B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle

Autores
Ostrowski, Matias; Mundo, Silvia Leonor; Harris, N. B.; Barletta, R. G.; Lopez, O. J.
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Mycobacterium avium ssp. paratuberculosis (M. paratuberculosis) causes Johne's disease, a chronic and fatal enteritis in ruminants. In the last stage of the disease, antibody titres rise and levels of interferon-γ decrease, suggesting that the host-immune response is switching from a T helper 1 (Th1) to a Th2 profile. In infected cattle, the membrane protein p34 elicits the predominant humoral response against M. paratuberculosis. To map the B-cell epitopes of this antigen, affinity-purified bovine antibodies against the carboxy-terminal region of p34 were used to screen a 12-mer phage display library. Several phage clones carrying peptides resembling fragments of p34 were affinity selected. Based on the predicted amino acid sequence, peptides were chemically synthesized, which demonstrated reactivity with serum from naturally infected and p34-vaccinated cattle. Immunization of mice with these peptides elicited an anti-p34 antibody response. Two B-cell epitopes were identified and characterized. Based on the reactivity and the type of immune response elicited, epitope A was determined to be conformational, whereas epitope B was demonstrated to be sequential. Both epitopes were shown to be present in p34 proteins from M. avium ssp. avium or M. paratuberculosis but absent from M. intracellulare, the other member of the M. avium complex. Furthermore, both epitopes were mapped to regions of p34 that display high variability when compared to homologous proteins from other mycobacterial species of public and animal health importance. We hypothesize that these variable regions of p34 may play a role in the immunobiology of M. paratuberculosis infections.
Fil: Ostrowski, Matias. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina
Fil: Mundo, Silvia Leonor. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
Fil: Harris, N. B.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
Fil: Barletta, R. G.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
Fil: Lopez, O. J.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
Materia
PARAUBERCULOSIS
P34
BOVINOS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/162969
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected CattleOstrowski, MatiasMundo, Silvia LeonorHarris, N. B.Barletta, R. G.Lopez, O. J.PARAUBERCULOSISP34BOVINOShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Mycobacterium avium ssp. paratuberculosis (M. paratuberculosis) causes Johne's disease, a chronic and fatal enteritis in ruminants. In the last stage of the disease, antibody titres rise and levels of interferon-γ decrease, suggesting that the host-immune response is switching from a T helper 1 (Th1) to a Th2 profile. In infected cattle, the membrane protein p34 elicits the predominant humoral response against M. paratuberculosis. To map the B-cell epitopes of this antigen, affinity-purified bovine antibodies against the carboxy-terminal region of p34 were used to screen a 12-mer phage display library. Several phage clones carrying peptides resembling fragments of p34 were affinity selected. Based on the predicted amino acid sequence, peptides were chemically synthesized, which demonstrated reactivity with serum from naturally infected and p34-vaccinated cattle. Immunization of mice with these peptides elicited an anti-p34 antibody response. Two B-cell epitopes were identified and characterized. Based on the reactivity and the type of immune response elicited, epitope A was determined to be conformational, whereas epitope B was demonstrated to be sequential. Both epitopes were shown to be present in p34 proteins from M. avium ssp. avium or M. paratuberculosis but absent from M. intracellulare, the other member of the M. avium complex. Furthermore, both epitopes were mapped to regions of p34 that display high variability when compared to homologous proteins from other mycobacterial species of public and animal health importance. We hypothesize that these variable regions of p34 may play a role in the immunobiology of M. paratuberculosis infections.Fil: Ostrowski, Matias. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; ArgentinaFil: Mundo, Silvia Leonor. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; ArgentinaFil: Harris, N. B.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; ArgentinaFil: Barletta, R. G.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; ArgentinaFil: Lopez, O. J.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; ArgentinaWiley Blackwell Publishing, Inc2003-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/162969Ostrowski, Matias; Mundo, Silvia Leonor; Harris, N. B.; Barletta, R. G.; Lopez, O. J.; B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle; Wiley Blackwell Publishing, Inc; Scandinavian Journal Of Immunology; 58; 5; 11-2003; 511-5210300-9475CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/full/10.1046/j.1365-3083.2003.01334.xinfo:eu-repo/semantics/altIdentifier/doi/10.1046/j.1365-3083.2003.01334.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-05-27T14:26:53Zoai:ri.conicet.gov.ar:11336/162969instacron: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:34982026-05-27 14:26:54.012CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
title B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
spellingShingle B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
Ostrowski, Matias
PARAUBERCULOSIS
P34
BOVINOS
title_short B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
title_full B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
title_fullStr B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
title_full_unstemmed B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
title_sort B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle
dc.creator.none.fl_str_mv Ostrowski, Matias
Mundo, Silvia Leonor
Harris, N. B.
