Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism media...

Autores
Gorgojo, Juan Pablo; Lamberti, Yanina Andrea; Valdez, Hugo Alberto; Harvill, Eric T.; Rodríguez, María Eugenia
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Whooping cough is a reemerging disease caused by two closely related pathogens, Bordetella pertussis and Bordetella parapertussis. The incidence of B. parapertussis in whooping cough cases has been increasing since the introduction of acellular pertussis vaccines containing purified antigens that are common to both strains. Recently published results demonstrated that these vaccines do not protect against B. parapertussis due to the presence of the O antigen on the bacterial surface that impairs antibody access to shared antigens. We have investigated the effect of the lack of opsonization of B. parapertussis on the outcome of its interaction with human neutrophils (polymorphonuclear leukocytes [PMNs]). In the absence of opsonic antibodies, PMN interaction with B. parapertussis resulted in nonbactericidal trafficking upon phagocytosis. A high percentage of nonopsonized B. parapertussis was found in nonacidic lysosome marker (lysosome-associated membrane protein [LAMP])-negative phagosomes with access to the host cell-recycling pathway of external nutrients, allowing bacterial survival as determined by intracellular CFU counts. The lipopolysaccharide (LPS) O antigen was found to be involved in directing B. parapertussis to PMN lipid rafts, eventually determining the nonbactericidal fate inside the PMN. IgG opsonization of B. parapertussis drastically changed this interaction by not only inducing efficient PMN phagocytosis but also promoting PMN bacterial killing. These data provide new insights into the immune mechanisms of hosts against B. parapertussis and document the crucial importance of opsonic antibodies in immunity to this pathogen.
Facultad de Ciencias Exactas
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Ciencias Exactas
Bordetella parapertussis
Lipopolysaccharide O Antigen
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:10915/84072
Acceder
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network_name_str SEDICI (UNLP)
spelling Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigenGorgojo, Juan PabloLamberti, Yanina AndreaValdez, Hugo AlbertoHarvill, Eric T.Rodríguez, María EugeniaCiencias ExactasBordetella parapertussisLipopolysaccharide O AntigenWhooping cough is a reemerging disease caused by two closely related pathogens, <i>Bordetella pertussis</i> and <i>Bordetella parapertussis</i>. The incidence of <i>B. parapertussis</i> in whooping cough cases has been increasing since the introduction of acellular pertussis vaccines containing purified antigens that are common to both strains. Recently published results demonstrated that these vaccines do not protect against <i>B. parapertussis</i> due to the presence of the O antigen on the bacterial surface that impairs antibody access to shared antigens. We have investigated the effect of the lack of opsonization of <i>B. parapertussis</i> on the outcome of its interaction with human neutrophils (polymorphonuclear leukocytes [PMNs]). In the absence of opsonic antibodies, PMN interaction with <i>B. parapertussis</i> resulted in nonbactericidal trafficking upon phagocytosis. A high percentage of nonopsonized <i>B. parapertussis</i> was found in nonacidic lysosome marker (lysosome-associated membrane protein [LAMP])-negative phagosomes with access to the host cell-recycling pathway of external nutrients, allowing bacterial survival as determined by intracellular CFU counts. The lipopolysaccharide (LPS) O antigen was found to be involved in directing <i>B. parapertussis</i> to PMN lipid rafts, eventually determining the nonbactericidal fate inside the PMN. IgG opsonization of <i>B. parapertussis</i> drastically changed this interaction by not only inducing efficient PMN phagocytosis but also promoting PMN bacterial killing. These data provide new insights into the immune mechanisms of hosts against <i>B. parapertussis</i> and document the crucial importance of opsonic antibodies in immunity to this pathogen.Facultad de Ciencias ExactasCentro de Investigación y Desarrollo en Fermentaciones Industriales2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf4309-4316http://sedici.unlp.edu.ar/handle/10915/84072enginfo:eu-repo/semantics/altIdentifier/issn/0019-9567info:eu-repo/semantics/altIdentifier/doi/10.1128/IAI.00662-12info: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:UNLP2025-10-15T11:07:56Zoai:sedici.unlp.edu.ar:10915/84072Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:07:56.993SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
title Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
spellingShingle Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
Gorgojo, Juan Pablo
Ciencias Exactas
Bordetella parapertussis
Lipopolysaccharide O Antigen
title_short Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
title_full Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
title_fullStr Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
title_full_unstemmed Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
title_sort Bordetella parapertussis survives the innate interaction with human neutrophils by impairing bactericidal trafficking inside the cell through a lipid raft-dependent mechanism mediated by the lipopolysaccharide O antigen
dc.creator.none.fl_str_mv Gorgojo, Juan Pablo
Lamberti, Yanina Andrea
Valdez, Hugo Alberto
Harvill, Eric T.
