Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine

Detalhes bibliográficos
Autor(a) principal: Rassy, Dunia
Data de Publicação: 2010
Outros Autores: Bobes, Raul J., Rosas, Gabriela, Anaya, Victor H., Brehm, Klaus, Hernandez, Beatriz, Cervantes, Jacquelynne, Pedraza, Saul, Morales, Julio, Villalobos, Nelly, de Aluja, Aline S., Laclette, Juan P., Nunes, Caris Maroni [UNESP], Biondi, Germano Francisco [UNESP], Fragoso, Gladis, Hernandez, Marisela, Sciutto, Edda
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1371/journal.pone.0011287
http://hdl.handle.net/11449/14783
Resumo: Background: Cysticercosis and hydatidosis seriously affect human health and are responsible for considerable economic loss in animal husbandry in non-developed and developed countries. S3Pvac and EG95 are the only field trial-tested vaccine candidates against cysticercosis and hydatidosis, respectively. S3Pvac is composed of three peptides (KETc1, GK1 and KETc12), originally identified in a Taenia crassiceps cDNA library. S3Pvac synthetically and recombinantly expressed is effective against experimentally and naturally acquired cysticercosis.Methodology/ Principal Findings: In this study, the homologous sequences of two of the S3Pvac peptides, GK1 and KETc1, were identified and further characterized in Taenia crassiceps WFU, Taenia solium, Taenia saginata, Echinococcus granulosus and Echinococcus multilocularis. Comparisons of the nucleotide and amino acid sequences coding for KETc1 and GK1 revealed significant homologies in these species. The predicted secondary structure of GK1 is almost identical between the species, while some differences were observed in the C terminal region of KETc1 according to 3D modeling. A KETc1 variant with a deletion of three C-terminal amino acids protected to the same extent against experimental murine cysticercosis as the entire peptide. on the contrary, immunization with the truncated GK1 failed to induce protection. Immunolocalization studies revealed the non stage-specificity of the two S3Pvac epitopes and their persistence in the larval tegument of all species and in Taenia adult tapeworms.Conclusions/ Significance: These results indicate that GK1 and KETc1 may be considered candidates to be included in the formulation of a multivalent and multistage vaccine against these cestodiases because of their enhancing effects on other available vaccine candidates.
id UNSP_86212392fe211d5ef8bd17e99e90e95b
oai_identifier_str oai:repositorio.unesp.br:11449/14783
network_acronym_str UNSP
network_name_str Repositório Institucional da UNESP
repository_id_str 2946
spelling Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis VaccineBackground: Cysticercosis and hydatidosis seriously affect human health and are responsible for considerable economic loss in animal husbandry in non-developed and developed countries. S3Pvac and EG95 are the only field trial-tested vaccine candidates against cysticercosis and hydatidosis, respectively. S3Pvac is composed of three peptides (KETc1, GK1 and KETc12), originally identified in a Taenia crassiceps cDNA library. S3Pvac synthetically and recombinantly expressed is effective against experimentally and naturally acquired cysticercosis.Methodology/ Principal Findings: In this study, the homologous sequences of two of the S3Pvac peptides, GK1 and KETc1, were identified and further characterized in Taenia crassiceps WFU, Taenia solium, Taenia saginata, Echinococcus granulosus and Echinococcus multilocularis. Comparisons of the nucleotide and amino acid sequences coding for KETc1 and GK1 revealed significant homologies in these species. The predicted secondary structure of GK1 is almost identical between the species, while some differences were observed in the C terminal region of KETc1 according to 3D modeling. A KETc1 variant with a deletion of three C-terminal amino acids protected to the same extent against experimental murine cysticercosis as the entire peptide. on the contrary, immunization with the truncated GK1 failed to induce protection. Immunolocalization studies revealed the non stage-specificity of the two S3Pvac epitopes and their persistence in the larval tegument of all species and in Taenia adult tapeworms.Conclusions/ Significance: These results indicate that GK1 and KETc1 may be considered candidates to be included in the formulation of a multivalent and multistage vaccine against these cestodiases because of their enhancing effects on other available vaccine candidates.Consejo Nacional de Ciencia y Tecnología (CONACYT)Direccion General de Asuntos del Personal Academico (DGAPA)Univ Nacl Autonoma Mexico, Inst Invest Biomed, Dept Inmunol, Mexico City 04510, DF, MexicoUniv Autonoma Estado Morelos, Fac Med, Cuernavaca, Morelos, MexicoHumboldt Univ, Inst Theoret Biol, Berlin, GermanyUniv Wurzburg, Inst Hyg & Mikrobiol, Wurzburg, GermanyUniv Nacl Autonoma Mexico, Fac Med, Mexico City 04510, DF, MexicoUniv Nacl Autonoma Mexico, Fac Med Vet & Zootecnia, Mexico City 04510, DF, MexicoUniv Estadual Paulista, Dept Apoio Prod & Saúde Anim, Aracatuba, Sao Paolo, BrazilUniv Estadual Paulista, Fac Med Vet & Zootecnia Botucatu, Dept Hyg Vet & Saúde Publ, Botucatu, SP, BrazilUniv Estadual Paulista, Dept Apoio Prod & Saúde Anim, Aracatuba, Sao Paolo, BrazilUniv Estadual Paulista, Fac Med Vet & Zootecnia Botucatu, Dept Hyg Vet & Saúde Publ, Botucatu, SP, BrazilCONACYT: S52680-R/70072CONACYT: CB-62471DGAPA: IN217908Public Library ScienceUniv Nacl Autonoma MexicoUniv Autonoma Estado MorelosHumboldt UnivUniv WurzburgUniversidade Estadual Paulista (Unesp)Rassy, DuniaBobes, Raul J.Rosas, GabrielaAnaya, Victor H.Brehm, KlausHernandez, BeatrizCervantes, JacquelynnePedraza, SaulMorales, JulioVillalobos, Nellyde Aluja, Aline S.Laclette, Juan P.Nunes, Caris Maroni [UNESP]Biondi, Germano Francisco [UNESP]Fragoso, GladisHernandez, MariselaSciutto, Edda2013-09-30T18:26:39Z2014-05-20T13:42:31Z2013-09-30T18:26:39Z2014-05-20T13:42:31Z2010-06-23info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article11application/pdfhttp://dx.doi.org/10.1371/journal.pone.0011287Plos One. San Francisco: Public Library Science, v. 5, n. 6, p. 11, 2010.1932-6203http://hdl.handle.net/11449/1478310.1371/journal.pone.0011287WOS:000279135400029WOS000279135400029.pdf1892359871207408Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPLOS ONE2.7661,164info:eu-repo/semantics/openAccess2024-09-04T19:15:52Zoai:repositorio.unesp.br:11449/14783Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462024-09-04T19:15:52Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
title Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
spellingShingle Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
Rassy, Dunia
title_short Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
title_full Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
title_fullStr Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
title_full_unstemmed Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
title_sort Characterization of S3Pvac Anti-Cysticercosis Vaccine Components: Implications for the Development of an Anti-Cestodiasis Vaccine
author Rassy, Dunia
author_facet Rassy, Dunia
Bobes, Raul J.
