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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/24532
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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 Técnicas2025-09-29T10:43:30Zoai: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:34982025-09-29 10:43:31.16CONICET 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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1844614470730514432 |
score |
13.070432 |