Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen

Detalhes bibliográficos
Autor(a) principal: Bobes, Raúl J.
Data de Publicação: 2017
Outros Autores: Navarrete-Perea, José, Ochoa-Leyva, Adrián, Anaya, Víctor Hugo, Hernández, Marisela, Cervantes-Torres, Jacquelynne, Estrada, Karel, Sánchez-Lopez, Filiberto, Soberón, Xavier, Rosas, Gabriela, Nunes, Cáris Maroni [UNESP], García-Varela, Martín, Sotelo-Mundo, Rogerio Rafael, López-Zavala, Alonso Alexis, Gevorkian, Goar, Acero, Gonzalo, Laclette, Juan P., Fragoso, Gladis, Sciutto, Edda
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1128/IAI.00395-17
http://hdl.handle.net/11449/179361
Resumo: Taenia solium cysticercosis, a parasitic disease that affects human health in various regions of the world, is preventable by vaccination. Both the 97-aminoacid- long KETc7 peptide and its carboxyl-terminal, 18-amino-acid-long sequence (GK-1) are found in Taenia crassiceps. Both peptides have proven protective capacity against cysticercosis and are part of the highly conserved, cestode-native, 264- amino-acid long protein KE7. KE7 belongs to a ubiquitously distributed family of proteins associated with membrane processes and may participate in several vital cell pathways. The aim of this study was to identify the T. solium KE7 (TsKE7) fulllength protein and to determine its immunogenic properties. Recombinant TsKE7 (rTsKE7) was expressed in Escherichia coli Rosetta2 cells and used to obtain mouse polyclonal antibodies. Anti-rTsKE7 antibodies detected the expected native protein among the 350 spots developed from T. solium cyst vesicular fluid in a mass spectrometry-coupled immune proteomic analysis. These antibodies were then used to screen a phage-displayed 7-random-peptide library to map B-cell epitopes. The recognized phages displayed 9 peptides, with the consensus motif Y(F/Y)PS sequence, which includes YYYPS (named GK-1M, for being a GK-1 mimotope), exactly matching a part of GK-1. GK-1M was recognized by 58% of serum samples from cysticercotic pigs with 100% specificity but induced weak protection against murine cysticercosis. In silico analysis revealed a universal T-cell epitope(s) in native TsKE7 potentially capable of stimulating cytotoxic T lymphocytes and helper T lymphocytes under different major histocompatibility complex class I and class II mouse haplotypes. Altogether, these results provide a rationale for the efficacy of the KETc7, rTsKE7, and GK-1 peptides as vaccines.
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spelling Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigenCysticercosisKETc7ProteomicsS3PvacTaenia crassicepsTaenia soliumVaccineTaenia solium cysticercosis, a parasitic disease that affects human health in various regions of the world, is preventable by vaccination. Both the 97-aminoacid- long KETc7 peptide and its carboxyl-terminal, 18-amino-acid-long sequence (GK-1) are found in Taenia crassiceps. Both peptides have proven protective capacity against cysticercosis and are part of the highly conserved, cestode-native, 264- amino-acid long protein KE7. KE7 belongs to a ubiquitously distributed family of proteins associated with membrane processes and may participate in several vital cell pathways. The aim of this study was to identify the T. solium KE7 (TsKE7) fulllength protein and to determine its immunogenic properties. Recombinant TsKE7 (rTsKE7) was expressed in Escherichia coli Rosetta2 cells and used to obtain mouse polyclonal antibodies. Anti-rTsKE7 antibodies detected the expected native protein among the 350 spots developed from T. solium cyst vesicular fluid in a mass spectrometry-coupled immune proteomic analysis. These antibodies were then used to screen a phage-displayed 7-random-peptide library to map B-cell epitopes. The recognized phages displayed 9 peptides, with the consensus motif Y(F/Y)PS