RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella
Brucellaceae are stealthy pathogens with the ability to survive and replicate in the host in the context of a strong immune response. This capacity relies on several virulence factors that are able to modulate the immune system and in their structural components that have low proinflammatory activit...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00221899_v217_n8_p1257_Valguarnera |
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todo:paper_00221899_v217_n8_p1257_Valguarnera2023-10-03T14:28:04Z RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella Valguarnera, E. Spera, J.M. Czibener, C. Fulgenzi, F.R. Casabuono, A.C. Altabe, S.G. Pasquevich, K.A. Guaimas, F. Cassataro, J. Couto, A.S. Ugalde, J.E. Brucella inflammation lipopolysaccharide lipopolysaccharide periplasmic protein RomA protein unclassified drug Alphaproteobacteria animal experiment animal model Article bacterial gene bacterial outer membrane bacterial strain bacterial virulence bacterium adherence biosynthesis Brucella abortus brucellosis carbohydrate analysis carbohydrate synthesis controlled study homeostasis inflammation macromolecule membrane damage mouse mutant nonhuman periplasm phenotype priority journal protein carbohydrate interaction protein determination protein function Brucellaceae are stealthy pathogens with the ability to survive and replicate in the host in the context of a strong immune response. This capacity relies on several virulence factors that are able to modulate the immune system and in their structural components that have low proinflammatory activities. Lipopolysaccharide (LPS), the main component of the outer membrane, is a central virulence factor of Brucella, and it has been well established that it induces a low inflammatory response. We describe here the identification and characterization of a novel periplasmic protein (RomA) conserved in alpha-proteobacteria, which is involved in the homeostasis of the outer membrane. A mutant in this gene showed several phenotypes, such as membrane defects, altered LPS composition, reduced adhesion, and increased virulence and inflammation. We show that RomA is involved in the synthesis of LPS, probably coordinating part of the biosynthetic complex in the periplasm. Its absence alters the normal synthesis of this macromolecule and affects the homeostasis of the outer membrane, resulting in a strain with a hyperinflammatory phenotype. Our results suggest that the proper synthesis of LPS is central to maximize virulence and minimize inflammation. © 2017 The Author(s). JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00221899_v217_n8_p1257_Valguarnera |
| institution |
Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Brucella inflammation lipopolysaccharide lipopolysaccharide periplasmic protein RomA protein unclassified drug Alphaproteobacteria animal experiment animal model Article bacterial gene bacterial outer membrane bacterial strain bacterial virulence bacterium adherence biosynthesis Brucella abortus brucellosis carbohydrate analysis carbohydrate synthesis controlled study homeostasis inflammation macromolecule membrane damage mouse mutant nonhuman periplasm phenotype priority journal protein carbohydrate interaction protein determination protein function |
| spellingShingle |
Brucella inflammation lipopolysaccharide lipopolysaccharide periplasmic protein RomA protein unclassified drug Alphaproteobacteria animal experiment animal model Article bacterial gene bacterial outer membrane bacterial strain bacterial virulence bacterium adherence biosynthesis Brucella abortus brucellosis carbohydrate analysis carbohydrate synthesis controlled study homeostasis inflammation macromolecule membrane damage mouse mutant nonhuman periplasm phenotype priority journal protein carbohydrate interaction protein determination protein function Valguarnera, E. Spera, J.M. Czibener, C. Fulgenzi, F.R. Casabuono, A.C. Altabe, S.G. Pasquevich, K.A. Guaimas, F. Cassataro, J. Couto, A.S. Ugalde, J.E. RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella |
| topic_facet |
Brucella inflammation lipopolysaccharide lipopolysaccharide periplasmic protein RomA protein unclassified drug Alphaproteobacteria animal experiment animal model Article bacterial gene bacterial outer membrane bacterial strain bacterial virulence bacterium adherence biosynthesis Brucella abortus brucellosis carbohydrate analysis carbohydrate synthesis controlled study homeostasis inflammation macromolecule membrane damage mouse mutant nonhuman periplasm phenotype priority journal protein carbohydrate interaction protein determination protein function |
| description |
Brucellaceae are stealthy pathogens with the ability to survive and replicate in the host in the context of a strong immune response. This capacity relies on several virulence factors that are able to modulate the immune system and in their structural components that have low proinflammatory activities. Lipopolysaccharide (LPS), the main component of the outer membrane, is a central virulence factor of Brucella, and it has been well established that it induces a low inflammatory response. We describe here the identification and characterization of a novel periplasmic protein (RomA) conserved in alpha-proteobacteria, which is involved in the homeostasis of the outer membrane. A mutant in this gene showed several phenotypes, such as membrane defects, altered LPS composition, reduced adhesion, and increased virulence and inflammation. We show that RomA is involved in the synthesis of LPS, probably coordinating part of the biosynthetic complex in the periplasm. Its absence alters the normal synthesis of this macromolecule and affects the homeostasis of the outer membrane, resulting in a strain with a hyperinflammatory phenotype. Our results suggest that the proper synthesis of LPS is central to maximize virulence and minimize inflammation. © 2017 The Author(s). |
| format |
JOUR |
| author |
Valguarnera, E. Spera, J.M. Czibener, C. Fulgenzi, F.R. Casabuono, A.C. Altabe, S.G. Pasquevich, K.A. Guaimas, F. Cassataro, J. Couto, A.S. Ugalde, J.E. |
| author_facet |
Valguarnera, E. Spera, J.M. Czibener, C. Fulgenzi, F.R. Casabuono, A.C. Altabe, S.G. Pasquevich, K.A. Guaimas, F. Cassataro, J. Couto, A.S. Ugalde, J.E. |
| author_sort |
Valguarnera, E. |
| title |
RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella |
| title_short |
RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella |
| title_full |
RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella |
| title_fullStr |
RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella |
| title_full_unstemmed |
RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella |
| title_sort |
roma, a periplasmic protein involved in the synthesis of the lipopolysaccharide, tunes down the inflammatory response triggered by brucella |
| url |
http://hdl.handle.net/20.500.12110/paper_00221899_v217_n8_p1257_Valguarnera |
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