Characterization of bacterial DNA binding to human neutrophil surface

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Bacterial DNA activates neutrophils through a CpG- and TLR9-independent mechanism. Neutrophil activation does not require DNA internalization, suggesting that it results from the interaction of bacterial DNA with a neutrophil surface receptor. The aim of this study was to characterize the interactio...

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Autores principales: Fuxman Bass, J.I., Gabelloni, M.L., Alvarez, M.E., Vermeulen, M.E., Russo, D.M., Zorreguieta, Á., Geffner, J.R., Trevani, A.S.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2008
Materias:
Bacterial DNA binding
Biofilm
CpG
Inflammation
Neutrophils
TLR9
bacterial DNA
chemoattractant
deoxyribonuclease
article
biotinylation
cell culture
cell isolation
cell migration
cell surface
controlled study
DNA binding
human
human cell
neutrophil
priority journal
Base Sequence
Biofilms
Cells, Cultured
DNA Primers
DNA, Bacterial
Escherichia coli
Humans
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00236837_v88_n9_p926_FuxmanBass
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling paperaa:paper_00236837_v88_n9_p926_FuxmanBass2023-06-12T16:44:53Z Characterization of bacterial DNA binding to human neutrophil surface Lab. Invest. 2008;88(9):926-937 Fuxman Bass, J.I. Gabelloni, M.L. Alvarez, M.E. Vermeulen, M.E. Russo, D.M. Zorreguieta, Á. Geffner, J.R. Trevani, A.S. Bacterial DNA binding Biofilm CpG Inflammation Neutrophils TLR9 bacterial DNA chemoattractant deoxyribonuclease article biotinylation cell culture cell isolation cell migration cell surface controlled study DNA binding human human cell neutrophil priority journal Base Sequence Biofilms Cells, Cultured DNA Primers DNA, Bacterial Escherichia coli Humans Neutrophils Bacterial DNA activates neutrophils through a CpG- and TLR9-independent mechanism. Neutrophil activation does not require DNA internalization, suggesting that it results from the interaction of bacterial DNA with a neutrophil surface receptor. The aim of this study was to characterize the interaction of bacterial DNA with the neutrophil surface. Bacterial DNA binding showed saturation and was inhibited by unlabeled DNA but not by other polyanions like yeast tRNA and poly-A. Resembling the conditions under which bacterial DNA triggers neutrophil activation, binding was not modified in the presence or absence of calcium, magnesium or serum. Treatment of neutrophils with proteases not only dramatically reduced bacterial DNA binding but also inhibited neutrophil activation induced by bacterial DNA. Experiments performed with DNA samples of different lengths obtained after digestion of bacterial DNA with DNase showed that only DNA fragments greater than ≈170-180 nucleotides competed bacterial DNA binding and retained the ability to trigger cell activation. Treatment of neutrophils with chemoattractants or conventional agonists significantly increased bacterial DNA binding. Moreover, neutrophils that underwent transmigration through human endothelial cell monolayers even in the absence of chemoattractants, exhibited higher binding levels of bacterial DNA. Together, our findings provide evidence that binding of bacterial DNA to neutrophils is a receptor-mediated process that conditions the ability of DNA to trigger cell activation. We speculate that neutrophil recognition of bacterial DNA might be modulated by the balance of agonists present at inflammatory foci. This effect might be relevant in bacterial infections with a biofilm etiology, in which extracellular DNA could function as a potent neutrophil agonist. © 2008 USCAP, Inc All rights reserved. Fil:Fuxman Bass, J.I. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gabelloni, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vermeulen, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Russo, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Zorreguieta, Á. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Trevani, A.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2008 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00236837_v88_n9_p926_FuxmanBass
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language Inglés
orig_language_str_mv eng
topic Bacterial DNA binding
Biofilm
CpG
Inflammation
Neutrophils
TLR9
bacterial DNA
chemoattractant
deoxyribonuclease
article
biotinylation
cell culture
cell isolation
cell migration
cell surface
controlled study
DNA binding
human
human cell
neutrophil
priority journal
Base Sequence
Biofilms
Cells, Cultured
DNA Primers
DNA, Bacterial
Escherichia coli
Humans
Neutrophils
spellingShingle Bacterial DNA binding
Biofilm
CpG
Inflammation
Neutrophils
TLR9
bacterial DNA
chemoattractant
deoxyribonuclease
article
biotinylation
cell culture
cell isolation
cell migration
cell surface
controlled study
DNA binding
human
human cell
neutrophil
priority journal
Base Sequence
Biofilms
Cells, Cultured
DNA Primers
DNA, Bacterial
Escherichia coli
Humans
Neutrophils
Fuxman Bass, J.I.
