Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis

Autores
Camussone, Cecilia María; González, Verónica Doris Guadalupe; Belluzo, María Soledad; Pujato, Nazarena; Ribone, María Élida; Lagier, Claudia Marina; Marcipar, Iván Sergio
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aim of this work was to determine the best strategy to display antigens (Ags) on immunochemical devices to improve test selectivity and sensitivity. We comparatively evaluated five Trypanosoma cruzi antigenic recombinant peptides, chose the three more sensitive ones, built up chimeras bearing these selected Ags, and systematically compared by enzyme-linked immunosorbent assay the performance of the assortments of those peptides with that of the multiepitope constructions bearing all those peptides lineally fused. The better-performing Ags that were compared included peptides homologous to the previously described T. cruzi flagellar repetitive Ag (here named RP1), shed acute-phase Ag (RP2), B13 (RP5), and the chimeric recombinant proteins CP1 and CP2, bearing repetitions of RP1-RP2 and RP1-RP2-RP5, respectively. The diagnostic performances of these Ags were assessed for discrimination efficiency by the formula +OD/cutoff value (where +OD is the mean optical density value of the positive serum samples tested), in comparison with each other either alone, in mixtures, or as peptide-fused chimeras and with total parasite homogenate (TPH). The discrimination efficiency values obtained for CP1 and CP2 were 25% and 52% higher, respectively, than those of their individual-Ag mixtures. CP2 was the only Ag that showed enhanced discrimination efficiency between Chagas´ disease-positive and -negative samples, compared with TPH. This study highlights the convenience of performing immunochemical assays using hybrid, single-molecule, chimeric Ags instead of peptide mixtures. CP2 preliminary tests rendered 98.6% sensitivity when evaluated with a 141-Chagas´ disease-positive serum sample panel and 99.4% specificity when assessed with a 164-Chagas´ disease-negative serum sample panel containing 15 samples from individuals infected with Leishmania spp.
Fil: Camussone, Cecilia María. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: González, Verónica Doris Guadalupe. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Belluzo, María Soledad. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pujato, Nazarena. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ribone, María Élida. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; Argentina
Fil: Lagier, Claudia Marina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; Argentina
Fil: Marcipar, Iván Sergio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
CHAGAS DISEASE
AMERICAN TRYPANOSOMIASIS DIAGNOSIS
MULTIEPITOPE CHIMERA
RECOMBINANT PEPTIDE MIXTURE
RECOMBINANT T. CRUZI ANTIGENS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/24532
Acceder
id CONICETDig_e12fcd528d0fa607daece1c03bcf8468
oai_identifier_str oai:ri.conicet.gov.ar:11336/24532
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosisCamussone, Cecilia MaríaGonzález, Verónica Doris GuadalupeBelluzo, María SoledadPujato, NazarenaRibone, María ÉlidaLagier, Claudia MarinaMarcipar, Iván SergioCHAGAS DISEASEAMERICAN TRYPANOSOMIASIS DIAGNOSISMULTIEPITOPE CHIMERARECOMBINANT PEPTIDE MIXTURERECOMBINANT T. CRUZI ANTIGENShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The aim of this work was to determine the best strategy to display antigens (Ags) on immunochemical devices to improve test selectivity and sensitivity. We comparatively evaluated five Trypanosoma cruzi antigenic recombinant peptides, chose the three more sensitive ones, built up chimeras bearing these selected Ags, and systematically compared by enzyme-linked immunosorbent assay the performance of the assortments of those peptides with that of the multiepitope constructions bearing all those peptides lineally fused. The better-performing Ags that were compared included peptides homologous to the previously described T. cruzi flagellar repetitive Ag (here named RP1), shed acute-phase Ag (RP2), B13 (RP5), and the chimeric recombinant proteins CP1 and CP2, bearing repetitions of RP1-RP2 and RP1-RP2-RP5, respectively. The diagnostic performances of these Ags were assessed for discrimination efficiency by the formula +OD/cutoff value (where +OD is the mean optical density value of the positive serum samples tested), in comparison with each other either alone, in mixtures, or as peptide-fused chimeras and with total parasite homogenate (TPH). The discrimination efficiency values obtained for CP1 and CP2 were 25% and 52% higher, respectively, than those of their individual-Ag mixtures. CP2 was the only Ag that showed enhanced discrimination efficiency between Chagas´ disease-positive and -negative samples, compared with TPH. This study highlights the convenience of performing immunochemical assays using hybrid, single-molecule, chimeric Ags instead of peptide mixtures. CP2 preliminary tests rendered 98.6% sensitivity when evaluated with a 141-Chagas´ disease-positive serum sample panel and 99.4% specificity when assessed with a 164-Chagas´ disease-negative serum sample panel containing 15 samples from individuals infected with Leishmania spp.Fil: Camussone, Cecilia María. