Figures
A prion-inhibition Nanobody, Nb484, does not induce neurotoxicity in organotypic cultured slice
Anti-PrP monoclonal antibody POM1, which binds to a discontinuous epitope of the C-terminal globular domain of mouse PrP, induces strong neurotoxicity in mice and cerebellar organotypic cultured slices. A cultured cerebellar organotypic cultured slice from tga20 transgenic mice remains healthy after being treated with Nb484, a Nanobody that inhibits prion propagation through binding to both the hydrophobic region and C-terminal domain of PrP, which highlights the great therapeutic potential of Nb484. Abskharon et al.
Image Credit: J Ruan, and R Abskharon (2019)
Citation: (2020) PLoS Pathogens Issue Image | Vol. 15(12) January 2020. PLoS Pathog 15(12): ev15.i12. https://doi.org/10.1371/image.ppat.v15.i12
Published: January 6, 2020
Copyright: © 2020 . This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Anti-PrP monoclonal antibody POM1, which binds to a discontinuous epitope of the C-terminal globular domain of mouse PrP, induces strong neurotoxicity in mice and cerebellar organotypic cultured slices. A cultured cerebellar organotypic cultured slice from tga20 transgenic mice remains healthy after being treated with Nb484, a Nanobody that inhibits prion propagation through binding to both the hydrophobic region and C-terminal domain of PrP, which highlights the great therapeutic potential of Nb484. Abskharon et al.
Image Credit: J Ruan, and R Abskharon (2019)