Proteomic analysis of Escherichia coli with experimentally induced resistance to piperacillin/tazobactam

The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host–pathogen interactions. The aim of th...

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Published in:Research in microbiology Vol. 161; no. 4; pp. 268 - 275
Main Authors: Valéria dos Santos, Kênia, Diniz, Cláudio Galuppo, de Castro Veloso, Luciano, Monteiro de Andrade, Hélida, da Silva Giusta, Mario, da Fonseca Pires, Simone, Santos, Agenor Valadares, Morais Apolônio, Ana Carolina, Roque de Carvalho, Maria Auxiliadora, de Macêdo Farias, Luiz
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Language:English
Published: Issy-les-Moulineaux Elsevier SAS 01-05-2010
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Abstract The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host–pathogen interactions. The aim of the present study was to identify changes in the subproteome of a laboratory-derived piperacillin/tazobactam-resistant strain of Escherichia coli (minimal inhibitory concentration [MIC] = 128 mg/L) as compared with its susceptible wild-type strain E. coli ATCC 25922 (MIC = 2 mg/L) using 2-D fluorescence difference gel electrophoresis (2D-DIGE) followed by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF MS). In the resistant strain, a total of 12 protein species were increased in abundance relative to the wild-type strain, including those related to bacterial virulence, antibiotic resistance and DNA protection during stress. Fourteen proteins were increased in abundance in the wild-type strain compared to the resistant strain, including those involved in glycolysis, protein biosynthesis, pentose-phosphate shunt, amino acid transport, cell division and oxidative stress response. In conclusion, our data show overall changes in the subproteome of the piperacillin/tazobactam-resistant strain, reporting for the first time the potential role of a multidrug efflux pump system in E. coli resistance to piperacillin/tazobactam.
AbstractList The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host–pathogen interactions. The aim of the present study was to identify changes in the subproteome of a laboratory-derived piperacillin/tazobactam-resistant strain of Escherichia coli (minimal inhibitory concentration [MIC] = 128 mg/L) as compared with its susceptible wild-type strain E. coli ATCC 25922 (MIC = 2 mg/L) using 2-D fluorescence difference gel electrophoresis (2D-DIGE) followed by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF MS). In the resistant strain, a total of 12 protein species were increased in abundance relative to the wild-type strain, including those related to bacterial virulence, antibiotic resistance and DNA protection during stress. Fourteen proteins were increased in abundance in the wild-type strain compared to the resistant strain, including those involved in glycolysis, protein biosynthesis, pentose-phosphate shunt, amino acid transport, cell division and oxidative stress response. In conclusion, our data show overall changes in the subproteome of the piperacillin/tazobactam-resistant strain, reporting for the first time the potential role of a multidrug efflux pump system in E. coli resistance to piperacillin/tazobactam.
The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host-pathogen interactions. The aim of the present study was to identify changes in the subproteome of a laboratory-derived piperacillin/tazobactam-resistant strain of Escherichia coli (minimal inhibitory concentration [MIC] = 128 mg/L) as compared with its susceptible wild-type strain E. coli ATCC 25922 (MIC = 2 mg/L) using 2-D fluorescence difference gel electrophoresis (2D-DIGE) followed by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF MS). In the resistant strain, a total of 12 protein species were increased in abundance relative to the wild-type strain, including those related to bacterial virulence, antibiotic resistance and DNA protection during stress. Fourteen proteins were increased in abundance in the wild-type strain compared to the resistant strain, including those involved in glycolysis, protein biosynthesis, pentose-phosphate shunt, amino acid transport, cell division and oxidative stress response. In conclusion, our data show overall changes in the subproteome of the piperacillin/tazobactam-resistant strain, reporting for the first time the potential role of a multidrug efflux pump system in E. coli resistance to piperacillin/tazobactam.
Author Diniz, Cláudio Galuppo
Valéria dos Santos, Kênia
de Macêdo Farias, Luiz
de Castro Veloso, Luciano
da Silva Giusta, Mario
da Fonseca Pires, Simone
Santos, Agenor Valadares
Roque de Carvalho, Maria Auxiliadora
Monteiro de Andrade, Hélida
Morais Apolônio, Ana Carolina
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  givenname: Luciano
  surname: de Castro Veloso
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– sequence: 6
  givenname: Simone
  surname: da Fonseca Pires
  fullname: da Fonseca Pires, Simone
  email: simonefpires@gmail.com
  organization: Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, Belo Horizonte MG, Brazil
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  givenname: Agenor Valadares
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  fullname: Santos, Agenor Valadares
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  givenname: Ana Carolina
  surname: Morais Apolônio
  fullname: Morais Apolônio, Ana Carolina
  email: carolinaapolonio@gmail.com
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  givenname: Maria Auxiliadora
  surname: Roque de Carvalho
  fullname: Roque de Carvalho, Maria Auxiliadora
  email: marc@icb.ufmg.br
  organization: Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Caixa Postal 486, 30.161-970 Belo Horizonte MG, Brazil
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  givenname: Luiz
  surname: de Macêdo Farias
  fullname: de Macêdo Farias, Luiz
  email: macedo@icb.ufmg.br
  organization: Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Caixa Postal 486, 30.161-970 Belo Horizonte MG, Brazil
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Issue 4
Keywords Resistance
2-D DIGE
Comparative proteome
Escherichia coli
Piperacillin/tazobactam
Enzyme
β-Lactams
Enzyme inhibitor
Proteome
β-Lactamase
Induced resistance
Penicillin derivatives
Antibiotic
Tazobactam
Piperacillin
Proteomics
Bacteria
Hydrolases
Antibacterial agent
Enterobacteriaceae
Language English
License CC BY 4.0
(c) 2010 Elsevier Masson SAS. All rights reserved.
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Snippet The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious...
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SubjectTerms 2-D DIGE
Amino acids
Analytical, structural and metabolic biochemistry
Anti-Bacterial Agents - pharmacology
Bacteriology
Biological and medical sciences
Comparative proteome
Drug Resistance, Multiple, Bacterial
Electrophoresis, Gel, Two-Dimensional
Escherichia coli
Escherichia coli - chemistry
Escherichia coli - drug effects
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Mass Spectrometry
Microbiology
Miscellaneous
Molecular Sequence Data
Penicillanic Acid - analogs & derivatives
Penicillanic Acid - pharmacology
Piperacillin - pharmacology
Piperacillin/tazobactam
Proteins
Proteomics
Resistance
Title Proteomic analysis of Escherichia coli with experimentally induced resistance to piperacillin/tazobactam
URI https://dx.doi.org/10.1016/j.resmic.2010.03.006
https://www.ncbi.nlm.nih.gov/pubmed/20381611
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https://search.proquest.com/docview/807259873
Volume 161
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