future investigations of strain specific disease progression and the development of targeted immunotherapeutic approaches to synucleinopathies.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1932-6203
Relation: https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0184731&type=printable; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0184731&type=printable
DOI: 10.1371/journal.pone.0184731
Access URL: https://doaj.org/article/bfe68da14bd048068f6cc63c309e977b
Accession Number: edsdoj.bfe68da14bd048068f6cc63c309e977b
Database: Directory of Open Access Journals
More Details
ISSN:19326203
DOI:10.1371/journal.pone.0184731&type=printable
Published in:PLoS ONE
Language:English