An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials
Identifieur interne : 000142 ( Pmc/Curation ); précédent : 000141; suivant : 000143An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials
Auteurs : Luc Bousset [France] ; Patrik Brundin [États-Unis] ; Anja Böckmann [France] ; Beat Meier [Suisse] ; Ronald Melki [France]Source :
- Journal of Parkinson's Disease [ 1877-7171 ] ; ????.
Abstract
Url:
DOI: 10.3233/JPD-150691
PubMed: 26639448
PubMed Central: 4927840
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<author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
<affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Paris-Saclay Institute of Neurosciences</institution>
, CNRS, Gif-sur-Yvette,<country>France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Brundin, Patrik" sort="Brundin, Patrik" uniqKey="Brundin P" first="Patrik" last="Brundin">Patrik Brundin</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"> Van Andel Research Institute,<institution>Center for Neurodegenerative Science</institution>
, Grand Rapids, Michigan,<country>USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Bockmann, Anja" sort="Bockmann, Anja" uniqKey="Bockmann A" first="Anja" last="Böckmann">Anja Böckmann</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Institut de Biologie et Chimie des Proteines,<institution>CNRS/Université de Lyon 1</institution>
, Lyon,<country>France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Meier, Beat" sort="Meier, Beat" uniqKey="Meier B" first="Beat" last="Meier">Beat Meier</name>
<affiliation wicri:level="1"><nlm:aff id="aff4"><institution>Physical Chemistry</institution>
, ETH Zurich, Zurich,<country>Switzerland</country>
</nlm:aff>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name>
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, CNRS, Gif-sur-Yvette,<country>France</country>
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<country xml:lang="fr">France</country>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials</title>
<author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
<affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Paris-Saclay Institute of Neurosciences</institution>
, CNRS, Gif-sur-Yvette,<country>France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Brundin, Patrik" sort="Brundin, Patrik" uniqKey="Brundin P" first="Patrik" last="Brundin">Patrik Brundin</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"> Van Andel Research Institute,<institution>Center for Neurodegenerative Science</institution>
, Grand Rapids, Michigan,<country>USA</country>
</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Bockmann, Anja" sort="Bockmann, Anja" uniqKey="Bockmann A" first="Anja" last="Böckmann">Anja Böckmann</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Institut de Biologie et Chimie des Proteines,<institution>CNRS/Université de Lyon 1</institution>
, Lyon,<country>France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Meier, Beat" sort="Meier, Beat" uniqKey="Meier B" first="Beat" last="Meier">Beat Meier</name>
<affiliation wicri:level="1"><nlm:aff id="aff4"><institution>Physical Chemistry</institution>
, ETH Zurich, Zurich,<country>Switzerland</country>
</nlm:aff>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
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<author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name>
<affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Paris-Saclay Institute of Neurosciences</institution>
, CNRS, Gif-sur-Yvette,<country>France</country>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
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<series><title level="j">Journal of Parkinson's Disease</title>
<idno type="ISSN">1877-7171</idno>
<idno type="eISSN">1877-718X</idno>
<imprint><date when="????">????</date>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
Preformed α-synuclein fibrils seed the aggregation of soluble α-synuclein in cultured cells and <italic>in vivo</italic>
. This, and other findings, has kindled the idea that α-synuclein fibrils possess prion-like properties.</p>
<p><bold>Objective:</bold>
As α-synuclein fibrils should not be considered as innocuous, there is a need for decontamination and inactivation procedures for laboratory benches and non-disposable laboratory material.</p>
<p><bold>Methods:</bold>
