Influence of Mabs on PrPSc Formation Using In Vitro and Cell-Free Systems
Identifieur interne : 000505 ( Pmc/Checkpoint ); précédent : 000504; suivant : 000506Influence of Mabs on PrPSc Formation Using In Vitro and Cell-Free Systems
Auteurs : Binggong Chang [États-Unis] ; Robert Petersen [États-Unis] ; Thomas Wisniewski [États-Unis] ; Richard Rubenstein [États-Unis]Source :
- PLoS ONE [ 1932-6203 ] ; 2012.
Abstract
PrPSc is believed to serve as a template for the conversion of PrPC to the abnormal isoform. This process requires contact between the two proteins and implies that there may be critical contact sites that are important for conversion. We hypothesized that antibodies binding to either PrPcor PrPSc would hinder or prevent the formation of the PrPC–PrPSc complex and thus slow down or prevent the conversion process. Two systems were used to analyze the effect of different antibodies on PrPSc formation: (i) neuroblastoma cells persistently infected with the 22L mouse-adapted scrapie stain, and (ii) protein misfolding cyclic amplification (PMCA), which uses PrPSc as a template or seed, and a series of incubations and sonications, to convert PrPC to PrPSc. The two systems yielded similar results, in most cases, and demonstrate that PrP-specific monoclonal antibodies (Mabs) vary in their ability to inhibit the PrPC–PrPSc conversion process. Based on the numerous and varied Mabs analyzed, the inhibitory effect does not appear to be epitope specific, related to PrPC conformation, or to cell membrane localization, but is influenced by the targeted PrP region (amino vs carboxy).
Url:
DOI: 10.1371/journal.pone.0041626
PubMed: 22848548
PubMed Central: 3407222
Affiliations:
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Formation Using <italic>In Vitro</italic>
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<author><name sortKey="Chang, Binggong" sort="Chang, Binggong" uniqKey="Chang B" first="Binggong" last="Chang">Binggong Chang</name>
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<wicri:regionArea>Departments of Neurology and Physiology/Pharmacology, State University New York Downstate Medical Center, Brooklyn, New York</wicri:regionArea>
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<author><name sortKey="Petersen, Robert" sort="Petersen, Robert" uniqKey="Petersen R" first="Robert" last="Petersen">Robert Petersen</name>
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<author><name sortKey="Rubenstein, Richard" sort="Rubenstein, Richard" uniqKey="Rubenstein R" first="Richard" last="Rubenstein">Richard Rubenstein</name>
<affiliation wicri:level="2"><nlm:aff id="aff1"><addr-line>Departments of Neurology and Physiology/Pharmacology, State University New York Downstate Medical Center, Brooklyn, New York, United States of America</addr-line>
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<front><div type="abstract" xml:lang="en"><p>PrP<sup>Sc</sup>
is believed to serve as a template for the conversion of PrP<sup>C</sup>
to the abnormal isoform. This process requires contact between the two proteins and implies that there may be critical contact sites that are important for conversion. We hypothesized that antibodies binding to either PrP<sup>c</sup>
or PrP<sup>Sc</sup>
would hinder or prevent the formation of the PrP<sup>C</sup>
–PrP<sup>Sc</sup>
complex and thus slow down or prevent the conversion process. Two systems were used to analyze the effect of different antibodies on PrP<sup>Sc</sup>
formation: (i) neuroblastoma cells persistently infected with the 22L mouse-adapted scrapie stain, and (ii) protein misfolding cyclic amplification (PMCA), which uses PrP<sup>Sc</sup>
as a template or seed, and a series of incubations and sonications, to convert PrP<sup>C</sup>
to PrP<sup>Sc</sup>
. The two systems yielded similar results, in most cases, and demonstrate that PrP-specific monoclonal antibodies (Mabs) vary in their ability to inhibit the PrP<sup>C</sup>
–PrP<sup>Sc</sup>
