Abstract
α-synuclein fibrillar polymorphs, Tau and Aß 1–42 fibrillar assemblies have been shown to propagate, amplify and trigger the formation of protein deposits reminiscent of those present within the central nervous system of patients developing synucleinopathies, tauopathies and amyloid plaques after injection intracerebrally, intramuscularly, intraperitoneally or within the blood stream of model animals. They are thus hazardous and there is need for decontamination and inactivation procedures for laboratory surfaces and non-disposable material. We assessed the effectiveness of different reagents to clean and disassemble potentially pathogenic assemblies adsorbed on non-disposable materials in laboratories. We show that commercial detergents and SDS are way more suited to detach α-synuclein fibrillar polymorphs, Tau and Aß 1–42 fibrillar assemblies from contaminated surfaces and disassemble the fibrils than methods designed to decrease PrP prion infectivity. Our observations reveal that the choice of the most adapted cleaning procedure for one given protein assembly or fibrillar polymorph should integrate detergent’s cleaning efficiency, material compatibility and capacity to dismantle assemblies. We provide an integrated representation where desorption and neutralization efficacy and surface compatibility are combined to facilitate the choice of the most adapted decontamination procedure. This representation, together with good laboratory practices, contributes to reducing potential health hazards associated to manipulating protein assemblies with prion-like properties.
Highlights
IntroductionThey are hazardous and there is need for decontamination and inactivation procedures for laboratory surfaces and non-disposable material
This is certainly due to the fact that protein particles, made of different proteins, have distinct properties
We show here that the cleaning procedure efficiency depends on the nature of the protein assembly and on the structural characteristics of distinct assemblies made of one given protein e.g. polymorphs
Summary
They are hazardous and there is need for decontamination and inactivation procedures for laboratory surfaces and non-disposable material. The monomeric forms of α-Syn, Tau and Aß1–42 form in vitro under physiological pH and salt conditions a continuum of oligomeric assemblies ranging from low to high molecular weight protein particles, the largest of which have fibrillar shape2 These assemblies, have been shown to propagate, amplify and trigger the formation of protein deposits reminiscent of those present within the central nervous system of patients developing synucleinopathies, tauopathies and amyloid plaques after their take up by cultured cells and/or upon injection within the central nervous system of model animals. We evaluated in a quantitative manner the protein assemblies disassembling propensities of those cleaning procedures
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