Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide

Background and Aims: Celiac disease is a permanent intolerance to gluten prolamins from wheat, barley, rye and, in some patients, oats. Partially digested gluten peptides produced in the digestive tract cause inflammation of the small intestine. High throughput, immune-based assays using monoclonal...

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Autores: Morón Flores, Belén, Bethune, Michael T., Comino Montilla, Isabel María, Manyani, Hamid, Ferragud, Marina, López, Manuel Carlos, Cebolla, Ángel, Khosla, Chaitan, Sousa Martín, Carolina
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2008
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/41963
Acceso en línea:http://hdl.handle.net/11441/41963
https://doi.org/10.1371/journal.pone.0002294
Access Level:acceso abierto
Palabra clave:Epitope
Gliadin
Gluten
Immunotoxin
Monoclonal antibody
Monoclonal antibody A1
Monoclonal antibody G12
Prolamin
Protein glutamine gamma glutamyltransferase
Recombinant protein
Synthetic peptide
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spelling Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten PeptideMorón Flores, BelénBethune, Michael T.Comino Montilla, Isabel MaríaManyani, HamidFerragud, MarinaLópez, Manuel CarlosCebolla, ÁngelKhosla, ChaitanSousa Martín, CarolinaEpitopeGliadinGlutenImmunotoxinMonoclonal antibodyMonoclonal antibody A1Monoclonal antibody G12ProlaminProtein glutamine gamma glutamyltransferaseRecombinant proteinSynthetic peptideBackground and Aims: Celiac disease is a permanent intolerance to gluten prolamins from wheat, barley, rye and, in some patients, oats. Partially digested gluten peptides produced in the digestive tract cause inflammation of the small intestine. High throughput, immune-based assays using monoclonal antibodies specific for these immunotoxic peptides would facilitate their detection in food and enable monitoring of their enzymatic detoxification. Two monoclonal antibodies, G12 and A1, were developed against a highly immunotoxic 33-mer peptide. The potential of each antibody for quantifying food toxicity for celiac patients was studied. Methods: Epitope preferences of G12 and A1 antibodies were determined by ELISA with gluten-derived peptide variants of recombinant, synthetic or enzymatic origin. Results: The recognition sequences of G12 and A1 antibodies were hexameric and heptameric epitopes, respectively. Although G12 affinity for the 33-mer was superior to A1, the sensitivity for gluten detection was higher for A1. This observation correlated to the higher number of A1 epitopes found in prolamins than G12 epitopes. Activation of T cell from gluten digested by glutenases decreased equivalently to the detection of intact peptides by A1 antibody. Peptide recognition of A1 included gliadin peptides involved in the both the adaptive and innate immunological response in celiac disease. Conclusions: The sensitivity and epitope preferences of the A1 antibody resulted to be useful to detect gluten relevant peptides to infer the potential toxicity of food for celiac patients as well as to monitor peptide modifications by transglutaminase 2 or glutenases.Public Library of ScienceMicrobiología y Parasitología2008info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/11441/41963https://doi.org/10.1371/journal.pone.0002294reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésPLoS One, 3 (5), e2294-.10.1371/journal.pone.0002294info:eu-repo/semantics/openAccessoai:idus.us.es:11441/419632026-06-17T12:51:07Z
dc.title.none.fl_str_mv Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
title Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
spellingShingle Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
Morón Flores, Belén
Epitope
Gliadin
Gluten
Immunotoxin
Monoclonal antibody
Monoclonal antibody A1
Monoclonal antibody G12
Prolamin
Protein glutamine gamma glutamyltransferase
Recombinant protein
Synthetic peptide
title_short Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
title_full Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
title_fullStr Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
title_full_unstemmed Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
title_sort Toward the Assessment of Food Toxicity for Celiac Patients: Characterization of Monoclonal Antibodies to a Main Immunogenic Gluten Peptide
dc.creator.none.fl_str_mv Morón Flores, Belén
Bethune, Michael T.
Comino Montilla, Isabel María
Manyani, Hamid
Ferragud, Marina
López, Manuel Carlos
Cebolla, Ángel
Khosla, Chaitan
Sousa Martín, Carolina
author Morón Flores, Belén
author_facet Morón Flores, Belén
Bethune, Michael T.
Comino Montilla, Isabel María
Manyani, Hamid
Ferragud, Marina
López, Manuel Carlos
Cebolla, Ángel
Khosla, Chaitan
Sousa Martín, Carolina
author_role author
author2 Bethune, Michael T.
Comino Montilla, Isabel María
Manyani, Hamid
Ferragud, Marina
López, Manuel Carlos
Cebolla, Ángel
Khosla, Chaitan
Sousa Martín, Carolina
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Microbiología y Parasitología
dc.subject.none.fl_str_mv Epitope
Gliadin
Gluten
Immunotoxin
Monoclonal antibody
Monoclonal antibody A1
Monoclonal antibody G12
Prolamin
Protein glutamine gamma glutamyltransferase
Recombinant protein
Synthetic peptide
topic Epitope
Gliadin
Gluten
Immunotoxin
Monoclonal antibody
Monoclonal antibody A1
Monoclonal antibody G12
Prolamin
Protein glutamine gamma glutamyltransferase
Recombinant protein
Synthetic peptide
description Background and Aims: Celiac disease is a permanent intolerance to gluten prolamins from wheat, barley, rye and, in some patients, oats. Partially digested gluten peptides produced in the digestive tract cause inflammation of the small intestine. High throughput, immune-based assays using monoclonal antibodies specific for these immunotoxic peptides would facilitate their detection in food and enable monitoring of their enzymatic detoxification. Two monoclonal antibodies, G12 and A1, were developed against a highly immunotoxic 33-mer peptide. The potential of each antibody for quantifying food toxicity for celiac patients was studied. Methods: Epitope preferences of G12 and A1 antibodies were determined by ELISA with gluten-derived peptide variants of recombinant, synthetic or enzymatic origin. Results: The recognition sequences of G12 and A1 antibodies were hexameric and heptameric epitopes, respectively. Although G12 affinity for the 33-mer was superior to A1, the sensitivity for gluten detection was higher for A1. This observation correlated to the higher number of A1 epitopes found in prolamins than G12 epitopes. Activation of T cell from gluten digested by glutenases decreased equivalently to the detection of intact peptides by A1 antibody. Peptide recognition of A1 included gliadin peptides involved in the both the adaptive and innate immunological response in celiac disease. Conclusions: The sensitivity and epitope preferences of the A1 antibody resulted to be useful to detect gluten relevant peptides to infer the potential toxicity of food for celiac patients as well as to monitor peptide modifications by transglutaminase 2 or glutenases.
publishDate 2008
dc.date.none.fl_str_mv 2008
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/11441/41963
https://doi.org/10.1371/journal.pone.0002294
url http://hdl.handle.net/11441/41963
https://doi.org/10.1371/journal.pone.0002294
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv PLoS One, 3 (5), e2294-.
10.1371/journal.pone.0002294
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.300724

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