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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Autores principales:	Alessandra M Martorana, Sara Motta, Dario Di Silvestre, Federica Falchi, Gianni Dehò, Pierluigi Mauri, Paola Sperandeo, Alessandra Polissi
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/90d253647ad848babbb6bba8a23d1aa3
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spelling	oai:doaj.org-article:90d253647ad848babbb6bba8a23d1aa32021-11-11T08:21:26ZDissecting Escherichia coli outer membrane biogenesis using differential proteomics.1932-620310.1371/journal.pone.0100941https://doaj.org/article/90d253647ad848babbb6bba8a23d1aa32014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24967819/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The 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.Alessandra M MartoranaSara MottaDario Di SilvestreFederica FalchiGianni DehòPierluigi MauriPaola SperandeoAlessandra PolissiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 6, p e100941 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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.
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.
format	article
author	Alessandra M Martorana Sara Motta Dario Di Silvestre Federica Falchi Gianni Dehò Pierluigi Mauri Paola Sperandeo Alessandra Polissi
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)
publishDate	2014
url	https://doaj.org/article/90d253647ad848babbb6bba8a23d1aa3
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Dissecting Escherichia coli outer membrane biogenesis using differential proteomics.

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