Fc receptor-mediated immunity against Bordetella pertussis

Autores
Rodríguez, María Eugenia; Hellwig, S. M. M.; Hozbor, Daniela Flavia; Leusen, J.; Pol, W. L. van der; Winkel, J. G. J. van de
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The relevance of specific Abs for the induction of cellular effector functions against Bordetella pertussis was studied. IgG-opsonized B. pertussis was efficiently phagocytosed by human polymorphonuclear leukocytes (PMN). This process was mediated by the PMN IgG receptors, FcγRIIa (CD32) and FcγRIIIb (CD16), working synergistically. Furthermore, these FcγR triggered efficient PMN respiratory burst activity and mediated transfer of B. pertussis to lysosomal compartments, ultimately resulting in reduced bacterial viability. Bacteria opsonized with IgA triggered similar PMN activation via FcαR (CD89). Simultaneous engagement of FcαRI and FcγR by B. pertussis resulted in increased phagocytosis rates, compared with responses induced by either isotype alone. These data provide new insights into host immune mechanisms against B. pertussis and document a crucial role for Ig-FcR interactions in immunity to this human pathogen.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Ciencias Exactas
Bordetella pertussis
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/84228

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network_name_str SEDICI (UNLP)
spelling Fc receptor-mediated immunity against Bordetella pertussisRodríguez, María EugeniaHellwig, S. M. M.Hozbor, Daniela FlaviaLeusen, J.Pol, W. L. van derWinkel, J. G. J. van deCiencias ExactasBordetella pertussisThe relevance of specific Abs for the induction of cellular effector functions against Bordetella pertussis was studied. IgG-opsonized B. pertussis was efficiently phagocytosed by human polymorphonuclear leukocytes (PMN). This process was mediated by the PMN IgG receptors, FcγRIIa (CD32) and FcγRIIIb (CD16), working synergistically. Furthermore, these FcγR triggered efficient PMN respiratory burst activity and mediated transfer of B. pertussis to lysosomal compartments, ultimately resulting in reduced bacterial viability. Bacteria opsonized with IgA triggered similar PMN activation via FcαR (CD89). Simultaneous engagement of FcαRI and FcγR by B. pertussis resulted in increased phagocytosis rates, compared with responses induced by either isotype alone. These data provide new insights into host immune mechanisms against B. pertussis and document a crucial role for Ig-FcR interactions in immunity to this human pathogen.Centro de Investigación y Desarrollo en Fermentaciones Industriales2001info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf6545-6551http://sedici.unlp.edu.ar/handle/10915/84228enginfo:eu-repo/semantics/altIdentifier/issn/0022-1767info:eu-repo/semantics/altIdentifier/doi/10.4049/jimmunol.167.11.6545info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:19Zoai:sedici.unlp.edu.ar:10915/84228Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:20.061SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Fc receptor-mediated immunity against Bordetella pertussis
title Fc receptor-mediated immunity against Bordetella pertussis
spellingShingle Fc receptor-mediated immunity against Bordetella pertussis
Rodríguez, María Eugenia
Ciencias Exactas
Bordetella pertussis
title_short Fc receptor-mediated immunity against Bordetella pertussis
title_full Fc receptor-mediated immunity against Bordetella pertussis
title_fullStr Fc receptor-mediated immunity against Bordetella pertussis
title_full_unstemmed Fc receptor-mediated immunity against Bordetella pertussis
title_sort Fc receptor-mediated immunity against Bordetella pertussis
dc.creator.none.fl_str_mv Rodríguez, María Eugenia
Hellwig, S. M. M.
Hozbor, Daniela Flavia
Leusen, J.
Pol, W. L. van der
Winkel, J. G. J. van de
author Rodríguez, María Eugenia
author_facet Rodríguez, María Eugenia
Hellwig, S. M. M.
Hozbor, Daniela Flavia
Leusen, J.
Pol, W. L. van der
Winkel, J. G. J. van de
author_role author
author2 Hellwig, S. M. M.
Hozbor, Daniela Flavia
Leusen, J.
Pol, W. L. van der
Winkel, J. G. J. van de
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Bordetella pertussis
topic Ciencias Exactas
Bordetella pertussis
dc.description.none.fl_txt_mv The relevance of specific Abs for the induction of cellular effector functions against Bordetella pertussis was studied. IgG-opsonized B. pertussis was efficiently phagocytosed by human polymorphonuclear leukocytes (PMN). This process was mediated by the PMN IgG receptors, FcγRIIa (CD32) and FcγRIIIb (CD16), working synergistically. Furthermore, these FcγR triggered efficient PMN respiratory burst activity and mediated transfer of B. pertussis to lysosomal compartments, ultimately resulting in reduced bacterial viability. Bacteria opsonized with IgA triggered similar PMN activation via FcαR (CD89). Simultaneous engagement of FcαRI and FcγR by B. pertussis resulted in increased phagocytosis rates, compared with responses induced by either isotype alone. These data provide new insights into host immune mechanisms against B. pertussis and document a crucial role for Ig-FcR interactions in immunity to this human pathogen.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description The relevance of specific Abs for the induction of cellular effector functions against Bordetella pertussis was studied. IgG-opsonized B. pertussis was efficiently phagocytosed by human polymorphonuclear leukocytes (PMN). This process was mediated by the PMN IgG receptors, FcγRIIa (CD32) and FcγRIIIb (CD16), working synergistically. Furthermore, these FcγR triggered efficient PMN respiratory burst activity and mediated transfer of B. pertussis to lysosomal compartments, ultimately resulting in reduced bacterial viability. Bacteria opsonized with IgA triggered similar PMN activation via FcαR (CD89). Simultaneous engagement of FcαRI and FcγR by B. pertussis resulted in increased phagocytosis rates, compared with responses induced by either isotype alone. These data provide new insights into host immune mechanisms against B. pertussis and document a crucial role for Ig-FcR interactions in immunity to this human pathogen.
publishDate 2001
dc.date.none.fl_str_mv 2001
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/84228
url http://sedici.unlp.edu.ar/handle/10915/84228
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0022-1767
info:eu-repo/semantics/altIdentifier/doi/10.4049/jimmunol.167.11.6545
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
6545-6551
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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