We assessed the effectiveness of different procedures designed to disassemble α-synuclein fibrils and reduce their infectivity. We examined different commercially available detergents to remove α-synuclein assemblies adsorbed on materials that are not disposable and that are most found in laboratories (e.g. plastic, glass, aluminum or stainless steel surfaces).</p>
<p><bold>Results:</bold>
We show that methods designed to decrease PrP prion infectivity neither effectively remove α-synuclein assemblies adsorbed to different materials commonly used in the laboratory nor disassemble the fibrillar form of the protein with efficiency. In contrast, both commercial detergents and SDS detached α-synuclein assemblies from contaminated surfaces and disassembled the fibrils.</p>
<p><bold>Conclusions:</bold>
We describe three cleaning procedures that effectively remove and disassemble α-synuclein seeds. The methods rely on the use of detergents that are compatible with most non-disposable tools in a laboratory. The procedures are easy to implement and significantly decrease any potential risks associated to handling α-synuclein assemblies.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Parkinsons Dis</journal-id>
<journal-id journal-id-type="iso-abbrev">J Parkinsons Dis</journal-id>
<journal-id journal-id-type="publisher-id">JPD</journal-id>
<journal-title-group><journal-title>Journal of Parkinson's Disease</journal-title>
</journal-title-group>
<issn pub-type="ppub">1877-7171</issn>
<issn pub-type="epub">1877-718X</issn>
<issn-l>1877-7171</issn-l>
<publisher><publisher-name>IOS Press</publisher-name>
<publisher-loc>Nieuwe Hemweg 6B, 1013 BG Amsterdam, The Netherlands</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">26639448</article-id>
<article-id pub-id-type="pmc">4927840</article-id>
<article-id pub-id-type="publisher-id">JPD150691</article-id>
<article-id pub-id-type="doi">10.3233/JPD-150691</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Report</subject>
</subj-group>
</article-categories>
<title-group><article-title>An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials</article-title>
<alt-title alt-title-type="left-running-head">L. Bousset et al.</alt-title>
<alt-title alt-title-type="right-running-head">Inactivation of Preformed α-Synuclein Fibrils</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Bousset</surname>
<given-names>Luc</given-names>
</name>
<xref ref-type="aff" rid="aff1">a</xref>
<xref ref-type="corresp" rid="cor1">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Brundin</surname>
<given-names>Patrik</given-names>
</name>
<xref ref-type="aff" rid="aff2">b</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Böckmann</surname>
<given-names>Anja</given-names>
</name>
<xref ref-type="aff" rid="aff3">c</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Meier</surname>
<given-names>Beat</given-names>
</name>
<xref ref-type="aff" rid="aff4">d</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Melki</surname>
<given-names>Ronald</given-names>
</name>
<xref ref-type="aff" rid="aff1">a</xref>
</contrib>
<aff id="aff1"><label>a</label>
<institution>Paris-Saclay Institute of Neurosciences</institution>
, CNRS, Gif-sur-Yvette,<country>France</country>
</aff>
<aff id="aff2"><label>b</label>
Van Andel Research Institute,<institution>Center for Neurodegenerative Science</institution>
, Grand Rapids, Michigan,<country>USA</country>
</aff>
<aff id="aff3"><label>c</label>
Institut de Biologie et Chimie des Proteines,<institution>CNRS/Université de Lyon 1</institution>
, Lyon,<country>France</country>
</aff>
<aff id="aff4"><label>d</label>
<institution>Physical Chemistry</institution>
, ETH Zurich, Zurich,<country>Switzerland</country>
</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>*</label>
Correspondence to: Luc Bousset, Paris-Saclay Institute of Neurosciences, CNRS, 91190 Gif-sur-Yvette, FranceTel.: +33169823479; Fax: +33169824111; E-mail: <email>luc.bousset@inaf.cnrs-gif.fr</email>
.</corresp>
</author-notes>
<pub-date date-type="preprint" publication-format="electronic"><day>30</day>
<month>11</month>
<year>2015</year>
</pub-date>
<pub-date date-type="pub" publication-format="electronic"><day>30</day>
<month>3</month>
<year>2016</year>
</pub-date>
<pub-date date-type="collection" publication-format="electronic"><year>2016</year>
</pub-date>
<volume>6</volume>
<issue>1</issue>
<fpage>143</fpage>
<lpage>151</lpage>
<permissions><copyright-statement>IOS Press and the authors. All rights reserved</copyright-statement>