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: González, Verónica Doris Guadalupe. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Belluzo, María Soledad. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Pujato, Nazarena. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Ribone, María Élida. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; ArgentinaFil: Lagier, Claudia Marina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; ArgentinaFil: Marcipar, Iván Sergio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAmerican Society for Microbiology2009-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24532Camussone, Cecilia María; González, Verónica Doris Guadalupe; Belluzo, María Soledad; Pujato, Nazarena; Ribone, María Élida; et al.; Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis; American Society for Microbiology; Clinical And Vaccine Immunology; 16; 6; 6-2009; 899-9051556-6811CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/CVI.00005-09info:eu-repo/semantics/altIdentifier/url/http://cvi.asm.org/content/16/6/899info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:41:42Zoai:ri.conicet.gov.ar:11336/24532instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:41:43.149CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
title Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
spellingShingle Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
Camussone, Cecilia María
CHAGAS DISEASE
AMERICAN TRYPANOSOMIASIS DIAGNOSIS
MULTIEPITOPE CHIMERA
RECOMBINANT PEPTIDE MIXTURE
RECOMBINANT T. CRUZI ANTIGENS
title_short Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
title_full Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
title_fullStr Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
title_full_unstemmed Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
title_sort Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis
dc.creator.none.fl_str_mv Camussone, Cecilia María
González, Verónica Doris Guadalupe
Belluzo, María Soledad
Pujato, Nazarena
Ribone, María Élida
Lagier, Claudia Marina
Marcipar, Iván Sergio
author Camussone, Cecilia María
author_facet Camussone, Cecilia María
González, Verónica Doris Guadalupe
Belluzo, María Soledad
Pujato, Nazarena
Ribone, María Élida
Lagier, Claudia Marina
Marcipar, Iván Sergio
author_role author
author2 González, Verónica Doris Guadalupe
Belluzo, María Soledad
Pujato, Nazarena
Ribone, María Élida
Lagier, Claudia Marina
Marcipar, Iván Sergio
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv CHAGAS DISEASE
AMERICAN TRYPANOSOMIASIS DIAGNOSIS
MULTIEPITOPE CHIMERA
RECOMBINANT PEPTIDE MIXTURE
RECOMBINANT T. CRUZI ANTIGENS
topic CHAGAS DISEASE
AMERICAN TRYPANOSOMIASIS DIAGNOSIS
MULTIEPITOPE CHIMERA
RECOMBINANT PEPTIDE MIXTURE
RECOMBINANT T. CRUZI ANTIGENS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The aim of this work was to determine the best strategy to display antigens (Ags) on immunochemical devices to improve test selectivity and sensitivity. We comparatively evaluated five Trypanosoma cruzi antigenic recombinant peptides, chose the three more sensitive ones, built up chimeras bearing these selected Ags, and systematically compared by enzyme-linked immunosorbent assay the performance of the assortments of those peptides with that of the multiepitope constructions bearing all those peptides lineally fused. The better-performing Ags that were compared included peptides homologous to the previously described T. cruzi flagellar repetitive Ag (here named RP1), shed acute-phase Ag (RP2), B13 (RP5), and the chimeric recombinant proteins CP1 and CP2, bearing repetitions of RP1-RP2 and RP1-RP2-RP5, respectively. The diagnostic performances of these Ags were assessed for discrimination efficiency by the formula +OD/cutoff value (where +OD is the mean optical density value of the positive serum samples tested), in comparison with each other either alone, in mixtures, or as peptide-fused chimeras and with total parasite homogenate (TPH). The discrimination efficiency values obtained for CP1 and CP2 were 25% and 52% higher, respectively, than those of their individual-Ag mixtures. CP2 was the only Ag that showed enhanced discrimination efficiency between Chagas´ disease-positive and -negative samples, compared with TPH. This study highlights the convenience of performing immunochemical assays using hybrid, single-molecule, chimeric Ags instead of peptide mixtures. CP2 preliminary tests rendered 98.6% sensitivity when evaluated with a 141-Chagas´ disease-positive serum sample panel and 99.4% specificity when assessed with a 164-Chagas´ disease-negative serum sample panel containing 15 samples from individuals infected with Leishmania spp.
