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. 2021 Nov 26;9:774650. doi: 10.3389/fcell.2021.774650

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Copyright © 2021 Fouke, Wegman, Weber, Brady, Román-Vendrell and Morgan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Lamprey and human synucleins are highly conserved. (A) Multiple sequence alignment of human synuclein (α, β, γ) and lamprey γ-synuclein (GenBank (JN544525.1). Black boxes indicate amino acid residues that are identical to human α-synuclein. The N-terminal domains (gray) are the most conserved sequences amongst synucleins. The epitope of the synuclein antibody used in this study is indicated (anti-pan-synuclein, ab6176 Abcam). (B) Disorder probability of human α-synuclein and lamprey γ-synuclein are nearly identical, even though the lamprey sequence is shorter. Sequences above the 0.5 probability threshold are predicted to be disordered, while those below are structured. Graphs were generated using PrDOS. Black bar indicates the Synuclein Ab epitope. (C) The charge distributions of human α-synuclein and lamprey γ-synuclein proteins are also nearly identical. Positively- and negatively-charged residues are indicated by + 1 and−1, respectively. Plots were generated using EMBOSS. (D) The pan-synuclein antibody, which was raised against the N-terminal domain of human α-synuclein, recognizes monomeric synuclein in both rat brain and lamprey CNS lysates.