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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Publicado: 2011
Materias:
LPS
Mus
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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spelling 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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