The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers

The amyloid beta-peptide (Aβ) plays a leading role in Alzheimer's disease (AD) physiopathology. Even though monomeric forms of Aβ are harmless to cells, Aβ can aggregate into β-sheet oligomers and fibrils, which are both neurotoxic. Therefore, one of the main therapeutic approaches to cure...

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Authors: Valls Comamala, Victòria, 1987-, Guivernau Almazán, Biuse, 1988-, Bonet Martínez, Jaume, 1982-, Puig, Marta, Perálvarez Marín, Alex, Palomer, Ernest, Fernàndez Busquets, Xavier, Altafaj, Xavier, Tajes Orduña, Marta, Puig-Pijoan, Albert, Vicente García, Rubén, 1978-, Oliva Miguel, Baldomero, Muñoz López, Francisco José, 1964-
Format: article
Status:Published version
Publication Date:2017
Country:España
Institution:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repository:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/33732
Online Access:http://hdl.handle.net/10230/33732
http://dx.doi.org/10.18632/oncotarget.17074
Access Level:Open access
Keyword:Alzheimer’s disease
Amyloid
Immunoglobulin
Fab
Oligomers
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spelling The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomersValls Comamala, Victòria, 1987-Guivernau Almazán, Biuse, 1988-Bonet Martínez, Jaume, 1982-Puig, MartaPerálvarez Marín, AlexPalomer, ErnestFernàndez Busquets, XavierAltafaj, XavierTajes Orduña, MartaPuig-Pijoan, AlbertVicente García, Rubén, 1978-Oliva Miguel, BaldomeroMuñoz López, Francisco José, 1964-Alzheimer’s diseaseAmyloidImmunoglobulinFabOligomersThe amyloid beta-peptide (Aβ) plays a leading role in Alzheimer's disease (AD) physiopathology. Even though monomeric forms of Aβ are harmless to cells, Aβ can aggregate into β-sheet oligomers and fibrils, which are both neurotoxic. Therefore, one of the main therapeutic approaches to cure or delay AD onset and progression is targeting Aβ aggregation. In the present study, we show that a pool of human gamma immunoglobulins (IgG) protected cortical neurons from the challenge with Aβ oligomers, as assayed by MTT reduction, caspase-3 activation and cytoskeleton integrity. In addition, we report the inhibitory effect of IgG on Aβ aggregation, as shown by Thioflavin T assay, size exclusion chromatography and atomic force microscopy. Similar results were obtained with Palivizumab, a human anti-sincitial virus antibody. In order to dissect the important domains, we cleaved the pool of human IgG with papain to obtain Fab and Fc fragments. Using these cleaved fragments, we functionally identified Fab as the immunoglobulin fragment inhibiting Aβ aggregation, a result that was further confirmed by an in silico structural model. Interestingly, bioinformatic tools show a highly conserved structure able to bind amyloid in the Fab region. Overall, our data strongly support the inhibitory effect of human IgG on Aβ aggregation and its neuroprotective role.This work was supported by the Plan Estatal de I+D+I 2013-2016 and the ISCIII-Subdirección General de Evaluación y Fomento de la Investigación (Grants PI13/00408, PI13/00135, and Miguel Servet Grant CP10/00548 to X.A.) and FEDER Funds; SAF2014-52228-R; BIO2014-57518-R and Fundació La Marató-TV3 (Nº 20140210; Nº 20134030)Impact Journals201820182017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/33732http://dx.doi.org/10.18632/oncotarget.17074reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésOncotarget. 2017 Jun 20;8(25):41154-65info:eu-repo/grantAgreement/ES/1PE/SAF2014-52228-Rinfo:eu-repo/grantAgreement/ES/1PE/BIO2014-57518-RValls-Comamala et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC-BY) (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.http://creativecommons.org/licenses/by/3.0/info:eu-repo/semantics/openAccessoai:recercat.cat:10230/337322026-05-29T05:05:01Z
dc.title.none.fl_str_mv The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