Fil: Camussone, Cecilia María. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: González, Verónica Doris Guadalupe. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Belluzo, María Soledad. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pujato, Nazarena. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ribone, María Élida. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; Argentina
Fil: Lagier, Claudia Marina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Analítica; Argentina
Fil: Marcipar, Iván Sergio. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Instituto de Tecnología Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The aim of this work was to determine the best strategy to display antigens (Ags) on immunochemical devices to improve test selectivity and sensitivity. We comparatively evaluated five Trypanosoma cruzi antigenic recombinant peptides, chose the three more sensitive ones, built up chimeras bearing these selected Ags, and systematically compared by enzyme-linked immunosorbent assay the performance of the assortments of those peptides with that of the multiepitope constructions bearing all those peptides lineally fused. The better-performing Ags that were compared included peptides homologous to the previously described T. cruzi flagellar repetitive Ag (here named RP1), shed acute-phase Ag (RP2), B13 (RP5), and the chimeric recombinant proteins CP1 and CP2, bearing repetitions of RP1-RP2 and RP1-RP2-RP5, respectively. The diagnostic performances of these Ags were assessed for discrimination efficiency by the formula +OD/cutoff value (where +OD is the mean optical density value of the positive serum samples tested), in comparison with each other either alone, in mixtures, or as peptide-fused chimeras and with total parasite homogenate (TPH). The discrimination efficiency values obtained for CP1 and CP2 were 25% and 52% higher, respectively, than those of their individual-Ag mixtures. CP2 was the only Ag that showed enhanced discrimination efficiency between Chagas´ disease-positive and -negative samples, compared with TPH. This study highlights the convenience of performing immunochemical assays using hybrid, single-molecule, chimeric Ags instead of peptide mixtures. CP2 preliminary tests rendered 98.6% sensitivity when evaluated with a 141-Chagas´ disease-positive serum sample panel and 99.4% specificity when assessed with a 164-Chagas´ disease-negative serum sample panel containing 15 samples from individuals infected with Leishmania spp.
publishDate 2009
dc.date.none.fl_str_mv 2009-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/24532
Camussone, Cecilia María; González, Verónica Doris Guadalupe; Belluzo, María Soledad; Pujato, Nazarena; Ribone, María Élida; et al.; Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis; American Society for Microbiology; Clinical And Vaccine Immunology; 16; 6; 6-2009; 899-905
1556-6811
CONICET Digital
CONICET
url http://hdl.handle.net/11336/24532
identifier_str_mv Camussone, Cecilia María; González, Verónica Doris Guadalupe; Belluzo, María Soledad; Pujato, Nazarena; Ribone, María Élida; et al.; Comparison of recombinant Trypanosoma cruzi peptide mixtures versus multiepitope chimeric proteins as sensitizing antigens for immunodiagnosis; American Society for Microbiology; Clinical And Vaccine Immunology; 16; 6; 6-2009; 899-905
1556-6811
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1128/CVI.00005-09
info:eu-repo/semantics/altIdentifier/url/http://cvi.asm.org/content/16/6/899
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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