conversion process. Based on the numerous and varied Mabs analyzed, the inhibitory effect does not appear to be epitope specific, related to PrP<sup>C</sup>
conformation, or to cell membrane localization, but is influenced by the targeted PrP region (amino vs carboxy).</p>
</div>
</front>
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</TEI>
<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">PLoS One</journal-id>
<journal-id journal-id-type="iso-abbrev">PLoS ONE</journal-id>
<journal-id journal-id-type="publisher-id">plos</journal-id>
<journal-id journal-id-type="pmc">plosone</journal-id>
<journal-title-group><journal-title>PLoS ONE</journal-title>
</journal-title-group>
<issn pub-type="epub">1932-6203</issn>
<publisher><publisher-name>Public Library of Science</publisher-name>
<publisher-loc>San Francisco, USA</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">22848548</article-id>
<article-id pub-id-type="pmc">3407222</article-id>
<article-id pub-id-type="publisher-id">PONE-D-12-13547</article-id>
<article-id pub-id-type="doi">10.1371/journal.pone.0041626</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
</subj-group>
<subj-group subj-group-type="Discipline-v2"><subject>Biology</subject>
<subj-group><subject>Biochemistry</subject>
<subj-group><subject>Proteins</subject>
<subj-group><subject>Transmembrane Proteins</subject>
</subj-group>
</subj-group>
</subj-group>
<subj-group><subject>Immunology</subject>
<subj-group><subject>Immunity</subject>
<subj-group><subject>Immunotherapy</subject>
</subj-group>
</subj-group>
<subj-group><subject>Immunologic Subspecialties</subject>
<subj-group><subject>Neuroimmunology</subject>
</subj-group>
</subj-group>
<subj-group><subject>Immunoglobulins</subject>
<subject>Immunomodulation</subject>
</subj-group>
</subj-group>
<subj-group><subject>Neuroscience</subject>
</subj-group>
</subj-group>
<subj-group subj-group-type="Discipline-v2"><subject>Medicine</subject>
<subj-group><subject>Infectious Diseases</subject>
<subj-group><subject>Prion Diseases</subject>
</subj-group>
</subj-group>
<subj-group><subject>Neurology</subject>
<subj-group><subject>Infectious Diseases of the Nervous System</subject>
<subject>Neurodegenerative Diseases</subject>
</subj-group>
</subj-group>
</subj-group>
</article-categories>
<title-group><article-title>Influence of Mabs on PrP<sup>Sc</sup>
Formation Using <italic>In Vitro</italic>
and Cell-Free Systems</article-title>
<alt-title alt-title-type="running-head">Mab Effects on PrP<sup>Sc</sup>
in Cells and Cell-Free Models</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Chang</surname>
<given-names>Binggong</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Petersen</surname>
<given-names>Robert</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wisniewski</surname>
<given-names>Thomas</given-names>
</name>
<xref ref-type="aff" rid="aff3"><sup>3</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Rubenstein</surname>
<given-names>Richard</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>1</sup>
</xref>
<xref ref-type="corresp" rid="cor1"><sup>*</sup>
</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>1</label>
<addr-line>Departments of Neurology and Physiology/Pharmacology, State University New York Downstate Medical Center, Brooklyn, New York, United States of America</addr-line>
</aff>
<aff id="aff2"><label>2</label>
<addr-line>Departments of Pathology, Neuroscience, and Neurology, Case Western Reserve University, Cleveland, Ohio, United States of America</addr-line>
</aff>
<aff id="aff3"><label>3</label>
<addr-line>Departments of Neurology, Psychiatry and Pathology, New York University School of Medicine, New York, New York, United States of America</addr-line>
</aff>
<contrib-group><contrib contrib-type="editor"><name><surname>Rezaei</surname>
<given-names>Human</given-names>
</name>
<role>Editor</role>
<xref ref-type="aff" rid="edit1"></xref>
</contrib>
</contrib-group>
