Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides

Autores
Guo, Jitao; Nair, Manoj K. M.; Galvan, Estela Maria; Liu, Shu Lin; Schifferli, Dieter M.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Bacterial pathogens display a variety of protection mechanisms against the inhibitory and lethal effects of host cationic antimicrobial peptides (CAMPs). To identify Yersinia pestis genes involved in CAMP resistance, libraries of DSY101 (KIM6 caf1 pla psa) minitransposon Tn5AraOut mutants were selected at 37°C for resistance to the model CAMPs polymyxin B or protamine. This approach targeted genes that needed to be repressed (null mutations) or induced (upstream P(BAD) insertions) for the detection of CAMP resistance, and predictably for improved pathogen fitness in mammalian hosts. Ten mutants demonstrated increased resistance to polymyxin B or protamine, with the mapped mutations pointing towards genes suspected to participate in modifying membrane components, genes encoding transport proteins or enzymes, or the regulator of a ferrous iron uptake system (feoC). Not all the mutants were resistant to both CAMPs used for selection. None of the polymyxin B- and only some protamine-resistant mutants, including the feoC mutant, showed increased resistance to rat bronchoalveolar lavage fluid (rBALF) known to contain cathelicidin and β-defensin 1. Thus, findings on bacterial resistance to polymyxin B or protamine don't always apply to CAMPs of the mammalian innate immune system, such as the ones in rBALF.
Fil: Guo, Jitao. Peking University Health Science Center. Department of Microbiology; China
Fil: Nair, Manoj K. M.. University of Pennsylvania. School of Veterinary Medicine; Estados Unidos
Fil: Galvan, Estela Maria. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. University of Pennsylvania; Estados Unidos
Fil: Liu, Shu Lin. Peking University Health Science Center. Department of Microbiology; China
Fil: Schifferli, Dieter M.. University of Pennsylvania. School of Veterinary Medicine; Estados Unidos
Materia
Yersinia Pestis
Minitransposon
Polymyxin B
Protamine
Ll-37
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/12813
Acceder
id CONICETDig_487df766896a8574b17a94761da7bec7
oai_identifier_str oai:ri.conicet.gov.ar:11336/12813
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptidesGuo, JitaoNair, Manoj K. M.Galvan, Estela MariaLiu, Shu LinSchifferli, Dieter M.Yersinia PestisMinitransposonPolymyxin BProtamineLl-37https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Bacterial pathogens display a variety of protection mechanisms against the inhibitory and lethal effects of host cationic antimicrobial peptides (CAMPs). To identify Yersinia pestis genes involved in CAMP resistance, libraries of DSY101 (KIM6 caf1 pla psa) minitransposon Tn5AraOut mutants were selected at 37°C for resistance to the model CAMPs polymyxin B or protamine. This approach targeted genes that needed to be repressed (null mutations) or induced (upstream P(BAD) insertions) for the detection of CAMP resistance, and predictably for improved pathogen fitness in mammalian hosts. Ten mutants demonstrated increased resistance to polymyxin B or protamine, with the mapped mutations pointing towards genes suspected to participate in modifying membrane components, genes encoding transport proteins or enzymes, or the regulator of a ferrous iron uptake system (feoC). Not all the mutants were resistant to both CAMPs used for selection. None of the polymyxin B- and only some protamine-resistant mutants, including the feoC mutant, showed increased resistance to rat bronchoalveolar lavage fluid (rBALF) known to contain cathelicidin and β-defensin 1. Thus, findings on bacterial resistance to polymyxin B or protamine don't always apply to CAMPs of the mammalian innate immune system, such as the ones in rBALF.Fil: Guo, Jitao. Peking University Health Science Center. Department of Microbiology; ChinaFil: Nair, Manoj K. M.. University of Pennsylvania. School of Veterinary Medicine; Estados UnidosFil: Galvan, Estela Maria. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. University of Pennsylvania; Estados UnidosFil: Liu, Shu Lin. Peking University Health Science Center. Department of Microbiology; ChinaFil: Schifferli, Dieter M.. University of Pennsylvania. School of Veterinary Medicine; Estados UnidosElsevier2011-05info: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/11336/12813Guo, Jitao; Nair, Manoj K. M.; Galvan, Estela Maria; Liu, Shu Lin; Schifferli, Dieter M.; Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides; Elsevier; Microbial Pathogenesis; 51; 3; 5-2011; 121-1320882-4010enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0882401011000970info:eu-repo/semantics/altIdentifier/doi/10.1016/j.micpath.2011.04.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:10:02Zoai:ri.conicet.gov.ar:11336/12813instacron: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:34982025-09-10 13:10:02.484CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
title Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
spellingShingle Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
Guo, Jitao
Yersinia Pestis
Minitransposon
Polymyxin B
Protamine
Ll-37
title_short Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
title_full Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
title_fullStr Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
title_full_unstemmed Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
title_sort Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides
dc.creator.none.fl_str_mv Guo, Jitao
Nair, Manoj K. M.