sequence, which includes YYYPS (named GK-1M, for being a GK-1 mimotope), exactly matching a part of GK-1. GK-1M was recognized by 58% of serum samples from cysticercotic pigs with 100% specificity but induced weak protection against murine cysticercosis. In silico analysis revealed a universal T-cell epitope(s) in native TsKE7 potentially capable of stimulating cytotoxic T lymphocytes and helper T lymphocytes under different major histocompatibility complex class I and class II mouse haplotypes. Altogether, these results provide a rationale for the efficacy of the KETc7, rTsKE7, and GK-1 peptides as vaccines.Instituto de Investigaciones Biomédicas Universidad Nacional Autónoma de MéxicoInstituto de Biotecnología Universidad Nacional Autónoma de MéxicoEscuela Nacional de Estudios Superiores Unidad Morelia Universidad Nacional Autónoma de MéxicoInstituto Nacional de Medicina GenómicaFacultad de Medicina Universidad Autónoma del Estado de MorelosUNESP Universidade Estadual Paulista Department of Animal Health and ProductionInstituto de Biología Universidad Nacional Autónoma de MéxicoLaboratorio de Estructura Biomolecular Centro de Investigación en Alimentación y Desarrollo A.C. (CIAD)Departamento de Ciencias Químico Biológicas Universidad de SonoraUNESP Universidade Estadual Paulista Department of Animal Health and ProductionUniversidad Nacional Autónoma de MéxicoInstituto Nacional de Medicina GenómicaUniversidad Autónoma del Estado de MorelosUniversidade Estadual Paulista (Unesp)A.C. (CIAD)Universidad de SonoraBobes, Raúl J.Navarrete-Perea, JoséOchoa-Leyva, AdriánAnaya, Víctor HugoHernández, MariselaCervantes-Torres, JacquelynneEstrada, KarelSánchez-Lopez, FilibertoSoberón, XavierRosas, GabrielaNunes, Cáris Maroni [UNESP]García-Varela, MartínSotelo-Mundo, Rogerio RafaelLópez-Zavala, Alonso AlexisGevorkian, GoarAcero, GonzaloLaclette, Juan P.Fragoso, GladisSciutto, Edda2018-12-11T17:34:52Z2018-12-11T17:34:52Z2017-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1128/IAI.00395-17Infection and Immunity, v. 85, n. 12, 2017.1098-55220019-9567http://hdl.handle.net/11449/17936110.1128/IAI.00395-172-s2.0-850340534042-s2.0-85034053404.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInfection and Immunity1,9541,954info:eu-repo/semantics/openAccess2024-09-04T19:15:51Zoai:repositorio.unesp.br:11449/179361Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462024-09-04T19:15:51Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
title Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
spellingShingle Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
Bobes, Raúl J.
Cysticercosis
KETc7
Proteomics
S3Pvac
Taenia crassiceps
Taenia solium
Vaccine
title_short Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
title_full Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
title_fullStr Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
title_full_unstemmed Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
title_sort Experimental and theoretical approaches to investigate the immunogenicity of Taenia soliumderived KE7 antigen
author Bobes, Raúl J.
author_facet Bobes, Raúl J.
Navarrete-Perea, José
Ochoa-Leyva, Adrián
Anaya, Víctor Hugo
Hernández, Marisela
Cervantes-Torres, Jacquelynne
Estrada, Karel
Sánchez-Lopez, Filiberto
Soberón, Xavier
Rosas, Gabriela
Nunes, Cáris Maroni [UNESP]
García-Varela, Martín
Sotelo-Mundo, Rogerio Rafael
López-Zavala, Alonso Alexis
Gevorkian, Goar
Acero, Gonzalo
Laclette, Juan P.
Fragoso, Gladis
Sciutto, Edda
author_role author
author2 Navarrete-Perea, José
Ochoa-Leyva, Adrián
Anaya, Víctor Hugo
Hernández, Marisela
Cervantes-Torres, Jacquelynne
Estrada, Karel
Sánchez-Lopez, Filiberto
Soberón, Xavier
Rosas, Gabriela
Nunes, Cáris Maroni [UNESP]
García-Varela, Martín
Sotelo-Mundo, Rogerio Rafael
López-Zavala, Alonso Alexis
Gevorkian, Goar
Acero, Gonzalo
Laclette, Juan P.