<copyright-year>2016</copyright-year>
<license xlink:href="https://creativecommons.org/licenses/by-nc/4.0/" license-type="open-access"><license-p>This is an open access article distributed under the terms of the <ext-link ext-link-type="uri" xlink:href="https://creativecommons.org/licenses/by-nc/4.0/">Creative Commons Attribution Non-Commercial (CC BY-NC 4.0) License</ext-link>
, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p>
</license>
</permissions>
<abstract><p><bold>Background:</bold>
Preformed α-synuclein fibrils seed the aggregation of soluble α-synuclein in cultured cells and <italic>in vivo</italic>
. This, and other findings, has kindled the idea that α-synuclein fibrils possess prion-like properties.</p>
<p><bold>Objective:</bold>
As α-synuclein fibrils should not be considered as innocuous, there is a need for decontamination and inactivation procedures for laboratory benches and non-disposable laboratory material.</p>
<p><bold>Methods:</bold>
We assessed the effectiveness of different procedures designed to disassemble α-synuclein fibrils and reduce their infectivity. We examined different commercially available detergents to remove α-synuclein assemblies adsorbed on materials that are not disposable and that are most found in laboratories (e.g. plastic, glass, aluminum or stainless steel surfaces).</p>
<p><bold>Results:</bold>
We show that methods designed to decrease PrP prion infectivity neither effectively remove α-synuclein assemblies adsorbed to different materials commonly used in the laboratory nor disassemble the fibrillar form of the protein with efficiency. In contrast, both commercial detergents and SDS detached α-synuclein assemblies from contaminated surfaces and disassembled the fibrils.</p>
<p><bold>Conclusions:</bold>
We describe three cleaning procedures that effectively remove and disassemble α-synuclein seeds. The methods rely on the use of detergents that are compatible with most non-disposable tools in a laboratory. The procedures are easy to implement and significantly decrease any potential risks associated to handling α-synuclein assemblies.</p>
</abstract>
<kwd-group><label>Keywords</label>
<kwd>Alpha synuclein</kwd>
<kwd>cleaning procedures</kwd>
<kwd>detergent</kwd>
<kwd>fibrils</kwd>
<kwd>inactivation</kwd>
<kwd>Parkinson’s disease</kwd>
<kwd>removal</kwd>
</kwd-group>
</article-meta>
</front>
<floats-group><fig id="jpd-6-jpd150691-g001" orientation="portrait" position="float"><label>Fig.1</label>
<caption><p>Efficiency of different cleaning solutions
to remove α-Syn assemblies from different surfaces. Quantification of the remaining Atto-550 labeled
oligomeric, <bold>A</bold>
, α-Syn fibrils, <bold>B</bold>
and α-Syn ribbons, <bold>C</bold>
, spotted and dried on plastic, glass,
aluminum and stainless steel surfaces, previously scraped with sandpaper, using a fluorescence imager after
cleaning with the different solutions. Error bars represent standard error (SE) (<italic>n</italic>
= 4 independent
measurements) performed in quadruplicates. The measured fluorescence data from imaging are presented as
averages±standard error in <xref ref-type="supplementary-material" rid="S2">Supplementary Table 1</xref>
, panels A, B, C and C’.</p>
</caption>
<graphic xlink:href="jpd-6-jpd150691-g001"></graphic>
</fig>
<fig id="jpd-6-jpd150691-g002" orientation="portrait" position="float"><label>Fig.2</label>
<caption><p>Quantitative assessment of the fraction of
fibrillar α-Syn solubilized in the different cleaning solutions. The fraction (%) of α-Syn
fibrils, <bold>A</bold>
and ribbons, <bold>B</bold>
, that becomes soluble relative to the initial total amount of fibrillar α-Syn
in the cleaning solution was determined following ultracentrifugation by measurement of the absorbance of
fluorescently labeled α-Syn in the supernatant fraction as described in the material and methods
section. Error bars represent standard error (SE) (<italic>n</italic>
= 4 independent measurements) performed in
quadruplicates. The measured absorbance data are presented as averages±standard error in <xref ref-type="supplementary-material" rid="S2">Supplementary Table 1</xref>
, panels D and E.</p>
</caption>
<graphic xlink:href="jpd-6-jpd150691-g002"></graphic>
</fig>
<table-wrap id="jpd-6-jpd150691-t001" orientation="portrait" position="float"><label>Table 1</label>
<caption><p>Laboratory Standard Operating Procedures for fibrillar α-synuclein</p>
</caption>