Galvan, Estela Maria
Liu, Shu Lin
Schifferli, Dieter M.
author Guo, Jitao
author_facet Guo, Jitao
Nair, Manoj K. M.
Galvan, Estela Maria
Liu, Shu Lin
Schifferli, Dieter M.
author_role author
author2 Nair, Manoj K. M.
Galvan, Estela Maria
Liu, Shu Lin
Schifferli, Dieter M.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Yersinia Pestis
Minitransposon
Polymyxin B
Protamine
Ll-37
topic Yersinia Pestis
Minitransposon
Polymyxin B
Protamine
Ll-37
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Bacterial pathogens display a variety of protection mechanisms against the inhibitory and lethal effects of host cationic antimicrobial peptides (CAMPs). To identify Yersinia pestis genes involved in CAMP resistance, libraries of DSY101 (KIM6 caf1 pla psa) minitransposon Tn5AraOut mutants were selected at 37°C for resistance to the model CAMPs polymyxin B or protamine. This approach targeted genes that needed to be repressed (null mutations) or induced (upstream P(BAD) insertions) for the detection of CAMP resistance, and predictably for improved pathogen fitness in mammalian hosts. Ten mutants demonstrated increased resistance to polymyxin B or protamine, with the mapped mutations pointing towards genes suspected to participate in modifying membrane components, genes encoding transport proteins or enzymes, or the regulator of a ferrous iron uptake system (feoC). Not all the mutants were resistant to both CAMPs used for selection. None of the polymyxin B- and only some protamine-resistant mutants, including the feoC mutant, showed increased resistance to rat bronchoalveolar lavage fluid (rBALF) known to contain cathelicidin and β-defensin 1. Thus, findings on bacterial resistance to polymyxin B or protamine don't always apply to CAMPs of the mammalian innate immune system, such as the ones in rBALF.
Fil: Guo, Jitao. Peking University Health Science Center. Department of Microbiology; China
Fil: Nair, Manoj K. M.. University of Pennsylvania. School of Veterinary Medicine; Estados Unidos
Fil: Galvan, Estela Maria. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. University of Pennsylvania; Estados Unidos
Fil: Liu, Shu Lin. Peking University Health Science Center. Department of Microbiology; China
Fil: Schifferli, Dieter M.. University of Pennsylvania. School of Veterinary Medicine; Estados Unidos
description Bacterial pathogens display a variety of protection mechanisms against the inhibitory and lethal effects of host cationic antimicrobial peptides (CAMPs). To identify Yersinia pestis genes involved in CAMP resistance, libraries of DSY101 (KIM6 caf1 pla psa) minitransposon Tn5AraOut mutants were selected at 37°C for resistance to the model CAMPs polymyxin B or protamine. This approach targeted genes that needed to be repressed (null mutations) or induced (upstream P(BAD) insertions) for the detection of CAMP resistance, and predictably for improved pathogen fitness in mammalian hosts. Ten mutants demonstrated increased resistance to polymyxin B or protamine, with the mapped mutations pointing towards genes suspected to participate in modifying membrane components, genes encoding transport proteins or enzymes, or the regulator of a ferrous iron uptake system (feoC). Not all the mutants were resistant to both CAMPs used for selection. None of the polymyxin B- and only some protamine-resistant mutants, including the feoC mutant, showed increased resistance to rat bronchoalveolar lavage fluid (rBALF) known to contain cathelicidin and β-defensin 1. Thus, findings on bacterial resistance to polymyxin B or protamine don't always apply to CAMPs of the mammalian innate immune system, such as the ones in rBALF.
publishDate 2011
dc.date.none.fl_str_mv 2011-05
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/11336/12813
Guo, Jitao; Nair, Manoj K. M.; Galvan, Estela Maria; Liu, Shu Lin; Schifferli, Dieter M.; Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides; Elsevier; Microbial Pathogenesis; 51; 3; 5-2011; 121-132
0882-4010
url http://hdl.handle.net/11336/12813
identifier_str_mv Guo, Jitao; Nair, Manoj K. M.; Galvan, Estela Maria; Liu, Shu Lin; Schifferli, Dieter M.; Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides; Elsevier; Microbial Pathogenesis; 51; 3; 5-2011; 121-132
0882-4010
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0882401011000970
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.micpath.2011.04.010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 12.993085

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