Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.

The cell envelope of Gram-negative bacteria is a complex multi-layered structure comprising an inner cytoplasmic membrane and an additional asymmetric lipid bilayer, the outer membrane, which functions as a selective permeability barrier and is essential for viability. Lipopolysaccharide, an essenti...

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Main Authors: Alessandra M Martorana, Sara Motta, Dario Di Silvestre, Federica Falchi, Gianni Dehò, Pierluigi Mauri, Paola Sperandeo, Alessandra Polissi
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24967819/pdf/?tool=EBI
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spelling doaj-90d253647ad848babbb6bba8a23d1aa32021-03-04T09:16:07ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0196e10094110.1371/journal.pone.0100941Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.Alessandra M MartoranaSara MottaDario Di SilvestreFederica FalchiGianni DehòPierluigi MauriPaola SperandeoAlessandra PolissiThe cell envelope of Gram-negative bacteria is a complex multi-layered structure comprising an inner cytoplasmic membrane and an additional asymmetric lipid bilayer, the outer membrane, which functions as a selective permeability barrier and is essential for viability. Lipopolysaccharide, an essential glycolipid located in the outer leaflet of the outer membrane, greatly contributes to the peculiar properties exhibited by the outer membrane. This complex molecule is transported to the cell surface by a molecular machine composed of seven essential proteins LptABCDEFG that form a transenvelope complex and function as a single device. While advances in understanding the mechanisms that govern the biogenesis of the cell envelope have been recently made, only few studies are available on how bacterial cells respond to severe envelope biogenesis defects on a global scale. Here we report the use of differential proteomics based on Multidimensional Protein Identification Technology (MudPIT) to investigate how Escherichia coli cells respond to a block of lipopolysaccharide transport to the outer membrane. We analysed the envelope proteome of a lptC conditional mutant grown under permissive and non permissive conditions and identified 123 proteins whose level is modulated upon LptC depletion. Most such proteins belong to pathways implicated in cell envelope biogenesis, peptidoglycan remodelling, cell division and protein folding. Overall these data contribute to our understanding on how E. coli cells respond to LPS transport defects to restore outer membrane functionality.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24967819/pdf/?tool=EBI
collection DOAJ
language English
format Article
sources DOAJ
author Alessandra M Martorana
Sara Motta
Dario Di Silvestre
Federica Falchi
Gianni Dehò
Pierluigi Mauri
Paola Sperandeo
Alessandra Polissi
spellingShingle Alessandra M Martorana
Sara Motta
Dario Di Silvestre
Federica Falchi
Gianni Dehò
Pierluigi Mauri
Paola Sperandeo
Alessandra Polissi
Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.
PLoS ONE
author_facet Alessandra M Martorana
Sara Motta
Dario Di Silvestre
Federica Falchi
Gianni Dehò
Pierluigi Mauri
Paola Sperandeo
Alessandra Polissi
author_sort Alessandra M Martorana
title Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.
title_short Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.
title_full Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.
title_fullStr Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.
title_full_unstemmed Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.
title_sort dissecting escherichia coli outer membrane biogenesis using differential proteomics.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2014-01-01
description The cell envelope of Gram-negative bacteria is a complex multi-layered structure comprising an inner cytoplasmic membrane and an additional asymmetric lipid bilayer, the outer membrane, which functions as a selective permeability barrier and is essential for viability. Lipopolysaccharide, an essential glycolipid located in the outer leaflet of the outer membrane, greatly contributes to the peculiar properties exhibited by the outer membrane. This complex molecule is transported to the cell surface by a molecular machine composed of seven essential proteins LptABCDEFG that form a transenvelope complex and function as a single device. While advances in understanding the mechanisms that govern the biogenesis of the cell envelope have been recently made, only few studies are available on how bacterial cells respond to severe envelope biogenesis defects on a global scale. Here we report the use of differential proteomics based on Multidimensional Protein Identification Technology (MudPIT) to investigate how Escherichia coli cells respond to a block of lipopolysaccharide transport to the outer membrane. We analysed the envelope proteome of a lptC conditional mutant grown under permissive and non permissive conditions and identified 123 proteins whose level is modulated upon LptC depletion. Most such proteins belong to pathways implicated in cell envelope biogenesis, peptidoglycan remodelling, cell division and protein folding. Overall these data contribute to our understanding on how E. coli cells respond to LPS transport defects to restore outer membrane functionality.
url https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24967819/pdf/?tool=EBI
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