Identification of human α-synuclein specific single chain antibodies

Parkinson’s disease (PD) is a common neurodegenerative disease of unknown etiology. Evidence suggests a role for protein misfolding in disease pathogenesis. One pathologic feature observed in dopaminergic neurons is the intracytoplasmic eosinophilic inclusions known as Lewy bodies. One component of...

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Veröffentlicht in:Biochemical and biophysical research communications 2006-11, Vol.349 (4), p.1198-1205
Hauptverfasser: Maguire-Zeiss, Kathleen A., Wang, Charlotte I., Yehling, Eric, Sullivan, Mark A., Short, Douglas W., Su, Xiaomin, Gouzer, Geraldine, Henricksen, Leigh A., Wuertzer, Charles A., Federoff, Howard J.
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Sprache:eng
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Zusammenfassung:Parkinson’s disease (PD) is a common neurodegenerative disease of unknown etiology. Evidence suggests a role for protein misfolding in disease pathogenesis. One pathologic feature observed in dopaminergic neurons is the intracytoplasmic eosinophilic inclusions known as Lewy bodies. One component of Lewy bodies, the presynaptic protein, α-synuclein forms oligomers and higher order aggregates and is proposed to be involved in dopaminergic neuronal death. In an effort to discriminate between α-synuclein conformational forms as well as design potential disruptors of pathogenic misfolding we panned a human phage antibody library for anti-synuclein single chain antibodies (scFvs). We identified six scFvs which recognize different conformers of α-synuclein in both an ELISA and Western blot analysis. These scFvs may further our understanding of α-synuclein’s role in PD.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.08.127