Rodríguez, María Eugenia
author Gorgojo, Juan Pablo
author_facet Gorgojo, Juan Pablo
Lamberti, Yanina Andrea
Valdez, Hugo Alberto
Harvill, Eric T.
Rodríguez, María Eugenia
author_role author
author2 Lamberti, Yanina Andrea
Valdez, Hugo Alberto
Harvill, Eric T.
Rodríguez, María Eugenia
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Bordetella parapertussis
Lipopolysaccharide O Antigen
topic Ciencias Exactas
Bordetella parapertussis
Lipopolysaccharide O Antigen
dc.description.none.fl_txt_mv Whooping cough is a reemerging disease caused by two closely related pathogens, <i>Bordetella pertussis</i> and <i>Bordetella parapertussis</i>. The incidence of <i>B. parapertussis</i> in whooping cough cases has been increasing since the introduction of acellular pertussis vaccines containing purified antigens that are common to both strains. Recently published results demonstrated that these vaccines do not protect against <i>B. parapertussis</i> due to the presence of the O antigen on the bacterial surface that impairs antibody access to shared antigens. We have investigated the effect of the lack of opsonization of <i>B. parapertussis</i> on the outcome of its interaction with human neutrophils (polymorphonuclear leukocytes [PMNs]). In the absence of opsonic antibodies, PMN interaction with <i>B. parapertussis</i> resulted in nonbactericidal trafficking upon phagocytosis. A high percentage of nonopsonized <i>B. parapertussis</i> was found in nonacidic lysosome marker (lysosome-associated membrane protein [LAMP])-negative phagosomes with access to the host cell-recycling pathway of external nutrients, allowing bacterial survival as determined by intracellular CFU counts. The lipopolysaccharide (LPS) O antigen was found to be involved in directing <i>B. parapertussis</i> to PMN lipid rafts, eventually determining the nonbactericidal fate inside the PMN. IgG opsonization of <i>B. parapertussis</i> drastically changed this interaction by not only inducing efficient PMN phagocytosis but also promoting PMN bacterial killing. These data provide new insights into the immune mechanisms of hosts against <i>B. parapertussis</i> and document the crucial importance of opsonic antibodies in immunity to this pathogen.
Facultad de Ciencias Exactas
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description Whooping cough is a reemerging disease caused by two closely related pathogens, <i>Bordetella pertussis</i> and <i>Bordetella parapertussis</i>. The incidence of <i>B. parapertussis</i> in whooping cough cases has been increasing since the introduction of acellular pertussis vaccines containing purified antigens that are common to both strains. Recently published results demonstrated that these vaccines do not protect against <i>B. parapertussis</i> due to the presence of the O antigen on the bacterial surface that impairs antibody access to shared antigens. We have investigated the effect of the lack of opsonization of <i>B. parapertussis</i> on the outcome of its interaction with human neutrophils (polymorphonuclear leukocytes [PMNs]). In the absence of opsonic antibodies, PMN interaction with <i>B. parapertussis</i> resulted in nonbactericidal trafficking upon phagocytosis. A high percentage of nonopsonized <i>B. parapertussis</i> was found in nonacidic lysosome marker (lysosome-associated membrane protein [LAMP])-negative phagosomes with access to the host cell-recycling pathway of external nutrients, allowing bacterial survival as determined by intracellular CFU counts. The lipopolysaccharide (LPS) O antigen was found to be involved in directing <i>B. parapertussis</i> to PMN lipid rafts, eventually determining the nonbactericidal fate inside the PMN. IgG opsonization of <i>B. parapertussis</i> drastically changed this interaction by not only inducing efficient PMN phagocytosis but also promoting PMN bacterial killing. These data provide new insights into the immune mechanisms of hosts against <i>B. parapertussis</i> and document the crucial importance of opsonic antibodies in immunity to this pathogen.
publishDate 2012
dc.date.none.fl_str_mv 2012
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/10915/84072
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dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0019-9567
info:eu-repo/semantics/altIdentifier/doi/10.1128/IAI.00662-12
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
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instname:Universidad Nacional de La Plata
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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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