A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses
The present authors have previously obtained the Bordetella bronchiseptica mutant BbLP39, which contains a deep-rough lipopolysaccharide (LPS) instead the wild type smooth LPS with O antigen. This mutant was found to be altered in the expression of some proteins and in its ability to colonize mouse...
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2011
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03855600_v55_n12_p847_Sisti http://hdl.handle.net/20.500.12110/paper_03855600_v55_n12_p847_Sisti |
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paper:paper_03855600_v55_n12_p847_Sisti2023-06-08T15:40:51Z A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses Bordetella bronchiseptica Deep rough mutant LPS bacterium lipopolysaccharide interleukin 10 lipid A messenger RNA tumor necrosis factor alpha animal cell animal experiment animal model article bacterial strain Bordetella bronchiseptica Bordetella bronchiseptica infection carbohydrate analysis controlled study female gene expression immune response immunomodulation in vitro study in vivo study lung infection matrix assisted laser desorption ionization time of flight mass spectrometry mouse nonhuman strain difference structure analysis wild type Animals Bordetella bronchiseptica Bordetella Infections Cytokines Female Lipid A Lipopolysaccharides Lung Mice Mice, Inbred BALB C Mice, Inbred C3H Mutation O Antigens Respiratory Tract Infections Toll-Like Receptor 4 Bacteria (microorganisms) Bordetella bronchiseptica Mus The present authors have previously obtained the Bordetella bronchiseptica mutant BbLP39, which contains a deep-rough lipopolysaccharide (LPS) instead the wild type smooth LPS with O antigen. This mutant was found to be altered in the expression of some proteins and in its ability to colonize mouse lungs. Particularly, in BbLP39 the expression of pertactin is decreased. To differentiate the contribution of each bacterial component to the observed phenotype, here mice defective in the LPS sensing receptor TLR4 (TLR4-defective mice) were used. In contrast to wild-type mice, infection of TLR4-defective mice with BbLP39 resulted in lung infection, which persisted for more than 10 days post-challenge. Comparative analysis of the immune responses induced by purified mutant and wild type LPSs showed that the mutant LPS induced significantly higher degrees of expression of TNF-α and IL-10 mRNA than did the wild type. UV matrix-assisted laser desorption/ionization time-of-flight (MALDI TOF) mass spectrometry analysis revealed that both LPSs had the same penta-acylated lipid A structure. However, the lipid A from BbLP39 contained pyrophosphate instead of phosphate at position 1. This structural difference, in addition to the lack of O-antigen in BbLP39, may explain the functional differences between BbLP39 and wild type strains. © 2011 The Societies and Blackwell Publishing Asia Pty Ltd. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03855600_v55_n12_p847_Sisti http://hdl.handle.net/20.500.12110/paper_03855600_v55_n12_p847_Sisti |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Bordetella bronchiseptica Deep rough mutant LPS bacterium lipopolysaccharide interleukin 10 lipid A messenger RNA tumor necrosis factor alpha animal cell animal experiment animal model article bacterial strain Bordetella bronchiseptica Bordetella bronchiseptica infection carbohydrate analysis controlled study female gene expression immune response immunomodulation in vitro study in vivo study lung infection matrix assisted laser desorption ionization time of flight mass spectrometry mouse nonhuman strain difference structure analysis wild type Animals Bordetella bronchiseptica Bordetella Infections Cytokines Female Lipid A Lipopolysaccharides Lung Mice Mice, Inbred BALB C Mice, Inbred C3H Mutation O Antigens Respiratory Tract Infections Toll-Like Receptor 4 Bacteria (microorganisms) Bordetella bronchiseptica Mus |
spellingShingle |
Bordetella bronchiseptica Deep rough mutant LPS bacterium lipopolysaccharide interleukin 10 lipid A messenger RNA tumor necrosis factor alpha animal cell animal experiment animal model article bacterial strain Bordetella bronchiseptica Bordetella bronchiseptica infection carbohydrate analysis controlled study female gene expression immune response immunomodulation in vitro study in vivo study lung infection matrix assisted laser desorption ionization time of flight mass spectrometry mouse nonhuman strain difference structure analysis wild type Animals Bordetella bronchiseptica Bordetella Infections Cytokines Female Lipid A Lipopolysaccharides Lung Mice Mice, Inbred BALB C Mice, Inbred C3H Mutation O Antigens Respiratory Tract Infections Toll-Like Receptor 4 Bacteria (microorganisms) Bordetella bronchiseptica Mus A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses |
topic_facet |
Bordetella bronchiseptica Deep rough mutant LPS bacterium lipopolysaccharide interleukin 10 lipid A messenger RNA tumor necrosis factor alpha animal cell animal experiment animal model article bacterial strain Bordetella bronchiseptica Bordetella bronchiseptica infection carbohydrate analysis controlled study female gene expression immune response immunomodulation in vitro study in vivo study lung infection matrix assisted laser desorption ionization time of flight mass spectrometry mouse nonhuman strain difference structure analysis wild type Animals Bordetella bronchiseptica Bordetella Infections Cytokines Female Lipid A Lipopolysaccharides Lung Mice Mice, Inbred BALB C Mice, Inbred C3H Mutation O Antigens Respiratory Tract Infections Toll-Like Receptor 4 Bacteria (microorganisms) Bordetella bronchiseptica Mus |
description |
The present authors have previously obtained the Bordetella bronchiseptica mutant BbLP39, which contains a deep-rough lipopolysaccharide (LPS) instead the wild type smooth LPS with O antigen. This mutant was found to be altered in the expression of some proteins and in its ability to colonize mouse lungs. Particularly, in BbLP39 the expression of pertactin is decreased. To differentiate the contribution of each bacterial component to the observed phenotype, here mice defective in the LPS sensing receptor TLR4 (TLR4-defective mice) were used. In contrast to wild-type mice, infection of TLR4-defective mice with BbLP39 resulted in lung infection, which persisted for more than 10 days post-challenge. Comparative analysis of the immune responses induced by purified mutant and wild type LPSs showed that the mutant LPS induced significantly higher degrees of expression of TNF-α and IL-10 mRNA than did the wild type. UV matrix-assisted laser desorption/ionization time-of-flight (MALDI TOF) mass spectrometry analysis revealed that both LPSs had the same penta-acylated lipid A structure. However, the lipid A from BbLP39 contained pyrophosphate instead of phosphate at position 1. This structural difference, in addition to the lack of O-antigen in BbLP39, may explain the functional differences between BbLP39 and wild type strains. © 2011 The Societies and Blackwell Publishing Asia Pty Ltd. |
title |
A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses |
title_short |
A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses |
title_full |
A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses |
title_fullStr |
A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses |
title_full_unstemmed |
A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses |
title_sort |
deep rough type structure in bordetella bronchiseptica lipopolysaccharide modulates host immune responses |
publishDate |
2011 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03855600_v55_n12_p847_Sisti http://hdl.handle.net/20.500.12110/paper_03855600_v55_n12_p847_Sisti |
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1768545009813946368 |