Quantitative proteomic profiling of the Escherichia coli response to metallic copper surfaces

Renu Nandakumar, Christophe Espirito Santo, Nandakumar Madayiputhiya, Gregor Grass

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Metallic copper surfaces have strong antimicrobial properties and kill bacteria, such as Escherichia coli, within minutes in a process called contact killing. These bacteria are exposed to acute copper stress under dry conditions which is different from chronic copper stress in growing liquid cultures. Currently, the physiological changes of E. coli during the acute contact killing process are largely unknown. Here, a label-free, quantitative proteomic approach was employed to identify the differential proteome profiles of E. coli cells after sub-lethal and lethal exposure to dry metallic copper. Of the 509 proteins identified, 110 proteins were differentially expressed after sub-lethal exposure, whereas 136 proteins had significant differences in their abundance levels after lethal exposure to copper compared to unexposed cells. A total of 210 proteins were identified only in copper-responsive proteomes. Copper surface stress coincided with increased abundance of proteins involved in secondary metabolite biosynthesis, transport and catabolism, including efflux proteins and multidrug resistance proteins. Proteins involved in translation, ribosomal structure and biogenesis functions were down-regulated after contact to metallic copper. The set of changes invoked by copper surface-exposure was diverse without a clear connection to copper ion stress but was different from that caused by exposure to stainless steel. Oxidative posttranslational modifications of proteins were observed in cells exposed to copper but also from stainless steel surfaces. However, proteins from copper stressed cells exhibited a higher degree of oxidative proline and threonine modifications.

Original languageEnglish (US)
Pages (from-to)429-444
Number of pages16
JournalBioMetals
Volume24
Issue number3
DOIs
StatePublished - Jun 1 2011

Fingerprint

Proteomics
proteomics
Escherichia coli
Copper
copper
Proteins
lethal genes
proteins
Stainless Steel
stainless steel
Proteome
proteome
Bacteria
Stainless steel
cells
P-Glycoproteins
multiple drug resistance
Biosynthesis
bacteria
post-translational modification

Keywords

  • Copper surfaces
  • Escherichia coli
  • Posttranslational modification
  • Quantitative proteomics

ASJC Scopus subject areas

  • Biomaterials
  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • Metals and Alloys

Cite this

Quantitative proteomic profiling of the Escherichia coli response to metallic copper surfaces. / Nandakumar, Renu; Santo, Christophe Espirito; Madayiputhiya, Nandakumar; Grass, Gregor.

In: BioMetals, Vol. 24, No. 3, 01.06.2011, p. 429-444.

Research output: Contribution to journalArticle

Nandakumar, Renu ; Santo, Christophe Espirito ; Madayiputhiya, Nandakumar ; Grass, Gregor. / Quantitative proteomic profiling of the Escherichia coli response to metallic copper surfaces. In: BioMetals. 2011 ; Vol. 24, No. 3. pp. 429-444.
@article{274dc26deb0b44cf9914d75277145dc2,
title = "Quantitative proteomic profiling of the Escherichia coli response to metallic copper surfaces",
abstract = "Metallic copper surfaces have strong antimicrobial properties and kill bacteria, such as Escherichia coli, within minutes in a process called contact killing. These bacteria are exposed to acute copper stress under dry conditions which is different from chronic copper stress in growing liquid cultures. Currently, the physiological changes of E. coli during the acute contact killing process are largely unknown. Here, a label-free, quantitative proteomic approach was employed to identify the differential proteome profiles of E. coli cells after sub-lethal and lethal exposure to dry metallic copper. Of the 509 proteins identified, 110 proteins were differentially expressed after sub-lethal exposure, whereas 136 proteins had significant differences in their abundance levels after lethal exposure to copper compared to unexposed cells. A total of 210 proteins were identified only in copper-responsive proteomes. Copper surface stress coincided with increased abundance of proteins involved in secondary metabolite biosynthesis, transport and catabolism, including efflux proteins and multidrug resistance proteins. Proteins involved in translation, ribosomal structure and biogenesis functions were down-regulated after contact to metallic copper. The set of changes invoked by copper surface-exposure was diverse without a clear connection to copper ion stress but was different from that caused by exposure to stainless steel. Oxidative posttranslational modifications of proteins were observed in cells exposed to copper but also from stainless steel surfaces. However, proteins from copper stressed cells exhibited a higher degree of oxidative proline and threonine modifications.",
keywords = "Copper surfaces, Escherichia coli, Posttranslational modification, Quantitative proteomics",
author = "Renu Nandakumar and Santo, {Christophe Espirito} and Nandakumar Madayiputhiya and Gregor Grass",
year = "2011",
month = "6",
day = "1",
doi = "10.1007/s10534-011-9434-5",
language = "English (US)",
volume = "24",
pages = "429--444",
journal = "BioMetals",
issn = "0966-0844",
publisher = "Springer Netherlands",
number = "3",