Fragoso, Gladis
Sciutto, Edda
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Nacional Autónoma de México
Instituto Nacional de Medicina Genómica
Universidad Autónoma del Estado de Morelos
Universidade Estadual Paulista (Unesp)
A.C. (CIAD)
Universidad de Sonora
dc.contributor.author.fl_str_mv Bobes, Raúl J.
Navarrete-Perea, José
Ochoa-Leyva, Adrián
Anaya, Víctor Hugo
Hernández, Marisela
Cervantes-Torres, Jacquelynne
Estrada, Karel
Sánchez-Lopez, Filiberto
Soberón, Xavier
Rosas, Gabriela
Nunes, Cáris Maroni [UNESP]
García-Varela, Martín
Sotelo-Mundo, Rogerio Rafael
López-Zavala, Alonso Alexis
Gevorkian, Goar
Acero, Gonzalo
Laclette, Juan P.
Fragoso, Gladis
Sciutto, Edda
dc.subject.por.fl_str_mv Cysticercosis
KETc7
Proteomics
S3Pvac
Taenia crassiceps
Taenia solium
Vaccine
topic Cysticercosis
KETc7
Proteomics
S3Pvac
Taenia crassiceps
Taenia solium
Vaccine
description Taenia solium cysticercosis, a parasitic disease that affects human health in various regions of the world, is preventable by vaccination. Both the 97-aminoacid- long KETc7 peptide and its carboxyl-terminal, 18-amino-acid-long sequence (GK-1) are found in Taenia crassiceps. Both peptides have proven protective capacity against cysticercosis and are part of the highly conserved, cestode-native, 264- amino-acid long protein KE7. KE7 belongs to a ubiquitously distributed family of proteins associated with membrane processes and may participate in several vital cell pathways. The aim of this study was to identify the T. solium KE7 (TsKE7) fulllength protein and to determine its immunogenic properties. Recombinant TsKE7 (rTsKE7) was expressed in Escherichia coli Rosetta2 cells and used to obtain mouse polyclonal antibodies. Anti-rTsKE7 antibodies detected the expected native protein among the 350 spots developed from T. solium cyst vesicular fluid in a mass spectrometry-coupled immune proteomic analysis. These antibodies were then used to screen a phage-displayed 7-random-peptide library to map B-cell epitopes. The recognized phages displayed 9 peptides, with the consensus motif Y(F/Y)PS sequence, which includes YYYPS (named GK-1M, for being a GK-1 mimotope), exactly matching a part of GK-1. GK-1M was recognized by 58% of serum samples from cysticercotic pigs with 100% specificity but induced weak protection against murine cysticercosis. In silico analysis revealed a universal T-cell epitope(s) in native TsKE7 potentially capable of stimulating cytotoxic T lymphocytes and helper T lymphocytes under different major histocompatibility complex class I and class II mouse haplotypes. Altogether, these results provide a rationale for the efficacy of the KETc7, rTsKE7, and GK-1 peptides as vaccines.
publishDate 2017
dc.date.none.fl_str_mv 2017-01-01
2018-12-11T17:34:52Z
2018-12-11T17:34:52Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1128/IAI.00395-17
Infection and Immunity, v. 85, n. 12, 2017.
1098-5522
0019-9567
http://hdl.handle.net/11449/179361
10.1128/IAI.00395-17
2-s2.0-85034053404
2-s2.0-85034053404.pdf
url http://dx.doi.org/10.1128/IAI.00395-17
http://hdl.handle.net/11449/179361
identifier_str_mv Infection and Immunity, v. 85, n. 12, 2017.
1098-5522
0019-9567
10.1128/IAI.00395-17
2-s2.0-85034053404
2-s2.0-85034053404.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Infection and Immunity
1,954
1,954
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv repositoriounesp@unesp.br
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