<table frame="hsides" rules="groups"><thead valign="top"><tr><td rowspan="1" colspan="1">Recommendations:</td>
</tr>
<tr><td rowspan="1" colspan="1">Step</td>
<td rowspan="1" colspan="1">Do</td>
<td rowspan="1" colspan="1">Do NOT</td>
</tr>
</thead>
<tbody><tr><td rowspan="1" colspan="1">General</td>
<td rowspan="1" colspan="1">Use appropriate personal protective equipment:</td>
<td rowspan="1" colspan="1">- Eat or drink in an environment where α-Syn fibrils are used</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Laboratory coat</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Gloves</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Goggles / safety glasses</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Mechanical filter respirators such as FFP2 particulate respirator mask,</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">brand 3M ref #8822</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Prefer disposable supplies</td>
</tr>
<tr><td rowspan="1" colspan="1">Purification</td>
<td rowspan="1" colspan="1">- Keep the concentration of α-Syn below 1 mM</td>
<td rowspan="1" colspan="1">- Concentrate α-Syn above 1 mM</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Maintain pH > 6.5 to avoid spontaneous assembly</td>
<td rowspan="1" colspan="1">- Sonicate continuously α-Syn solution above 5 min</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Aliquot α-Syn upon purification (1 to 5 mg per fraction)</td>
</tr>
<tr><td rowspan="1" colspan="1">Fibrillization</td>
<td rowspan="1" colspan="1">- Use the minimal amount of α-Syn needed for the experiment</td>
<td rowspan="1" colspan="1">- Sonicate in open containers. This generates aerosol containing α-Syn fibrils that conceivably might reach the brain through the olfactory epithelium following inhalation</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Assemble in sealed tubes</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Sonicate in closed/sealed tubes using appropriated apparatus such VialTweeter or cup-horn sonotrode</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Operate under a PSM2 if working with open tubes/vials</td>
</tr>
<tr><td rowspan="1" colspan="1">Storage</td>
<td rowspan="1" colspan="1">- Keep fibrils in closed tubes and discard in biohazard container immediately after use</td>
<td rowspan="1" colspan="1">- Do not dry the fibrils on any surfaces, as this renders them more resistant to detergent solubilization / inactivation</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Keep α-Syn fibrils in solution</td>
</tr>
<tr><td rowspan="1" colspan="1">Inactivation</td>
<td rowspan="1" colspan="1">- Inactivate samples and contaminated surfaces with 1% SDS (W/V) or commercial inactivation solutions for 1 hours at room temperature</td>
<td rowspan="1" colspan="1">- Do not use NaOH or Sodium Hypochlorite</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">- Discard inactivated samples with limited volume (e.g. less than 100 l) in Biohazard waste container</td>
</tr>
</tbody>
</table>
<table frame="hsides" rules="groups"><thead valign="top"><tr><td rowspan="1" colspan="1">Recommendations:</td>
</tr>
<tr><td colspan="2" align="left" rowspan="1">α-Syn waste</td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">inactivation</td>
</tr>
</thead>
<tbody><tr><td colspan="2" align="left" rowspan="1">α-Syn fibril in solution</td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">Dilute the solution 10 folds in inactivation solution</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">Incubate 1 h at room temperature</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">Discard in biohazard waste</td>
</tr>
<tr><td colspan="2" align="left" rowspan="1">Contaminated surfaces with α-Syn fibril</td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">Immerse completely in inactivation solution</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">Incubate 1 h at room temperature under gentle shaking</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">Rinse with water</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">Discard inactivation solution in biohazard waste</td>
</tr>
<tr><td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1"></td>
<td rowspan="1" colspan="1">If the surface is a bench, wipe with inactivation solution, discard tissues in solid biohazard waste</td>
</tr>
</tbody>
</table>
</table-wrap>
</floats-group>
</pmc>
</record>
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