title The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
spellingShingle The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
Valls Comamala, Victòria, 1987-
Alzheimer’s disease
Amyloid
Immunoglobulin
Fab
Oligomers
title_short The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
title_full The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
title_fullStr The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
title_full_unstemmed The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
title_sort The antigen-binding fragment of human gamma immunoglobulin prevents amyloid β-peptide folding into β-sheet to form oligomers
dc.creator.none.fl_str_mv Valls Comamala, Victòria, 1987-
Guivernau Almazán, Biuse, 1988-
Bonet Martínez, Jaume, 1982-
Puig, Marta
Perálvarez Marín, Alex
Palomer, Ernest
Fernàndez Busquets, Xavier
Altafaj, Xavier
Tajes Orduña, Marta
Puig-Pijoan, Albert
Vicente García, Rubén, 1978-
Oliva Miguel, Baldomero
Muñoz López, Francisco José, 1964-
author Valls Comamala, Victòria, 1987-
author_facet Valls Comamala, Victòria, 1987-
Guivernau Almazán, Biuse, 1988-
Bonet Martínez, Jaume, 1982-
Puig, Marta
Perálvarez Marín, Alex
Palomer, Ernest
Fernàndez Busquets, Xavier
Altafaj, Xavier
Tajes Orduña, Marta
Puig-Pijoan, Albert
Vicente García, Rubén, 1978-
Oliva Miguel, Baldomero
Muñoz López, Francisco José, 1964-
author_role author
author2 Guivernau Almazán, Biuse, 1988-
Bonet Martínez, Jaume, 1982-
Puig, Marta
Perálvarez Marín, Alex
Palomer, Ernest
Fernàndez Busquets, Xavier
Altafaj, Xavier
Tajes Orduña, Marta
Puig-Pijoan, Albert
Vicente García, Rubén, 1978-
Oliva Miguel, Baldomero
Muñoz López, Francisco José, 1964-
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Alzheimer’s disease
Amyloid
Immunoglobulin
Fab
Oligomers
topic Alzheimer’s disease
Amyloid
Immunoglobulin
Fab
Oligomers
description The amyloid beta-peptide (Aβ) plays a leading role in Alzheimer's disease (AD) physiopathology. Even though monomeric forms of Aβ are harmless to cells, Aβ can aggregate into β-sheet oligomers and fibrils, which are both neurotoxic. Therefore, one of the main therapeutic approaches to cure or delay AD onset and progression is targeting Aβ aggregation. In the present study, we show that a pool of human gamma immunoglobulins (IgG) protected cortical neurons from the challenge with Aβ oligomers, as assayed by MTT reduction, caspase-3 activation and cytoskeleton integrity. In addition, we report the inhibitory effect of IgG on Aβ aggregation, as shown by Thioflavin T assay, size exclusion chromatography and atomic force microscopy. Similar results were obtained with Palivizumab, a human anti-sincitial virus antibody. In order to dissect the important domains, we cleaved the pool of human IgG with papain to obtain Fab and Fc fragments. Using these cleaved fragments, we functionally identified Fab as the immunoglobulin fragment inhibiting Aβ aggregation, a result that was further confirmed by an in silico structural model. Interestingly, bioinformatic tools show a highly conserved structure able to bind amyloid in the Fab region. Overall, our data strongly support the inhibitory effect of human IgG on Aβ aggregation and its neuroprotective role.
publishDate 2017
dc.date.none.fl_str_mv 2017
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/33732
http://dx.doi.org/10.18632/oncotarget.17074
url http://hdl.handle.net/10230/33732
http://dx.doi.org/10.18632/oncotarget.17074
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Oncotarget. 2017 Jun 20;8(25):41154-65
info:eu-repo/grantAgreement/ES/1PE/SAF2014-52228-R
info:eu-repo/grantAgreement/ES/1PE/BIO2014-57518-R
dc.rights.none.fl_str_mv http://creativecommons.org/licenses/by/3.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/3.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Impact Journals
publisher.none.fl_str_mv Impact Journals
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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