Rosas, Gabriela
Anaya, Victor H.
Brehm, Klaus
Hernandez, Beatriz
Cervantes, Jacquelynne
Pedraza, Saul
Morales, Julio
Villalobos, Nelly
de Aluja, Aline S.
Laclette, Juan P.
Nunes, Caris Maroni [UNESP]
Biondi, Germano Francisco [UNESP]
Fragoso, Gladis
Hernandez, Marisela
Sciutto, Edda
author_role author
author2 Bobes, Raul J.
Rosas, Gabriela
Anaya, Victor H.
Brehm, Klaus
Hernandez, Beatriz
Cervantes, Jacquelynne
Pedraza, Saul
Morales, Julio
Villalobos, Nelly
de Aluja, Aline S.
Laclette, Juan P.
Nunes, Caris Maroni [UNESP]
Biondi, Germano Francisco [UNESP]
Fragoso, Gladis
Hernandez, Marisela
Sciutto, Edda
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Univ Nacl Autonoma Mexico
Univ Autonoma Estado Morelos
Humboldt Univ
Univ Wurzburg
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Rassy, Dunia
Bobes, Raul J.
Rosas, Gabriela
Anaya, Victor H.
Brehm, Klaus
Hernandez, Beatriz
Cervantes, Jacquelynne
Pedraza, Saul
Morales, Julio
Villalobos, Nelly
de Aluja, Aline S.
Laclette, Juan P.
Nunes, Caris Maroni [UNESP]
Biondi, Germano Francisco [UNESP]
Fragoso, Gladis
Hernandez, Marisela
Sciutto, Edda
description Background: Cysticercosis and hydatidosis seriously affect human health and are responsible for considerable economic loss in animal husbandry in non-developed and developed countries. S3Pvac and EG95 are the only field trial-tested vaccine candidates against cysticercosis and hydatidosis, respectively. S3Pvac is composed of three peptides (KETc1, GK1 and KETc12), originally identified in a Taenia crassiceps cDNA library. S3Pvac synthetically and recombinantly expressed is effective against experimentally and naturally acquired cysticercosis.Methodology/ Principal Findings: In this study, the homologous sequences of two of the S3Pvac peptides, GK1 and KETc1, were identified and further characterized in Taenia crassiceps WFU, Taenia solium, Taenia saginata, Echinococcus granulosus and Echinococcus multilocularis. Comparisons of the nucleotide and amino acid sequences coding for KETc1 and GK1 revealed significant homologies in these species. The predicted secondary structure of GK1 is almost identical between the species, while some differences were observed in the C terminal region of KETc1 according to 3D modeling. A KETc1 variant with a deletion of three C-terminal amino acids protected to the same extent against experimental murine cysticercosis as the entire peptide. on the contrary, immunization with the truncated GK1 failed to induce protection. Immunolocalization studies revealed the non stage-specificity of the two S3Pvac epitopes and their persistence in the larval tegument of all species and in Taenia adult tapeworms.Conclusions/ Significance: These results indicate that GK1 and KETc1 may be considered candidates to be included in the formulation of a multivalent and multistage vaccine against these cestodiases because of their enhancing effects on other available vaccine candidates.
publishDate 2010
dc.date.none.fl_str_mv 2010-06-23
2013-09-30T18:26:39Z
2013-09-30T18:26:39Z
2014-05-20T13:42:31Z
2014-05-20T13:42:31Z
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/10.1371/journal.pone.0011287
Plos One. San Francisco: Public Library Science, v. 5, n. 6, p. 11, 2010.
1932-6203
http://hdl.handle.net/11449/14783
10.1371/journal.pone.0011287
WOS:000279135400029
WOS000279135400029.pdf
1892359871207408
url http://dx.doi.org/10.1371/journal.pone.0011287
http://hdl.handle.net/11449/14783
identifier_str_mv Plos One. San Francisco: Public Library Science, v. 5, n. 6, p. 11, 2010.
1932-6203
10.1371/journal.pone.0011287
WOS:000279135400029
WOS000279135400029.pdf
1892359871207408
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv PLOS ONE
2.766
1,164
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 11
application/pdf
dc.publisher.none.fl_str_mv Public Library Science
publisher.none.fl_str_mv Public Library Science
dc.source.none.fl_str_mv Web of Science
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
_version_ 1810021404959047680