}

TY - JOUR

T1 - Quantitative proteomic profiling of the Escherichia coli response to metallic copper surfaces

AU - Nandakumar, Renu

AU - Santo, Christophe Espirito

AU - Madayiputhiya, Nandakumar

AU - Grass, Gregor

PY - 2011/6/1

Y1 - 2011/6/1

N2 - Metallic copper surfaces have strong antimicrobial properties and kill bacteria, such as Escherichia coli, within minutes in a process called contact killing. These bacteria are exposed to acute copper stress under dry conditions which is different from chronic copper stress in growing liquid cultures. Currently, the physiological changes of E. coli during the acute contact killing process are largely unknown. Here, a label-free, quantitative proteomic approach was employed to identify the differential proteome profiles of E. coli cells after sub-lethal and lethal exposure to dry metallic copper. Of the 509 proteins identified, 110 proteins were differentially expressed after sub-lethal exposure, whereas 136 proteins had significant differences in their abundance levels after lethal exposure to copper compared to unexposed cells. A total of 210 proteins were identified only in copper-responsive proteomes. Copper surface stress coincided with increased abundance of proteins involved in secondary metabolite biosynthesis, transport and catabolism, including efflux proteins and multidrug resistance proteins. Proteins involved in translation, ribosomal structure and biogenesis functions were down-regulated after contact to metallic copper. The set of changes invoked by copper surface-exposure was diverse without a clear connection to copper ion stress but was different from that caused by exposure to stainless steel. Oxidative posttranslational modifications of proteins were observed in cells exposed to copper but also from stainless steel surfaces. However, proteins from copper stressed cells exhibited a higher degree of oxidative proline and threonine modifications.

AB - Metallic copper surfaces have strong antimicrobial properties and kill bacteria, such as Escherichia coli, within minutes in a process called contact killing. These bacteria are exposed to acute copper stress under dry conditions which is different from chronic copper stress in growing liquid cultures. Currently, the physiological changes of E. coli during the acute contact killing process are largely unknown. Here, a label-free, quantitative proteomic approach was employed to identify the differential proteome profiles of E. coli cells after sub-lethal and lethal exposure to dry metallic copper. Of the 509 proteins identified, 110 proteins were differentially expressed after sub-lethal exposure, whereas 136 proteins had significant differences in their abundance levels after lethal exposure to copper compared to unexposed cells. A total of 210 proteins were identified only in copper-responsive proteomes. Copper surface stress coincided with increased abundance of proteins involved in secondary metabolite biosynthesis, transport and catabolism, including efflux proteins and multidrug resistance proteins. Proteins involved in translation, ribosomal structure and biogenesis functions were down-regulated after contact to metallic copper. The set of changes invoked by copper surface-exposure was diverse without a clear connection to copper ion stress but was different from that caused by exposure to stainless steel. Oxidative posttranslational modifications of proteins were observed in cells exposed to copper but also from stainless steel surfaces. However, proteins from copper stressed cells exhibited a higher degree of oxidative proline and threonine modifications.

KW - Copper surfaces

KW - Escherichia coli

KW - Posttranslational modification

KW - Quantitative proteomics

UR - http://www.scopus.com/inward/record.url?scp=79959928955&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79959928955&partnerID=8YFLogxK

U2 - 10.1007/s10534-011-9434-5

DO - 10.1007/s10534-011-9434-5

M3 - Article

C2 - 21384090

AN - SCOPUS:79959928955

VL - 24

SP - 429

EP - 444

JO - BioMetals

JF - BioMetals

SN - 0966-0844

IS - 3

ER -