<aff id="edit1"><addr-line>National Institute for Agricultural Research, France</addr-line>
</aff>
<author-notes><corresp id="cor1">* E-mail: <email>richard.rubenstein@downstate.edu</email>
</corresp>
<fn fn-type="COI-statement"><p><bold>Competing Interests: </bold>
TW is a PLoS ONE Editorial Board member. This does not alter the authors’ adherence to all the PLoS ONE policies on sharing data and materials.</p>
</fn>
<fn fn-type="con"><p>Conceived and designed the experiments: RR TW. Performed the experiments: BC RP TW RR. Analyzed the data: BC RP TW RR. Contributed reagents/materials/analysis tools: RP TW RR. Wrote the paper: RR.</p>
</fn>
</author-notes>
<pub-date pub-type="collection"><year>2012</year>
</pub-date>
<pub-date pub-type="epub"><day>27</day>
<month>7</month>
<year>2012</year>
</pub-date>
<volume>7</volume>
<issue>7</issue>
<elocation-id>e41626</elocation-id>
<history><date date-type="received"><day>1</day>
<month>5</month>
<year>2012</year>
</date>
<date date-type="accepted"><day>22</day>
<month>6</month>
<year>2012</year>
</date>
</history>
<permissions><copyright-statement>© 2012 Chang et al</copyright-statement>
<copyright-year>2012</copyright-year>
<copyright-holder>Chang et al</copyright-holder>
<license xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>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 properly credited.</license-p>
</license>
</permissions>
<abstract><p>PrP<sup>Sc</sup>
is believed to serve as a template for the conversion of PrP<sup>C</sup>
to the abnormal isoform. This process requires contact between the two proteins and implies that there may be critical contact sites that are important for conversion. We hypothesized that antibodies binding to either PrP<sup>c</sup>
or PrP<sup>Sc</sup>
would hinder or prevent the formation of the PrP<sup>C</sup>
–PrP<sup>Sc</sup>
complex and thus slow down or prevent the conversion process. Two systems were used to analyze the effect of different antibodies on PrP<sup>Sc</sup>
formation: (i) neuroblastoma cells persistently infected with the 22L mouse-adapted scrapie stain, and (ii) protein misfolding cyclic amplification (PMCA), which uses PrP<sup>Sc</sup>
as a template or seed, and a series of incubations and sonications, to convert PrP<sup>C</sup>
to PrP<sup>Sc</sup>
. The two systems yielded similar results, in most cases, and demonstrate that PrP-specific monoclonal antibodies (Mabs) vary in their ability to inhibit the PrP<sup>C</sup>
–PrP<sup>Sc</sup>
conversion process. Based on the numerous and varied Mabs analyzed, the inhibitory effect does not appear to be epitope specific, related to PrP<sup>C</sup>
conformation, or to cell membrane localization, but is influenced by the targeted PrP region (amino vs carboxy).</p>
</abstract>
<funding-group><funding-statement>This work was supported in part by the State University New York Downstate Medical Center, National Institutes of Health grant NS47433 (TW) and grant NP020048 from the United States Department of Defense National Prion Research Program. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.</funding-statement>
</funding-group>
<counts><page-count count="7"></page-count>
</counts>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Ohio</li>
<li>État de New York</li>
</region>
</list>
<tree><country name="États-Unis"><region name="État de New York"><name sortKey="Chang, Binggong" sort="Chang, Binggong" uniqKey="Chang B" first="Binggong" last="Chang">Binggong Chang</name>
</region>
<name sortKey="Petersen, Robert" sort="Petersen, Robert" uniqKey="Petersen R" first="Robert" last="Petersen">Robert Petersen</name>
<name sortKey="Rubenstein, Richard" sort="Rubenstein, Richard" uniqKey="Rubenstein R" first="Richard" last="Rubenstein">Richard Rubenstein</name>
<name sortKey="Wisniewski, Thomas" sort="Wisniewski, Thomas" uniqKey="Wisniewski T" first="Thomas" last="Wisniewski">Thomas Wisniewski</name>
</country>
</tree>
</affiliations>
</record>
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