Barletta, R. G.
Lopez, O. J.
author Ostrowski, Matias
author_facet Ostrowski, Matias
Mundo, Silvia Leonor
Harris, N. B.
Barletta, R. G.
Lopez, O. J.
author_role author
author2 Mundo, Silvia Leonor
Harris, N. B.
Barletta, R. G.
Lopez, O. J.
author2_role author
author
author
author
dc.subject.none.fl_str_mv PARAUBERCULOSIS
P34
BOVINOS
topic PARAUBERCULOSIS
P34
BOVINOS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Mycobacterium avium ssp. paratuberculosis (M. paratuberculosis) causes Johne's disease, a chronic and fatal enteritis in ruminants. In the last stage of the disease, antibody titres rise and levels of interferon-γ decrease, suggesting that the host-immune response is switching from a T helper 1 (Th1) to a Th2 profile. In infected cattle, the membrane protein p34 elicits the predominant humoral response against M. paratuberculosis. To map the B-cell epitopes of this antigen, affinity-purified bovine antibodies against the carboxy-terminal region of p34 were used to screen a 12-mer phage display library. Several phage clones carrying peptides resembling fragments of p34 were affinity selected. Based on the predicted amino acid sequence, peptides were chemically synthesized, which demonstrated reactivity with serum from naturally infected and p34-vaccinated cattle. Immunization of mice with these peptides elicited an anti-p34 antibody response. Two B-cell epitopes were identified and characterized. Based on the reactivity and the type of immune response elicited, epitope A was determined to be conformational, whereas epitope B was demonstrated to be sequential. Both epitopes were shown to be present in p34 proteins from M. avium ssp. avium or M. paratuberculosis but absent from M. intracellulare, the other member of the M. avium complex. Furthermore, both epitopes were mapped to regions of p34 that display high variability when compared to homologous proteins from other mycobacterial species of public and animal health importance. We hypothesize that these variable regions of p34 may play a role in the immunobiology of M. paratuberculosis infections.
Fil: Ostrowski, Matias. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina
Fil: Mundo, Silvia Leonor. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
Fil: Harris, N. B.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
Fil: Barletta, R. G.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
Fil: Lopez, O. J.. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias; Argentina
description Mycobacterium avium ssp. paratuberculosis (M. paratuberculosis) causes Johne's disease, a chronic and fatal enteritis in ruminants. In the last stage of the disease, antibody titres rise and levels of interferon-γ decrease, suggesting that the host-immune response is switching from a T helper 1 (Th1) to a Th2 profile. In infected cattle, the membrane protein p34 elicits the predominant humoral response against M. paratuberculosis. To map the B-cell epitopes of this antigen, affinity-purified bovine antibodies against the carboxy-terminal region of p34 were used to screen a 12-mer phage display library. Several phage clones carrying peptides resembling fragments of p34 were affinity selected. Based on the predicted amino acid sequence, peptides were chemically synthesized, which demonstrated reactivity with serum from naturally infected and p34-vaccinated cattle. Immunization of mice with these peptides elicited an anti-p34 antibody response. Two B-cell epitopes were identified and characterized. Based on the reactivity and the type of immune response elicited, epitope A was determined to be conformational, whereas epitope B was demonstrated to be sequential. Both epitopes were shown to be present in p34 proteins from M. avium ssp. avium or M. paratuberculosis but absent from M. intracellulare, the other member of the M. avium complex. Furthermore, both epitopes were mapped to regions of p34 that display high variability when compared to homologous proteins from other mycobacterial species of public and animal health importance. We hypothesize that these variable regions of p34 may play a role in the immunobiology of M. paratuberculosis infections.
publishDate 2003
dc.date.none.fl_str_mv 2003-11
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/11336/162969
Ostrowski, Matias; Mundo, Silvia Leonor; Harris, N. B.; Barletta, R. G.; Lopez, O. J.; B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle; Wiley Blackwell Publishing, Inc; Scandinavian Journal Of Immunology; 58; 5; 11-2003; 511-521
0300-9475
CONICET Digital
CONICET
url http://hdl.handle.net/11336/162969
identifier_str_mv Ostrowski, Matias; Mundo, Silvia Leonor; Harris, N. B.; Barletta, R. G.; Lopez, O. J.; B-Cell Epitopes in the Immunodominant p34 Antigen of Mycobacterium avium ssp. paratuberculosis Recognized by Antibodies from Infected Cattle; Wiley Blackwell Publishing, Inc; Scandinavian Journal Of Immunology; 58; 5; 11-2003; 511-521
0300-9475
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/full/10.1046/j.1365-3083.2003.01334.x
info:eu-repo/semantics/altIdentifier/doi/10.1046/j.1365-3083.2003.01334.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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 13.264256

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