Gabelloni, M.L.
Alvarez, M.E.
Vermeulen, M.E.
Russo, D.M.
Zorreguieta, Á.
Geffner, J.R.
Trevani, A.S.
Characterization of bacterial DNA binding to human neutrophil surface
topic_facet Bacterial DNA binding
Biofilm
CpG
Inflammation
Neutrophils
TLR9
bacterial DNA
chemoattractant
deoxyribonuclease
article
biotinylation
cell culture
cell isolation
cell migration
cell surface
controlled study
DNA binding
human
human cell
neutrophil
priority journal
Base Sequence
Biofilms
Cells, Cultured
DNA Primers
DNA, Bacterial
Escherichia coli
Humans
Neutrophils
description Bacterial DNA activates neutrophils through a CpG- and TLR9-independent mechanism. Neutrophil activation does not require DNA internalization, suggesting that it results from the interaction of bacterial DNA with a neutrophil surface receptor. The aim of this study was to characterize the interaction of bacterial DNA with the neutrophil surface. Bacterial DNA binding showed saturation and was inhibited by unlabeled DNA but not by other polyanions like yeast tRNA and poly-A. Resembling the conditions under which bacterial DNA triggers neutrophil activation, binding was not modified in the presence or absence of calcium, magnesium or serum. Treatment of neutrophils with proteases not only dramatically reduced bacterial DNA binding but also inhibited neutrophil activation induced by bacterial DNA. Experiments performed with DNA samples of different lengths obtained after digestion of bacterial DNA with DNase showed that only DNA fragments greater than ≈170-180 nucleotides competed bacterial DNA binding and retained the ability to trigger cell activation. Treatment of neutrophils with chemoattractants or conventional agonists significantly increased bacterial DNA binding. Moreover, neutrophils that underwent transmigration through human endothelial cell monolayers even in the absence of chemoattractants, exhibited higher binding levels of bacterial DNA. Together, our findings provide evidence that binding of bacterial DNA to neutrophils is a receptor-mediated process that conditions the ability of DNA to trigger cell activation. We speculate that neutrophil recognition of bacterial DNA might be modulated by the balance of agonists present at inflammatory foci. This effect might be relevant in bacterial infections with a biofilm etiology, in which extracellular DNA could function as a potent neutrophil agonist. © 2008 USCAP, Inc All rights reserved.
format Artículo
Artículo
publishedVersion
author Fuxman Bass, J.I.
Gabelloni, M.L.
Alvarez, M.E.
Vermeulen, M.E.
Russo, D.M.
Zorreguieta, Á.
Geffner, J.R.
Trevani, A.S.
author_facet Fuxman Bass, J.I.
Gabelloni, M.L.
Alvarez, M.E.
Vermeulen, M.E.
Russo, D.M.
Zorreguieta, Á.
Geffner, J.R.
Trevani, A.S.
author_sort Fuxman Bass, J.I.
title Characterization of bacterial DNA binding to human neutrophil surface
title_short Characterization of bacterial DNA binding to human neutrophil surface
title_full Characterization of bacterial DNA binding to human neutrophil surface
title_fullStr Characterization of bacterial DNA binding to human neutrophil surface
title_full_unstemmed Characterization of bacterial DNA binding to human neutrophil surface
title_sort characterization of bacterial dna binding to human neutrophil surface
publishDate 2008
url http://hdl.handle.net/20.500.12110/paper_00236837_v88_n9_p926_FuxmanBass
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AT zorreguietaa characterizationofbacterialdnabindingtohumanneutrophilsurface
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